{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,20]],"date-time":"2026-10-20T21:45:32Z","timestamp":1792532732922,"version":"4.5.0"},"reference-count":326,"publisher":"Frontiers Media SA","license":[{"start":{"date-parts":[[2023,1,19]],"date-time":"2023-01-19T00:00:00Z","timestamp":1674086400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":["frontiersin.org"],"crossmark-restriction":true},"short-container-title":["Front. Immunol."],"abstract":"<jats:p>Matrix metalloproteinases (MMPs) are an important class of enzymes in the body that function through the extracellular matrix (ECM). They are involved in diverse pathophysiological processes, such as tumor invasion and metastasis, cardiovascular diseases, arthritis, periodontal disease, osteogenesis imperfecta, and diseases of the central nervous system. MMPs participate in the occurrence and development of numerous cancers and are closely related to immunity. In the present study, we review the immunomodulatory role of MMPs in colitis-associated cancer (CAC) and discuss relevant clinical applications. We analyze more than 300 pharmacological studies retrieved from PubMed and the Web of Science, related to MMPs, cancer, colitis, CAC, and immunomodulation. Key MMPs that interfere with pathological processes in CAC such as MMP-2, MMP-3, MMP-7, MMP-9, MMP-10, MMP-12, and MMP-13, as well as their corresponding mechanisms are elaborated. MMPs are involved in cell proliferation, cell differentiation, angiogenesis, ECM remodeling, and the inflammatory response in CAC. They also affect the immune system by modulating differentiation and immune activity of immune cells, recruitment of macrophages, and recruitment of neutrophils. Herein we describe the immunomodulatory role of MMPs in CAC to facilitate treatment of this special type of colon cancer, which is preceded by detectable inflammatory bowel disease in clinical populations.<\/jats:p>","DOI":"10.3389\/fimmu.2022.1093990","type":"journal-article","created":{"date-parts":[[2023,1,20]],"date-time":"2023-01-20T09:47:54Z","timestamp":1674208074000},"update-policy":"https:\/\/doi.org\/10.3389\/crossmark-policy","source":"Crossref","is-referenced-by-count":127,"title":["The immunomodulatory role of matrix metalloproteinases in colitis-associated cancer"],"prefix":"10.3389","volume":"13","author":[{"given":"Luying","family":"He","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Qianming","family":"Kang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ka Iong","family":"Chan","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yang","family":"Zhang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Zhangfeng","family":"Zhong","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Wen","family":"Tan","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1965","published-online":{"date-parts":[[2023,1,19]]},"reference":[{"key":"B1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.48.6.1014","article-title":"Collagenolytic activity in amphibian tissues: A tissue culture assay","volume":"48","author":"Gross","year":"1962","journal-title":"Proc Natl Acad Sci U.S.A."},{"key":"B2","doi-asserted-by":"publisher","DOI":"10.1128\/iai.65.4.1431-1439.1997","article-title":"The bacteroides fragilis toxin fragilysin disrupts the paracellular barrier of epithelial cells","volume":"65","author":"Obiso","year":"1997","journal-title":"Infect Immun"},{"key":"B3","doi-asserted-by":"publisher","DOI":"10.1067\/mva.2001.119503","article-title":"Role of matrix metalloproteinases 1, 2, and 9 and tissue inhibitor of matrix metalloproteinase-1 in chronic venous insufficiency","volume":"34","author":"Saito","year":"2001","journal-title":"J Vasc Surg"},{"key":"B4","doi-asserted-by":"publisher","first-page":"241","DOI":"10.1016\/bs.apha.2017.08.002","article-title":"Matrix metalloproteinases, vascular remodeling, and vascular disease","volume":"81","author":"Wang","year":"2018","journal-title":"Adv Pharmacol"},{"key":"B5","doi-asserted-by":"publisher","DOI":"10.3390\/ijms20123077","article-title":"Post-translational modification-dependent activity of matrix metalloproteinases","volume":"20","author":"Madzharova","year":"2019","journal-title":"Int J Mol Sci"},{"key":"B6","doi-asserted-by":"publisher","DOI":"10.1016\/j.ceb.2004.07.010","article-title":"Regulation of matrix biology by matrix metalloproteinases","volume":"16","author":"Mott","year":"2004","journal-title":"Curr Opin Cell Biol"},{"key":"B7","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1007\/978-3-0348-0364-9_1","article-title":"Matrix metalloproteinases","volume":"103","author":"Vargov\u00e1","year":"2012","journal-title":"Exp Suppl"},{"key":"B8","doi-asserted-by":"publisher","DOI":"10.1016\/j.biocel.2007.12.006","article-title":"The regulation of matrix metalloproteinases and their inhibitors","volume":"40","author":"Clark","year":"2008","journal-title":"Int J Biochem Cell Biol"},{"key":"B9","doi-asserted-by":"publisher","first-page":"463","DOI":"10.1146\/annurev.cellbio.17.1.463","article-title":"How matrix metalloproteinases regulate cell behavior","volume":"17","author":"Sternlicht","year":"2001","journal-title":"Annu Rev Cell Dev Biol"},{"key":"B10","doi-asserted-by":"publisher","DOI":"10.1038\/nrc745","article-title":"New functions for the matrix metalloproteinases in cancer progression","volume":"2","author":"Egeblad","year":"2002","journal-title":"Nat Rev Cancer"},{"key":"B11","doi-asserted-by":"publisher","DOI":"10.1021\/bi00499a008","article-title":"Characterization of 58-kilodalton human neutrophil collagenase: Comparison with human fibroblast collagenase","volume":"29","author":"Mallya","year":"1990","journal-title":"Biochemistry"},{"key":"B12","doi-asserted-by":"publisher","DOI":"10.1038\/6657","article-title":"Crystal structures of MMP-1 and -13 reveal the structural basis for selectivity of collagenase inhibitors","volume":"6","author":"Lovejoy","year":"1999","journal-title":"Nat Struct Biol"},{"key":"B13","doi-asserted-by":"publisher","DOI":"10.1016\/S0022-5193(05)80617-4","article-title":"Domain structure of human 72-kDa gelatinase\/type IV collagenase. Characterization of proteolytic activity and identification of the tissue inhibitor of metalloproteinase-2 (TIMP-2) binding regions","volume":"267","author":"Fridman","year":"1992","journal-title":"J Biol Chem"},{"key":"B14","doi-asserted-by":"publisher","DOI":"10.1021\/bi015930p","article-title":"Identification of the active site of gelatinase B as the structural element sufficient for converting a protein to a metalloprotease","volume":"41","author":"Kaur","year":"2002","journal-title":"Biochemistry"},{"key":"B15","doi-asserted-by":"publisher","DOI":"10.1002\/pro.5560041002","article-title":"Stromelysin-1: Three-dimensional structure of the inhibited catalytic domain and of the c-truncated proenzyme","volume":"4","author":"Becker","year":"1995","journal-title":"Protein Sci"},{"key":"B16","doi-asserted-by":"publisher","DOI":"10.1110\/ps.8.7.1455","article-title":"X-Ray structure of human stromelysin catalytic domain complexed with nonpeptide inhibitors: Implications for inhibitor selectivity","volume":"8","author":"Pavlovsky","year":"1999","journal-title":"Protein Sci"},{"key":"B17","doi-asserted-by":"publisher","DOI":"10.1042\/BST0350689","article-title":"Matrix metalloproteinases: Useful and deleterious","volume":"35","author":"Ganea","year":"2007","journal-title":"Biochem Soc Trans"},{"key":"B18","doi-asserted-by":"publisher","DOI":"10.1093\/emboj\/17.17.5238","article-title":"Crystal structure of the complex formed by the membrane type 1-matrix metalloproteinase with the tissue inhibitor of metalloproteinases-2, the soluble progelatinase a receptor","volume":"17","author":"Fernandez-Catalan","year":"1998","journal-title":"EMBO J"},{"key":"B19","doi-asserted-by":"publisher","DOI":"10.3390\/ijms17060868","article-title":"Role of matrix metalloproteinases in photoaging and photocarcinogenesis","volume":"17","author":"PittaYAPruek","year":"2016","journal-title":"Int J Mol Sci"},{"key":"B20","doi-asserted-by":"publisher","first-page":"119","DOI":"10.1016\/j.mam.2011.10.015","article-title":"Human matrix metalloproteinases: An ubiquitarian class of enzymes involved in several pathological processes","volume":"33","author":"Sbardella","year":"2012","journal-title":"Mol Aspects Med"},{"key":"B21","doi-asserted-by":"publisher","DOI":"10.1161\/01.RES.0000070112.80711.3D","article-title":"Matrix metalloproteinases and tissue inhibitors of metalloproteinases: Structure, function, and biochemistry","volume":"92","author":"Visse","year":"2003","journal-title":"Circ Res"},{"key":"B22","doi-asserted-by":"publisher","first-page":"87","DOI":"10.1016\/s0378-1119(01)00360-2","article-title":"MMP-28, a new human matrix metalloproteinase with an unusual cysteine-switch sequence is widely expressed in tumors","volume":"265","author":"Marchenko","year":"2001","journal-title":"Gene"},{"key":"B23","doi-asserted-by":"publisher","DOI":"10.1038\/nrm763","article-title":"Matrix metalloproteinases: A tail of a frog that became a prince","volume":"3","author":"Brinckerhoff","year":"2002","journal-title":"Nat Rev Mol Cell Biol"},{"key":"B24","doi-asserted-by":"publisher","first-page":"75","DOI":"10.1080\/17460441.2020.1819235","article-title":"Challenges with matrix metalloproteinase inhibition and future drug discovery avenues","volume":"16","author":"Fischer","year":"2021","journal-title":"Expert Opin Drug Discovery"},{"key":"B25","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.274.31.21491","article-title":"Matrix metalloproteinases","volume":"274","author":"Nagase","year":"1999","journal-title":"J Biol Chem"},{"key":"B26","doi-asserted-by":"publisher","DOI":"10.1016\/bs.pmbts.2017.01.002","article-title":"Matrix metalloproteinases and platelet function","volume":"147","author":"Gresele","year":"2017","journal-title":"Prog Mol Biol Transl Sci"},{"key":"B27","doi-asserted-by":"publisher","DOI":"10.1002\/jcp.21208","article-title":"Signal transduction and cell-type specific regulation of matrix metalloproteinase gene expression: Can MMPs be good for you","volume":"213","author":"Vincenti","year":"2007","journal-title":"J Cell Physiol"},{"key":"B28","doi-asserted-by":"publisher","DOI":"10.1158\/0008-5472.CAN-08-0955","article-title":"Steroid receptor coactivator-3\/AIB1 promotes cell migration and invasiveness through focal adhesion turnover and matrix metalloproteinase expression","volume":"68","author":"Yan","year":"2008","journal-title":"Cancer Res"},{"key":"B29","doi-asserted-by":"publisher","DOI":"10.1016\/j.bbamcr.2009.04.003","article-title":"Matrix metalloproteinases: Fold and function of their catalytic domains","volume":"1803","author":"Tallant","year":"2010","journal-title":"Biochim Biophys Acta"},{"key":"B30","doi-asserted-by":"publisher","DOI":"10.1038\/sj.onc.1201111","article-title":"Differential regulation of interstitial collagenase (MMP-1) gene expression by ETS transcription factors","volume":"14","author":"Westermarck","year":"1997","journal-title":"Oncogene"},{"key":"B31","doi-asserted-by":"publisher","DOI":"10.1186\/ar401","article-title":"Transcriptional regulation of collagenase (MMP-1, MMP-13) genes in arthritis: Integration of complex signaling pathways for the recruitment of gene-specific transcription factors","volume":"4","author":"Vincenti","year":"2002","journal-title":"Arthritis Res"},{"key":"B32","doi-asserted-by":"publisher","DOI":"10.2353\/ajpath.2008.071009","article-title":"L-arginine decreases inflammation and modulates the nuclear factor-\u03baB\/Matrix metalloproteinase cascade in Mdx muscle fibers","volume":"172","author":"Hnia","year":"2008","journal-title":"Am J Pathol"},{"key":"B33","doi-asserted-by":"publisher","DOI":"10.1158\/0008-5472.CAN-07-2803","article-title":"Down-regulation of platelet-derived growth factor-D inhibits cell growth and angiogenesis through inactivation of notch-1 and nuclear factor-\u03baB signaling","volume":"67","author":"Wang","year":"2007","journal-title":"Cancer Res"},{"key":"B34","doi-asserted-by":"publisher","DOI":"10.1016\/j.semcancer.2017.11.008","article-title":"Matrix metalloproteinases: A challenging paradigm of cancer management","volume":"56","author":"Alaseem","year":"2019","journal-title":"Semin Cancer Biol"},{"key":"B35","doi-asserted-by":"publisher","first-page":"397","DOI":"10.3892\/ijo.2021.5173","article-title":"Inhibition of the invasion and metastasis of mammary carcinoma cells by NBD peptide targeting S100A4 via the suppression of the Sp1\/MMP-14 axis","volume":"58","author":"Takenaga","year":"2021","journal-title":"Int J Oncol"},{"key":"B36","doi-asserted-by":"publisher","first-page":"19","DOI":"10.1002\/jcp.20948","article-title":"Regulation of matrix metalloproteinase gene expression","volume":"211","author":"Yan","year":"2007","journal-title":"J Cell Physiol"},{"key":"B37","doi-asserted-by":"publisher","DOI":"10.1021\/bi00232a039","article-title":"The AP-1 sequence is necessary but not sufficient for phorbol induction of collagenase in fibroblasts","volume":"30","author":"Auble","year":"1991","journal-title":"Biochemistry"},{"key":"B38","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.273.9.5279","article-title":"Central role of Ferrous\/Ferric iron in the ultraviolet B irradiation-mediated signaling pathway leading to increased interstitial collagenase (Matrix-degrading metalloprotease (MMP)-1) and stromelysin-1 (MMP-3) mRNA levels in cultured human dermal fibroblasts","volume":"273","author":"Brenneisen","year":"1998","journal-title":"J Biol Chem"},{"key":"B39","doi-asserted-by":"publisher","DOI":"10.1038\/379335a0","article-title":"Molecular basis of sun-induced premature skin ageing and retinoid antagonism","volume":"379","author":"Fisher","year":"1996","journal-title":"Nature"},{"key":"B40","doi-asserted-by":"publisher","first-page":"27","DOI":"10.1023\/a:1026404227624","article-title":"Transforming growth factor Beta1 acts as an inducer of matrix metalloproteinase expression and activity in human bone-metastasizing cancer cells","volume":"17","author":"Duivenvoorden","year":"1999","journal-title":"Clin Exp Metastasis"},{"key":"B41","doi-asserted-by":"publisher","first-page":"57","DOI":"10.1016\/s0378-1119(98)00076-6","article-title":"Cloning of three caenorhabditis elegans genes potentially encoding novel matrix metalloproteinases","volume":"211","author":"Wada","year":"1998","journal-title":"Gene"},{"key":"B42","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.272.2.1188","article-title":"The mitogen-activated protein kinase and JAK-STAT signaling pathways are required for an oncostatin M-responsive element-mediated activation of matrix metalloproteinase 1 gene expression","volume":"272","author":"Korzus","year":"1997","journal-title":"J Biol Chem"},{"key":"B43","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.273.9.5137","article-title":"Enhancement of fibroblast collagenase (Matrix metalloproteinase-1) gene expression by ceramide is mediated by extracellular signal-regulated and stress-activated protein kinase pathways","volume":"273","author":"Reunanen","year":"1998","journal-title":"J Biol Chem"},{"key":"B44","doi-asserted-by":"publisher","DOI":"10.1016\/s0955-0674(96)80061-5","article-title":"Signal transduction through lipid second messengers","volume":"8","author":"Spiegel","year":"1996","journal-title":"Curr Opin Cell Biol"},{"key":"B45","doi-asserted-by":"publisher","DOI":"10.2174\/092986710793213724","article-title":"Matrix metalloproteinases","volume":"17","author":"Zitka","year":"2010","journal-title":"Curr Med Chem"},{"key":"B46","doi-asserted-by":"publisher","first-page":"25","DOI":"10.1007\/s10549-014-2989-4","article-title":"Hypomethylation of the MMP-7 promoter and increased expression of MMP-7 distinguishes the basal-like breast cancer subtype from other triple-negative tumors","volume":"146","author":"Sizemore","year":"2014","journal-title":"Breast Cancer Res Treat"},{"key":"B47","doi-asserted-by":"publisher","DOI":"10.1016\/S0006-291X(02)02283-0","article-title":"Evidence for the role of promoter methylation in the regulation of MMP-9 gene expression","volume":"297","author":"Chicoine","year":"2002","journal-title":"Biochem Biophys Res Commun"},{"key":"B48","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.87.1.364","article-title":"Multiple modes of activation of latent human fibroblast collagenase: Evidence for the role of a Cys73 active-site zinc complex in latency and a \"Cysteine switch\" mechanism for activation","volume":"87","author":"Springman","year":"1990","journal-title":"Proc Natl Acad Sci U.S.A."},{"key":"B49","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.87.14.5578","article-title":"The cysteine switch: A principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene family","volume":"87","author":"Van Wart","year":"1990","journal-title":"Proc Natl Acad Sci U.S.A."},{"key":"B50","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M109.033472","article-title":"Neutrophil MMP-9 proenzyme, unencumbered by TIMP-1, undergoes efficient activation in vivo and catalytically induces angiogenesis via a basic fibroblast growth factor (FGF-2)\/FGFR-2 pathway","volume":"284","author":"Ardi","year":"2009","journal-title":"J Biol Chem"},{"key":"B51","doi-asserted-by":"publisher","DOI":"10.1126\/scisignal.127re6","article-title":"Tissue inhibitors of metalloproteinases in cell signaling: Metalloproteinase-independent biological activities","volume":"1","author":"Stetler-Stevenson","year":"2008","journal-title":"Sci Signal"},{"key":"B52","doi-asserted-by":"publisher","first-page":"799","DOI":"10.1055\/s-0037-1614573","article-title":"Temporal and topographic matrix metalloproteinase expression after vascular injury in mice","volume":"81","author":"Lijnen","year":"1999","journal-title":"Thromb Haemost"},{"key":"B53","doi-asserted-by":"publisher","DOI":"10.1038\/nri3499","article-title":"Metalloproteinases and their natural inhibitors in inflammation and immunity","volume":"13","author":"Khokha","year":"2013","journal-title":"Nat Rev Immunol"},{"key":"B54","doi-asserted-by":"publisher","first-page":"99","DOI":"10.1056\/NEJM194907212410305","article-title":"Active immunization","volume":"241","author":"Edsall","year":"1949","journal-title":"N Engl J Med"},{"key":"B55","doi-asserted-by":"publisher","DOI":"10.1016\/j.pcl.2019.06.011","article-title":"Innate immunity","volume":"66","author":"Kaur","year":"2019","journal-title":"Pediatr Clin North Am"},{"key":"B56","doi-asserted-by":"publisher","DOI":"10.1016\/j.redox.2020.101759","article-title":"Innate-adaptive immunity interplay and redox regulation in immune response","volume":"37","author":"Sun","year":"2020","journal-title":"Redox Biol"},{"key":"B57","doi-asserted-by":"publisher","DOI":"10.1016\/j.intimp.2021.107823","article-title":"Anti-inflammatory and M2 macrophage polarization-promoting effect of mesenchymal stem cell-derived exosomes","volume":"97","author":"Arabpour","year":"2021","journal-title":"Int Immunopharmacol"},{"key":"B58","doi-asserted-by":"publisher","DOI":"10.1007\/978-1-4939-1115-8_1","article-title":"A brief outline of the immune system","volume":"1184","author":"Tomar","year":"2014","journal-title":"Methods Mol Biol"},{"key":"B59","doi-asserted-by":"publisher","DOI":"10.1038\/nri2711","article-title":"The regulation of IL-10 production by immune cells","volume":"10","author":"Saraiva","year":"2010","journal-title":"Nat Rev Immunol"},{"key":"B60","doi-asserted-by":"publisher","DOI":"10.1152\/physrev.00012.2018","article-title":"The neutrophil's role during health and disease","volume":"99","author":"Liew","year":"2019","journal-title":"Physiol Rev"},{"key":"B61","doi-asserted-by":"publisher","DOI":"10.1016\/j.cyto.2017.10.001","article-title":"T-Cells and their cytokine production: The anti-inflammatory and immunosuppressive effects of strenuous exercise","volume":"104","author":"Shaw","year":"2018","journal-title":"Cytokine"},{"key":"B62","doi-asserted-by":"publisher","DOI":"10.3390\/cells10020304","article-title":"Mapping the metabolic networks of tumor cells and cancer-associated fibroblasts","volume":"10","author":"Karta","year":"2021","journal-title":"Cells"},{"key":"B63","doi-asserted-by":"publisher","DOI":"10.1111\/pin.13033","article-title":"Stromal metalloproteinases: Crucial contributors to the tumor microenvironment","volume":"71","author":"Shimoda","year":"2021","journal-title":"Pathol Int"},{"key":"B64","doi-asserted-by":"publisher","DOI":"10.4049\/jimmunol.1102199","article-title":"Stromal TIMP3 regulates liver lymphocyte populations and provides protection against Th1 T cell-driven autoimmune hepatitis","volume":"188","author":"Murthy","year":"2012","journal-title":"J Immunol"},{"key":"B65","doi-asserted-by":"publisher","DOI":"10.1111\/j.1432-1033.1991.tb16027.x","article-title":"Purification and identification of 91-kDa neutrophil gelatinase. release by the activating peptide interleukin-8","volume":"198","author":"Masure","year":"1991","journal-title":"Eur J Biochem"},{"key":"B66","doi-asserted-by":"publisher","DOI":"10.1189\/jlb.69.6.851","article-title":"Gelatinase B functions as regulator and effector in leukocyte biology","volume":"69","author":"Opdenakker","year":"2001","journal-title":"J Leukoc Biol"},{"key":"B67","doi-asserted-by":"publisher","DOI":"10.1093\/brain\/awg285","article-title":"Analyses of all matrix metalloproteinase members in leukocytes emphasize monocytes as major inflammatory mediators in multiple sclerosis","volume":"126","author":"Bar-Or","year":"2003","journal-title":"Brain"},{"key":"B68","doi-asserted-by":"publisher","first-page":"78","DOI":"10.1016\/j.cyto.2010.03.003","article-title":"Lymphotoxin-alphabeta heterotrimers are cleaved by metalloproteinases and contribute to synovitis in rheumatoid arthritis","volume":"51","author":"Young","year":"2010","journal-title":"Cytokine"},{"key":"B69","doi-asserted-by":"publisher","DOI":"10.1038\/nri3193","article-title":"Fine-tuning of dendritic cell biology by the TNF superfamily","volume":"12","author":"Summers deLuca","year":"2012","journal-title":"Nat Rev Immunol"},{"key":"B70","doi-asserted-by":"publisher","DOI":"10.1016\/j.ccr.2011.01.037","article-title":"Matrix metalloproteinase-2 conditions human dendritic cells to prime inflammatory T(H)2 cells via an IL-12- and OX40L-dependent pathway","volume":"19","author":"Godefroy","year":"2011","journal-title":"Cancer Cell"},{"key":"B71","doi-asserted-by":"publisher","DOI":"10.1016\/s0092-8674(02)01079-6","article-title":"Matrilysin shedding of syndecan-1 regulates chemokine mobilization and transepithelial efflux of neutrophils in acute lung injury","volume":"111","author":"Li","year":"2002","journal-title":"Cell"},{"key":"B72","doi-asserted-by":"publisher","DOI":"10.1038\/ng1249","article-title":"Loss of collagenase-2 confers increased skin tumor susceptibility to Male mice","volume":"35","author":"Balb\u00edn","year":"2003","journal-title":"Nat Genet"},{"key":"B73","doi-asserted-by":"publisher","DOI":"10.1038\/ng.340","article-title":"Analysis of the matrix metalloproteinase family reveals that MMP8 is often mutated in melanoma","volume":"41","author":"Palavalli","year":"2009","journal-title":"Nat Genet"},{"key":"B74","doi-asserted-by":"publisher","first-page":"e312","DOI":"10.1371\/journal.pone.0000312","article-title":"Lps responsiveness and neutrophil chemotaxis in vivo require PMN MMP-8 activity","volume":"2","author":"Tester","year":"2007","journal-title":"PLos One"},{"key":"B75","doi-asserted-by":"publisher","DOI":"10.1182\/blood.V96.8.2673","article-title":"Neutrophil gelatinase B potentiates interleukin-8 tenfold by aminoterminal processing, whereas it degrades CTAP-III, PF-4, and GRO-alpha and leaves RANTES and MCP-2 intact","volume":"96","author":"Van den Steen","year":"2000","journal-title":"Blood"},{"key":"B76","doi-asserted-by":"publisher","first-page":"52","DOI":"10.1016\/j.cell.2010.03.015","article-title":"Matrix metalloproteinases: Regulators of the tumor microenvironment","volume":"141","author":"Kessenbrock","year":"2010","journal-title":"Cell"},{"key":"B77","doi-asserted-by":"publisher","DOI":"10.1128\/microbiolspec.MCHD-0002-2015","article-title":"Metalloproteinases: A functional pathway for myeloid cells","volume":"4","author":"Chou","year":"2016","journal-title":"Microbiol Spectr"},{"key":"B78","doi-asserted-by":"publisher","DOI":"10.4049\/jimmunol.1202286","article-title":"In vivo processing of CXCL5 (LIX) by matrix metalloproteinase (MMP)-2 and MMP-9 promotes early neutrophil recruitment in IL-1\u03b2-induced peritonitis","volume":"190","author":"Song","year":"2013","journal-title":"J Immunol"},{"key":"B79","doi-asserted-by":"publisher","DOI":"10.1016\/j.febslet.2012.10.033","article-title":"Meprins process matrix metalloproteinase-9 (MMP-9)\/gelatinase B and enhance the activation kinetics by MMP-3","volume":"586","author":"Geurts","year":"2012","journal-title":"FEBS Lett"},{"key":"B80","doi-asserted-by":"publisher","DOI":"10.1126\/science.289.5482.1202","article-title":"Inflammation dampened by gelatinase a cleavage of monocyte chemoattractant protein-3","volume":"289","author":"McQuibban","year":"2000","journal-title":"Science"},{"key":"B81","doi-asserted-by":"publisher","DOI":"10.1002\/(SICI)1097-4644(19980701)70:1<121::AID-JCB12>3.0.CO;2-S","article-title":"Gene expression of monocyte chemoattractant protein-1 in giant cell tumors of bone osteoclastoma: Possible involvement in CD68+ macrophage-like cell migration","volume":"70","author":"Zheng","year":"1998","journal-title":"J Cell Biochem"},{"key":"B82","doi-asserted-by":"publisher","DOI":"10.3390\/genes13050756","article-title":"Macrophage polarization in atherosclerosis","volume":"13","author":"Eshghjoo","year":"2022","journal-title":"Genes"},{"key":"B83","doi-asserted-by":"publisher","DOI":"10.3389\/fcimb.2020.00287","article-title":"Regulations of glycolytic activities on macrophages functions in tumor and infectious inflammation","volume":"10","author":"Yu","year":"2020","journal-title":"Front Cell Infection Microbiol"},{"key":"B84","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0198464","article-title":"Impact of MMP-2 and MMP-9 enzyme activity on wound healing, tumor growth and RACPP cleavage","volume":"13","author":"Hingorani","year":"2018","journal-title":"PLos One"},{"key":"B85","doi-asserted-by":"publisher","first-page":"910","DOI":"10.1038\/s41467-018-03351-4","article-title":"MT4-MMP deficiency increases patrolling monocyte recruitment to early lesions and accelerates atherosclerosis","volume":"9","author":"Clemente","year":"2018","journal-title":"Nat Commun"},{"key":"B86","doi-asserted-by":"publisher","DOI":"10.3389\/fimmu.2020.586126","article-title":"Prostate cancer peripheral blood NK cells show enhanced CD9, CD49a, CXCR4, CXCL8, MMP-9 production and secrete monocyte-recruiting and polarizing factors","volume":"11","author":"Gallazzi","year":"2020","journal-title":"Front Immunol"},{"key":"B87","doi-asserted-by":"publisher","first-page":"e26718","DOI":"10.1371\/journal.pone.0026718","article-title":"TIMP3 regulates mammary epithelial apoptosis with immune cell recruitment through differential TNF dependence","volume":"6","author":"Hojilla","year":"2011","journal-title":"PLos One"},{"key":"B88","doi-asserted-by":"publisher","DOI":"10.1038\/nri1733","article-title":"Monocyte and macrophage heterogeneity","volume":"5","author":"Gordon","year":"2005","journal-title":"Nat Rev Immunol"},{"key":"B89","doi-asserted-by":"publisher","DOI":"10.1146\/annurev.immunol.021908.132532","article-title":"Alternative activation of macrophages: An immunologic functional perspective","volume":"27","author":"Martinez","year":"2009","journal-title":"Annu Rev Immunol"},{"key":"B90","doi-asserted-by":"publisher","DOI":"10.1038\/nri1418","article-title":"Matrix metalloproteinases as modulators of inflammation and innate immunity","volume":"4","author":"Parks","year":"2004","journal-title":"Nat Rev Immunol"},{"key":"B91","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0042507","article-title":"Classical macrophage activation up-regulates several matrix metalloproteinases through mitogen activated protein kinases and nuclear factor-\u03baB","volume":"7","author":"Huang","year":"2012","journal-title":"PLos One"},{"key":"B92","doi-asserted-by":"publisher","DOI":"10.1172\/JCI19855","article-title":"Th2-predominant inflammation and blockade of IFN-gamma signaling induce aneurysms in allografted aortas","volume":"114","author":"Shimizu","year":"2004","journal-title":"J Clin Invest"},{"key":"B93","doi-asserted-by":"publisher","DOI":"10.1038\/nri2448","article-title":"Exploring the full spectrum of macrophage activation","volume":"8","author":"Mosser","year":"2008","journal-title":"Nat Rev Immunol"},{"key":"B94","doi-asserted-by":"publisher","DOI":"10.1016\/j.cell.2010.02.029","article-title":"Nonresolving inflammation","volume":"140","author":"Nathan","year":"2010","journal-title":"Cell"},{"key":"B95","doi-asserted-by":"publisher","DOI":"10.1016\/s1471-4906(03)00139-x","article-title":"PI3K and negative regulation of TLR signaling","volume":"24","author":"Fukao","year":"2003","journal-title":"Trends Immunol"},{"key":"B96","doi-asserted-by":"publisher","first-page":"24","DOI":"10.1016\/j.it.2009.09.007","article-title":"Innate and adaptive immune responses regulated by glycogen synthase kinase-3 (GSK3)","volume":"31","author":"Beurel","year":"2010","journal-title":"Trends Immunol"},{"key":"B97","doi-asserted-by":"publisher","first-page":"395","DOI":"10.1101\/gad.178749.111","article-title":"MT1-MMP regulates the PI3K\u03b4\u00b7Mi-2\/NuRD-dependent control of macrophage immune function","volume":"26","author":"Shimizu-Hirota","year":"2012","journal-title":"Genes Dev"},{"key":"B98","doi-asserted-by":"publisher","DOI":"10.1101\/gad.1383206","article-title":"Selective and antagonistic functions of SWI\/SNF and Mi-2beta nucleosome remodeling complexes during an inflammatory response","volume":"20","author":"Ramirez-Carrozzi","year":"2006","journal-title":"Genes Dev"},{"key":"B99","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.0811274106","article-title":"Induction of TLR4-target genes entails calcium\/calmodulin-dependent regulation of chromatin remodeling","volume":"106","author":"Lai","year":"2009","journal-title":"Proc Natl Acad Sci U.S.A."},{"key":"B100","doi-asserted-by":"publisher","DOI":"10.1189\/jlb.0409289","article-title":"Protein tyrosine phosphatase shp-1 positively regulates TLR-induced IL-12p40 production in macrophages through inhibition of phosphatidylinositol 3-kinase","volume":"87","author":"Zhou","year":"2010","journal-title":"J Leukoc Biol"},{"key":"B101","doi-asserted-by":"publisher","DOI":"10.1182\/blood-2007-12-129080","article-title":"Macrophage-specific metalloelastase (MMP-12) truncates and inactivates ELR+ CXC chemokines and generates CCL2, -7, -8, and -13 antagonists: Potential role of the macrophage in terminating polymorphonuclear leukocyte influx","volume":"112","author":"Dean","year":"2008","journal-title":"Blood"},{"key":"B102","doi-asserted-by":"publisher","DOI":"10.1126\/science.286.5439.420","article-title":"Defensins and host defense","volume":"286","author":"Ganz","year":"1999","journal-title":"Science"},{"key":"B103","doi-asserted-by":"publisher","DOI":"10.1189\/jlb.69.5.691","article-title":"Participation of mammalian defensins and cathelicidins in anti-microbial immunity: Receptors and activities of human defensins and cathelicidin (LL-37)","volume":"69","author":"Yang","year":"2001","journal-title":"J Leukoc Biol"},{"key":"B104","doi-asserted-by":"publisher","DOI":"10.1038\/77783","article-title":"Secretion of microbicidal alpha-defensins by intestinal paneth cells in response to bacteria","volume":"1","author":"Ayabe","year":"2000","journal-title":"Nat Immunol"},{"key":"B105","doi-asserted-by":"publisher","DOI":"10.1002\/jcp.1041550223","article-title":"Defensins are mitogenic for epithelial cells and fibroblasts","volume":"155","author":"Murphy","year":"1993","journal-title":"J Cell Physiol"},{"key":"B106","doi-asserted-by":"publisher","DOI":"10.1016\/j.dci.2022.104348","article-title":"Matrix metalloproteinase-25 from Japanese Sea bass (Lateolabrax japonicus) is involved in pro-inflammatory responses","volume":"129","author":"Chen","year":"2022","journal-title":"Dev Comp Immunol"},{"key":"B107","doi-asserted-by":"publisher","DOI":"10.1002\/path.1027","article-title":"The role of tumour-associated macrophages in tumour progression: Implications for new anticancer therapies","volume":"196","author":"Bingle","year":"2002","journal-title":"J Pathol"},{"key":"B108","doi-asserted-by":"publisher","DOI":"10.1111\/cas.14272","article-title":"Infiltration of tumor-associated macrophages is involved in tumor programmed death-ligand 1 expression in early lung adenocarcinoma","volume":"111","author":"Shima","year":"2020","journal-title":"Cancer Sci"},{"key":"B109","doi-asserted-by":"publisher","first-page":"39","DOI":"10.1016\/j.cell.2010.03.014","article-title":"Macrophage diversity enhances tumor progression and metastasis","volume":"141","author":"Qian","year":"2010","journal-title":"Cell"},{"key":"B110","doi-asserted-by":"publisher","DOI":"10.1084\/jem.20051342","article-title":"Dystroglycan is selectively cleaved at the parenchymal basement membrane at sites of leukocyte extravasation in experimental autoimmune encephalomyelitis","volume":"203","author":"Agrawal","year":"2006","journal-title":"J Exp Med"},{"key":"B111","doi-asserted-by":"publisher","DOI":"10.1007\/s10555-006-9005-3","article-title":"TNF-alpha in promotion and progression of cancer","volume":"25","author":"Balkwill","year":"2006","journal-title":"Cancer Metastasis Rev"},{"key":"B112","doi-asserted-by":"publisher","first-page":"34","DOI":"10.1016\/j.semcdb.2007.07.003","article-title":"Matrix metalloproteinases as modulators of inflammation","volume":"19","author":"Manicone","year":"2008","journal-title":"Semin Cell Dev Biol"},{"key":"B113","doi-asserted-by":"publisher","DOI":"10.1160\/TH13-07-0588","article-title":"Matrix metalloproteinase-2 of human carotid atherosclerotic plaques promotes platelet activation. correlation with ischaemic events","volume":"111","author":"Lenti","year":"2014","journal-title":"Thromb Haemost"},{"key":"B114","doi-asserted-by":"publisher","DOI":"10.1161\/CIRCULATIONAHA.105.568162","article-title":"Extracellular matrix metalloproteinase inducer regulates matrix metalloproteinase activity in cardiovascular cells: Implications in acute myocardial infarction","volume":"113","author":"Schmidt","year":"2006","journal-title":"Circulation"},{"key":"B115","doi-asserted-by":"publisher","DOI":"10.1161\/01.atv.0000021411.53577.1c","article-title":"Extracellular matrix metalloproteinase inducer (EMMPRIN) is induced upon monocyte differentiation and is expressed in human atheroma","volume":"22","author":"Major","year":"2002","journal-title":"Arterioscler Thromb Vasc Biol"},{"key":"B116","article-title":"Proteinases in rheumatoid arthritis","volume":"32","author":"Murphy","year":"1992","journal-title":"J Rheumatol Suppl"},{"key":"B117","doi-asserted-by":"publisher","DOI":"10.1111\/j.1600-0765.1987.tb01544.x","article-title":"Demonstration of tissue collagenase activity in vivo and its relationship to inflammation severity in human gingiva","volume":"22","author":"Overall","year":"1987","journal-title":"J Periodontal Res"},{"key":"B118","doi-asserted-by":"publisher","DOI":"10.3390\/ijerph17144923","article-title":"The role of matrix metalloproteinases in periodontal disease","volume":"17","author":"Checchi","year":"2020","journal-title":"Int J Environ Res Public Health"},{"key":"B119","doi-asserted-by":"publisher","DOI":"10.1016\/bs.pmbts.2017.03.003","article-title":"Matrix metalloproteinases and synovial joint pathology","volume":"148","author":"Malemud","year":"2017","journal-title":"Prog Mol Biol Transl Sci"},{"key":"B120","doi-asserted-by":"publisher","DOI":"10.1016\/j.actbio.2021.02.042","article-title":"Cryptic ligand on collagen matrix unveiled by MMP13 accelerates bone tissue regeneration via MMP13\/Integrin \u03b13\/RUNX2 feedback loop","volume":"125","author":"Arai","year":"2021","journal-title":"Acta Biomater"},{"key":"B121","doi-asserted-by":"publisher","DOI":"10.1021\/acs.jmedchem.0c00352","article-title":"Matrix metalloproteinases as new targets in Alzheimer\u2019s disease: opportunities and challenges","volume":"63","author":"Zipfel","year":"2020","journal-title":"J Med Chem"},{"key":"B122","doi-asserted-by":"publisher","first-page":"62","DOI":"10.1016\/j.jconrel.2017.01.034","article-title":"Matrix-metalloproteinases as targets for controlled delivery in cancer: An analysis of upregulation and expression","volume":"259","author":"Isaacson","year":"2017","journal-title":"J Control Release"},{"key":"B123","doi-asserted-by":"publisher","DOI":"10.3390\/ijms21165934","article-title":"Matrix metalloproteinases in age-related macular degeneration (AMD)","volume":"21","author":"Garc\u00eda-Onrubia","year":"2020","journal-title":"Int J Mol Sci"},{"key":"B124","doi-asserted-by":"publisher","first-page":"87","DOI":"10.1016\/bs.pmbts.2017.04.001","article-title":"Matrix metalloproteinases in normal pregnancy and preeclampsia","volume":"148","author":"Chen","year":"2017","journal-title":"Prog Mol Biol Transl Sci"},{"key":"B125","doi-asserted-by":"publisher","DOI":"10.1038\/labinvest.2012.141","article-title":"Lack of MMP10 exacerbates experimental colitis and promotes development of inflammation-associated colonic dysplasia","volume":"92","author":"Koller","year":"2012","journal-title":"Lab Invest"},{"key":"B126","doi-asserted-by":"publisher","DOI":"10.1038\/mi.2015.117","article-title":"MMP-19 deficiency causes aggravation of colitis due to defects in innate immune cell function","volume":"9","author":"Brauer","year":"2016","journal-title":"Mucosal Immunol"},{"key":"B127","doi-asserted-by":"publisher","DOI":"10.3109\/14756366.2016.1161620","article-title":"Matrix metalloproteinases (MMPs), the main extracellular matrix (ECM) enzymes in collagen degradation, as a target for anticancer drugs","volume":"31","author":"Jab\u0142o\u0144ska-Trypu\u0107","year":"2016","journal-title":"J Enzyme Inhibition Medicinal Chem"},{"key":"B128","doi-asserted-by":"publisher","DOI":"10.1002\/chem.201805361","article-title":"Design and structural evolution of matrix metalloproteinase inhibitors","volume":"25","author":"Fischer","year":"2019","journal-title":"Chemistry"},{"key":"B129","doi-asserted-by":"publisher","DOI":"10.1016\/j.cardiores.2005.12.002","article-title":"Structure and function of matrix metalloproteinases and TIMPs","volume":"69","author":"Nagase","year":"2006","journal-title":"Cardiovasc Res"},{"key":"B130","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.92.2.402","article-title":"Macrophage foam cells from experimental atheroma constitutively produce matrix-degrading proteinases","volume":"92","author":"Galis","year":"1995","journal-title":"Proc Natl Acad Sci U.S.A."},{"key":"B131","doi-asserted-by":"publisher","DOI":"10.1172\/jci8040","article-title":"Disruption of the myocardial extracellular matrix leads to cardiac dysfunction","volume":"106","author":"Kim","year":"2000","journal-title":"J Clin Invest"},{"key":"B132","doi-asserted-by":"publisher","first-page":"65","DOI":"10.1002\/jor.20716","article-title":"A critical role for collagen II in cartilage matrix degradation: Collagen II induces pro-inflammatory cytokines and MMPs in primary human chondrocytes","volume":"27","author":"Klatt","year":"2009","journal-title":"J Orthopaedic Res"},{"key":"B133","doi-asserted-by":"publisher","DOI":"10.1053\/gast.2003.50063","article-title":"Delivery of matrix metalloproteinase-1 attenuates established liver fibrosis in the rat","volume":"124","author":"Iimuro","year":"2003","journal-title":"Gastroenterology"},{"key":"B134","doi-asserted-by":"publisher","DOI":"10.1161\/01.Cir.0000090687.97972.10","article-title":"Myocardial collagen turnover in hypertrophic cardiomyopathy","volume":"108","author":"Lombardi","year":"2003","journal-title":"Circulation"},{"key":"B135","doi-asserted-by":"publisher","first-page":"R224","DOI":"10.1186\/ar3211","article-title":"Matrix metalloproteinase-8 deficiency increases joint inflammation and bone erosion in the K\/BxN serum-transfer arthritis model","volume":"12","author":"Garc\u00eda","year":"2010","journal-title":"Arthritis Res Ther"},{"key":"B136","doi-asserted-by":"publisher","first-page":"26","DOI":"10.1016\/j.atherosclerosis.2009.01.025","article-title":"Activation of MMP8 and MMP13 by angiotensin II correlates to severe intra-plaque hemorrhages and collagen breakdown in atherosclerotic lesions with a vulnerable phenotype","volume":"204","author":"Cheng","year":"2009","journal-title":"Atherosclerosis"},{"key":"B137","doi-asserted-by":"publisher","DOI":"10.1161\/atvbaha.111.231563","article-title":"Selective inhibition of matrix metalloproteinase-13 increases collagen content of established mouse atherosclerosis","volume":"31","author":"Quillard","year":"2011","journal-title":"Arterioscler Thromb Vasc Biol"},{"key":"B138","doi-asserted-by":"publisher","DOI":"10.1038\/mt.2010.262","article-title":"Antifibrotic effect of MMP13-encoding plasmid DNA delivered using polyethylenimine shielded with hyaluronic acid","volume":"19","author":"Kim","year":"2011","journal-title":"Mol Ther"},{"key":"B139","doi-asserted-by":"publisher","DOI":"10.1002\/cam4.20","article-title":"GM-CSF enhances tumor invasion by elevated MMP-2, -9, and -26 expression","volume":"2","author":"Gutschalk","year":"2013","journal-title":"Cancer Med"},{"key":"B140","doi-asserted-by":"publisher","DOI":"10.1038\/sj.bjc.6690291","article-title":"Gelatinase-a (MMP-2), gelatinase-b (MMP-9) and membrane type matrix metalloproteinase-1 (MT1-MMP) are involved in different aspects of the pathophysiology of malignant gliomas","volume":"79","author":"Forsyth","year":"1999","journal-title":"Br J Cancer"},{"key":"B141","doi-asserted-by":"publisher","DOI":"10.1212\/01.wnl.0000033799.58866.7a","article-title":"MMP-9 correlates with electrophysiologic abnormalities in Guillain-Barr\u00e9 syndrome","volume":"59","author":"Sharshar","year":"2002","journal-title":"Neurology"},{"key":"B142","doi-asserted-by":"publisher","DOI":"10.1212\/WNL.0000000000004257","article-title":"Serum matrix metalloproteinase-9 levels and prognosis of acute ischemic stroke","volume":"89","author":"Zhong","year":"2017","journal-title":"Neurology"},{"key":"B143","doi-asserted-by":"publisher","DOI":"10.2147\/idr.S329004","article-title":"Impact of high serum levels of MMP-7, MMP-9, TGF-\u03b2 and PDGF macrophage activation markers on severity of COVID-19 in obese-diabetic patients","volume":"14","author":"Nasr El-Din","year":"2021","journal-title":"Infection Drug Resistance"},{"key":"B144","doi-asserted-by":"publisher","DOI":"10.1016\/j.neo.2020.08.004","article-title":"Prostate cancer-derived MMP-3 controls intrinsic cell growth and extrinsic angiogenesis","volume":"22","author":"Frieling","year":"2020","journal-title":"Neoplasia"},{"key":"B145","doi-asserted-by":"publisher","DOI":"10.3389\/fimmu.2022.885229","article-title":"Concentration of serum matrix metalloproteinase-3 in patients with primary biliary cholangitis","volume":"13","author":"Bauer","year":"2022","journal-title":"Front Immunol"},{"key":"B146","doi-asserted-by":"publisher","DOI":"10.1161\/atvbaha.120.314143","article-title":"A role for MMP-10 (Matrix metalloproteinase-10) in calcific aortic valve stenosis","volume":"40","author":"Matilla","year":"2020","journal-title":"Arterioscler Thromb Vasc Biol"},{"key":"B147","doi-asserted-by":"publisher","DOI":"10.1038\/onc.2008.119","article-title":"Matrix metalloproteinase-10 is a critical effector of protein kinase Ciota-Par6alpha-Mediated lung cancer","volume":"27","author":"Frederick","year":"2008","journal-title":"Oncogene"},{"key":"B148","doi-asserted-by":"publisher","DOI":"10.1016\/j.cca.2009.11.009","article-title":"The clinical implications of MMP-11 and CK-20 expression in human breast cancer","volume":"411","author":"Cheng","year":"2010","journal-title":"Clinica Chimica Acta"},{"key":"B149","doi-asserted-by":"publisher","first-page":"337","DOI":"10.1186\/s12967-015-0702-y","article-title":"Expression of CD147 and matrix metalloproteinase-11 in colorectal cancer and their relationship to clinicopathological features","volume":"13","author":"Tian","year":"2015","journal-title":"J Trans Med"},{"key":"B150","doi-asserted-by":"publisher","DOI":"10.1016\/j.ijporl.2010.02.016","article-title":"The role of matrix metalloproteinases in recurrent tonsillitis","volume":"74","author":"Acioglu","year":"2010","journal-title":"Int J Pediatr Otorhinolaryngol"},{"key":"B151","doi-asserted-by":"publisher","DOI":"10.1038\/onc.2014.22","article-title":"MMP-7-mediated cleavage of nucleolin at ASP255 induces MMP9 expression to promote tumor malignancy","volume":"34","author":"Hsu","year":"2015","journal-title":"Oncogene"},{"key":"B152","doi-asserted-by":"publisher","DOI":"10.1523\/jneurosci.1588-12.2012","article-title":"Metalloproteinases and their associated genes contribute to the functional integrity and noise-induced damage in the cochlear sensory epithelium","volume":"32","author":"Hu","year":"2012","journal-title":"J Neurosci"},{"key":"B153","doi-asserted-by":"publisher","DOI":"10.1016\/j.cardfail.2019.02.006","article-title":"The role of matrix metalloproteinases and tissue inhibitors of metalloproteinases in duchenne muscular dystrophy cardiomyopathy","volume":"25","author":"Soslow","year":"2019","journal-title":"J Cardiac Failure"},{"key":"B154","doi-asserted-by":"publisher","DOI":"10.1186\/1471-2202-10-17","article-title":"Matrix metalloproteinase-7 facilitates immune access to the CNS in experimental autoimmune encephalomyelitis","volume":"10","author":"Buhler","year":"2009","journal-title":"BMC Neurosci"},{"key":"B155","doi-asserted-by":"publisher","DOI":"10.1016\/0168-8278(88)80010-2","article-title":"Membrane-type matrix metalloproteinase-1(MT1-MTP) gene is overexpressed in highly invasive hepatocellular carcinomas","volume":"28","author":"Harada","year":"1998","journal-title":"J Hepatol"},{"key":"B156","doi-asserted-by":"publisher","first-page":"e115577","DOI":"10.1371\/journal.pone.0115577","article-title":"miR-150-5p inhibits hepatoma cell migration and invasion by targeting MMP14","volume":"9","author":"Li","year":"2014","journal-title":"PLos One"},{"key":"B157","doi-asserted-by":"publisher","DOI":"10.1002\/(SICI)1097-0347(199910)21:7<627::AID-HED7>3.0.CO;2-2","article-title":"Expression of MMPs, MT-MMP, and TIMPs in squamous cell carcinoma of the oral cavity: Correlations with tumor invasion and metastasis","volume":"21","author":"Kurahara","year":"1999","journal-title":"Head Neck"},{"key":"B158","doi-asserted-by":"publisher","DOI":"10.1245\/s10434-008-9916-z","article-title":"A Large-scale study of MT1-MMP as a marker for isolated tumor cells in peripheral blood and bone marrow in gastric cancer cases","volume":"15","author":"Mimori","year":"2008","journal-title":"Ann Surg Oncol"},{"key":"B159","article-title":"Increased MT2-MMP expression in gastric cancer patients is associated with poor prognosis","volume":"8","author":"Xu","year":"2015","journal-title":"Int J Clin Exp Pathol"},{"key":"B160","doi-asserted-by":"publisher","DOI":"10.1111\/nan.12166","article-title":"A role for matrix remodelling proteins in invasive and malignant meningiomas","volume":"41","author":"Jalali","year":"2015","journal-title":"Neuropathol Appl Neurobiol"},{"key":"B161","doi-asserted-by":"publisher","DOI":"10.1158\/0008-5472.Can-05-3012","article-title":"Membrane-type 4 matrix metalloproteinase promotes breast cancer growth and metastases","volume":"66","author":"Chabottaux","year":"2006","journal-title":"Cancer Res"},{"key":"B162","doi-asserted-by":"publisher","DOI":"10.3389\/fnmol.2016.00163","article-title":"MT5-MMP promotes Alzheimer\u2019s pathogenesis in the frontal cortex of 5xFAD mice and app trafficking in vitro","volume":"9","author":"Baranger","year":"2016","journal-title":"Front Mol Neurosci"},{"key":"B163","doi-asserted-by":"publisher","DOI":"10.1007\/s00018-015-1992-1","article-title":"MT5-MMP is a new pro-amyloidogenic proteinase that promotes amyloid pathology and cognitive decline in a transgenic mouse model of Alzheimer\u2019s disease","volume":"73","author":"Baranger","year":"2016","journal-title":"Cell Mol Life Sci"},{"key":"B164","doi-asserted-by":"publisher","first-page":"65","DOI":"10.1186\/s12974-022-02407-z","article-title":"MT5-MMP promotes neuroinflammation, neuronal excitability and A\u03b2 production in primary neuron\/astrocyte cultures from the 5xFAD mouse model of Alzheimer\u2019s disease","volume":"19","author":"Pilat","year":"2022","journal-title":"J Neuroinflamm"},{"key":"B165","doi-asserted-by":"publisher","DOI":"10.3390\/bioengineering7010018","article-title":"MMP24 as a target of YAP is a potential prognostic factor in cancer patients","volume":"7","author":"Sugimoto","year":"2020","journal-title":"Bioengineering"},{"key":"B166","article-title":"Human MT6-matrix metalloproteinase: Identification, progelatinase a activation, and expression in brain tumors","volume":"60","author":"Velasco","year":"2000","journal-title":"Cancer Res"},{"key":"B167","doi-asserted-by":"publisher","DOI":"10.1161\/circulationaha.109.912774","article-title":"Circulating biomarkers of collagen metabolism in cardiac diseases","volume":"121","author":"L\u00f3pez","year":"2010","journal-title":"Circulation"},{"key":"B168","doi-asserted-by":"publisher","DOI":"10.1016\/j.ejvs.2005.03.009","article-title":"A review of biological factors implicated in abdominal aortic aneurysm rupture","volume":"30","author":"Choke","year":"2005","journal-title":"Eur J Vasc Endovascular Surg"},{"key":"B169","doi-asserted-by":"publisher","first-page":"375","DOI":"10.1080\/10409230290771546","article-title":"Biochemistry and molecular biology of gelatinase B or matrix metalloproteinase-9 (MMP-9)","volume":"37","author":"Van den Steen","year":"2002","journal-title":"Crit Rev Biochem Mol Biol"},{"key":"B170","doi-asserted-by":"publisher","first-page":"299","DOI":"10.1007\/s10875-006-9022-6","article-title":"Matrix metalloproteinase-9 and autoimmune diseases","volume":"26","author":"Ram","year":"2006","journal-title":"J Clin Immunol"},{"key":"B171","doi-asserted-by":"publisher","DOI":"10.1038\/nrc884","article-title":"Strategies for MMP inhibition in cancer: Innovations for the post-trial era","volume":"2","author":"Overall","year":"2002","journal-title":"Nat Rev Cancer"},{"key":"B172","doi-asserted-by":"publisher","first-page":"18","DOI":"10.1016\/j.pain.2011.08.001","article-title":"Suppression of pain and joint destruction by inhibition of the proteasome system in experimental osteoarthritis","volume":"153","author":"Ahmed","year":"2012","journal-title":"Pain"},{"key":"B173","doi-asserted-by":"publisher","DOI":"10.1002\/jcp.25430","article-title":"Intricate functions of matrix metalloproteinases in physiological and pathological conditions","volume":"231","author":"Mittal","year":"2016","journal-title":"J Cell Physiol"},{"key":"B174","article-title":"Molecular cloning of a novel membrane-type matrix metalloproteinase from a human breast carcinoma","volume":"56","author":"Puente","year":"1996","journal-title":"Cancer Res"},{"key":"B175","doi-asserted-by":"publisher","DOI":"10.3390\/ijms21249739","article-title":"The roles of matrix metalloproteinases and their inhibitors in human diseases","volume":"21","author":"Cabral-Pacheco","year":"2020","journal-title":"Int J Mol Sci"},{"key":"B176","doi-asserted-by":"publisher","DOI":"10.3390\/cells9051313","article-title":"Metalloproteinases and their inhibitors: Potential for the development of new therapeutics","volume":"9","author":"Raeeszadeh-Sarmazdeh","year":"2020","journal-title":"Cells"},{"key":"B177","doi-asserted-by":"publisher","DOI":"10.1126\/science.282.5392.1281","article-title":"An essential role for ectodomain shedding in mammalian development","volume":"282","author":"Peschon","year":"1998","journal-title":"Science"},{"key":"B178","doi-asserted-by":"publisher","DOI":"10.1038\/sj.onc.1207387","article-title":"Cleavage of CD95 by matrix metalloproteinase-7 induces apoptosis resistance in tumour cells","volume":"23","author":"Strand","year":"2004","journal-title":"Oncogene"},{"key":"B179","doi-asserted-by":"publisher","DOI":"10.1038\/sj.onc.1206292","article-title":"Tissue inhibitor of metalloproteinases-3 induces apoptosis in melanoma cells by stabilization of death receptors","volume":"22","author":"Ahonen","year":"2003","journal-title":"Oncogene"},{"key":"B180","doi-asserted-by":"publisher","DOI":"10.1083\/jcb.200405001","article-title":"MT1-MMP-dependent neovessel formation within the confines of the three-dimensional extracellular matrix","volume":"167","author":"Chun","year":"2004","journal-title":"J Cell Biol"},{"key":"B181","doi-asserted-by":"publisher","DOI":"10.1182\/blood-2008-12-196451","article-title":"Endothelial cell lumen and vascular guidance tunnel formation requires MT1-MMP-dependent proteolysis in 3-dimensional collagen matrices","volume":"114","author":"Stratman","year":"2009","journal-title":"Blood"},{"key":"B182","doi-asserted-by":"publisher","DOI":"10.1093\/carcin\/24.2.343","article-title":"Matrix metalloproteinases, angiogenesis, and cancer: Commentary re: A. c. Lockhart et\u00a0al., reduction of wound angiogenesis in patients treated with BMS-275291, a broad spectrum matrix metalloproteinase inhibitor","volume":"9","author":"Rundhaug","year":"2003","journal-title":"Clin Cancer Res"},{"key":"B183","doi-asserted-by":"publisher","DOI":"10.1002\/jcb.26396","article-title":"Leptin induces matrix metalloproteinase 7 expression to promote ovarian cancer cell invasion by activating ERK and JNK pathways","volume":"119","author":"Ghasemi","year":"2018","journal-title":"J Cell Biochem"},{"key":"B184","doi-asserted-by":"publisher","DOI":"10.3390\/antiox4020248","article-title":"Mechanisms of photoaging and cutaneous photocarcinogenesis, and photoprotective strategies with phytochemicals","volume":"4","author":"Bosch","year":"2015","journal-title":"Antioxidants"},{"key":"B185","doi-asserted-by":"publisher","DOI":"10.3892\/ol.2018.9092","article-title":"Upregulating MMP-1 in carcinoma-associated fibroblasts reduces the efficacy of Taxotere on breast cancer synergized by Collagen IV","volume":"16","author":"Cui","year":"2018","journal-title":"Oncol Lett"},{"key":"B186","doi-asserted-by":"publisher","DOI":"10.3892\/ol.2018.9779","article-title":"MMP-1 is overexpressed in triple-negative breast cancer tissues and the knockdown of MMP-1 expression inhibits tumor cell malignant behaviors in vitro","volume":"17","author":"Wang","year":"2019","journal-title":"Oncol Lett"},{"key":"B187","doi-asserted-by":"publisher","DOI":"10.1097\/CAD.0b013e32833ab7a0","article-title":"Overexpression of MMP-13 gene in colorectal cancer with liver metastasis","volume":"30","author":"Yamada","year":"2010","journal-title":"Anticancer Res"},{"key":"B188","doi-asserted-by":"publisher","DOI":"10.3892\/ijo.2016.3400","article-title":"Insights into the distinct roles of MMP-11 in tumor biology and future therapeutics (Review)","volume":"48","author":"Zhang","year":"2016","journal-title":"Int J Oncol"},{"key":"B189","doi-asserted-by":"publisher","DOI":"10.3390\/ph12020077","article-title":"The expanding role of MT1-MMP in cancer progression","volume":"12","author":"Knapinska","year":"2019","journal-title":"Pharmaceuticals"},{"key":"B190","doi-asserted-by":"publisher","first-page":"16","DOI":"10.1111\/j.1742-4658.2010.07919.x","article-title":"Roles of matrix metalloproteinases in cancer progression and their pharmacological targeting","volume":"278","author":"Gialeli","year":"2011","journal-title":"FEBS J"},{"key":"B191","doi-asserted-by":"publisher","first-page":"83","DOI":"10.1186\/s13073-020-00780-z","article-title":"Small-molecule MMP2\/MMP9 inhibitor SB-3CT modulates tumor immune surveillance by regulating PD-L1","volume":"12","author":"Ye","year":"2020","journal-title":"Genome Med"},{"key":"B192","doi-asserted-by":"publisher","DOI":"10.1016\/j.matbio.2015.01.016","article-title":"MMP generated matrikines","author":"Wells","year":"2015","journal-title":"Matrix Biol"},{"key":"B193","doi-asserted-by":"publisher","DOI":"10.3390\/ijms23010146","article-title":"Matrix metalloproteinases shape the tumor microenvironment in cancer progression","volume":"23","author":"Niland","year":"2021","journal-title":"Int J Mol Sci"},{"key":"B194","doi-asserted-by":"publisher","first-page":"581","DOI":"10.1186\/s12885-019-5768-0","article-title":"A pan-cancer perspective of matrix metalloproteases (MMP) gene expression profile and their diagnostic\/prognostic potential","volume":"19","author":"Gobin","year":"2019","journal-title":"BMC Cancer"},{"key":"B195","doi-asserted-by":"publisher","DOI":"10.3390\/ijms222212389","article-title":"Integrated multi-omics investigations of metalloproteinases in colon cancer: Focus on MMP2 and MMP9","volume":"22","author":"Buttacavoli","year":"2021","journal-title":"Int J Mol Sci"},{"key":"B196","doi-asserted-by":"publisher","DOI":"10.4049\/jimmunol.1202610","article-title":"Inflammation induced by MMP-9 enhances tumor regression of experimental breast cancer","volume":"190","author":"Leifler","year":"2013","journal-title":"J Immunol"},{"key":"B197","doi-asserted-by":"publisher","DOI":"10.1556\/EuJMI.1.2011.4.6","article-title":"The distinct roles of MMP-2 and MMP-9 in acute DSS colitis","volume":"1","author":"Heimesaat","year":"2011","journal-title":"Eur J Microbiol Immunol"},{"key":"B198","doi-asserted-by":"publisher","DOI":"10.1007\/s11596-018-1873-6","article-title":"WGCNA reveals key roles of IL8 and MMP-9 in progression of involvement area in colon of patients with ulcerative colitis","volume":"38","author":"Lin","year":"2018","journal-title":"Curr Med Sci"},{"key":"B199","doi-asserted-by":"publisher","DOI":"10.1155\/2022\/2592962","article-title":"Prognostic and immunological roles of MMP-9 in pan-cancer","volume":"2022","author":"Zeng","year":"2022","journal-title":"BioMed Res Int"},{"key":"B200","doi-asserted-by":"publisher","first-page":"e2101029","DOI":"10.1002\/advs.202101029","article-title":"Interleukin-33 is a novel immunosuppressor that protects cancer cells from TIL killing by a macrophage-mediated shedding mechanism","volume":"8","author":"Wu","year":"2021","journal-title":"Advanced Sci"},{"key":"B201","doi-asserted-by":"publisher","first-page":"e0252052","DOI":"10.1371\/journal.pone.0252052","article-title":"High MMP-11 expression associated with low CD8+ T cells decreases the survival rate in patients with breast cancer","volume":"16","author":"Kim","year":"2021","journal-title":"PLos One"},{"key":"B202","doi-asserted-by":"publisher","DOI":"10.1016\/j.bbamcr.2017.05.010","article-title":"Matrix metalloproteinases as regulators of inflammatory processes","volume":"1864","author":"Fingleton","year":"2017","journal-title":"Biochim Biophys Acta Mol Cell Res"},{"key":"B203","doi-asserted-by":"publisher","first-page":"899","DOI":"10.4049\/jimmunol.1600502","article-title":"Stromelysin-2 (MMP10) moderates inflammation by controlling macrophage activation","volume":"197","author":"McMahan","year":"2016","journal-title":"J Immunol"},{"key":"B204","doi-asserted-by":"publisher","DOI":"10.1016\/s0016-5085(99)70339-2","article-title":"Matrix metalloproteinase levels are elevated in inflammatory bowel disease","volume":"117","author":"Baugh","year":"1999","journal-title":"Gastroenterology"},{"key":"B205","doi-asserted-by":"publisher","first-page":"63","DOI":"10.1136\/gut.47.1.63","article-title":"Differential expression of matrix metalloproteinases and their tissue inhibitors in colon mucosa of patients with inflammatory bowel disease","volume":"47","author":"von Lampe","year":"2000","journal-title":"Gut"},{"key":"B206","doi-asserted-by":"publisher","DOI":"10.1007\/s005350300062","article-title":"The expression of matrix metalloproteinase matrilysin indicates the degree of inflammation in ulcerative colitis","volume":"38","author":"Matsuno","year":"2003","journal-title":"J Gastroenterol"},{"key":"B207","doi-asserted-by":"publisher","DOI":"10.1111\/j.1399-0039.1996.tb02552.x","article-title":"Enhanced expression of matrilysin, collagenase, and stromelysin-1 in gastrointestinal ulcers","volume":"148","author":"Saarialho-Kere","year":"1996","journal-title":"Am J Pathol"},{"key":"B208","doi-asserted-by":"publisher","DOI":"10.3389\/fnins.2020.585544","article-title":"MMP13 expression is increased following mutant \u03b1-synuclein exposure and promotes inflammatory responses in microglia","volume":"14","author":"S\u00e1nchez","year":"2020","journal-title":"Front Neurosci"},{"key":"B209","doi-asserted-by":"publisher","DOI":"10.2741\/2161","article-title":"The dual personalities of matrix metalloproteinases in inflammation","volume":"12","author":"Le","year":"2007","journal-title":"Front Biosci"},{"key":"B210","doi-asserted-by":"publisher","DOI":"10.1128\/CMR.00047-08","article-title":"Matrix metalloproteinases as drug targets in infections caused by gram-negative bacteria and in septic shock","volume":"22","author":"Vanlaere","year":"2009","journal-title":"Clin Microbiol Rev"},{"key":"B211","doi-asserted-by":"publisher","DOI":"10.1002\/emmm.201100145","article-title":"A matrix metalloprotease-PAR1 system regulates vascular integrity, systemic inflammation and death in sepsis","volume":"3","author":"Tressel","year":"2011","journal-title":"EMBO Mol Med"},{"key":"B212","doi-asserted-by":"publisher","first-page":"767","DOI":"10.1038\/s41419-020-02959-z","article-title":"Matrix metalloproteinase 9 (MMP9) limits reactive oxygen species (ROS) accumulation and DNA damage in colitis-associated cancer","volume":"11","author":"Walter","year":"2020","journal-title":"Cell Death Dis"},{"key":"B213","doi-asserted-by":"publisher","first-page":"792","DOI":"10.1158\/0008-5472.CAN-09-3166","article-title":"Matrix metalloproteinase-9 functions as a tumor suppressor in colitis-associated cancer","volume":"70","author":"Garg","year":"2010","journal-title":"Cancer Res"},{"key":"B214","doi-asserted-by":"publisher","DOI":"10.1038\/ajg.2011.51","article-title":"Molecular pathways underlying IBD-associated colorectal neoplasia: Therapeutic implications","volume":"106","author":"Goel","year":"2011","journal-title":"Am J Gastroenterol"},{"key":"B215","doi-asserted-by":"publisher","DOI":"10.1097\/MIB.0000000000000163","article-title":"Matrix metalloproteases role in bowel inflammation and inflammatory bowel disease: An up to date review","volume":"20","author":"O\u02bcShea","year":"2014","journal-title":"Inflammation Bowel Dis"},{"key":"B216","doi-asserted-by":"publisher","DOI":"10.1152\/ajpheart.00036.2002","article-title":"Increased activity and expression of matrix metalloproteinase-9 in a rat model of distal colitis","volume":"284","author":"Medina","year":"2003","journal-title":"Am J Physiol Gastrointestinal Liver Physiol"},{"key":"B217","doi-asserted-by":"publisher","first-page":"97","DOI":"10.1002\/ibd.20011","article-title":"Matrix metalloproteinases in inflammatory bowel disease: Boon or a bane","volume":"13","author":"Ravi","year":"2007","journal-title":"Inflamm Bowel Dis"},{"key":"B218","doi-asserted-by":"publisher","DOI":"10.1016\/j.dld.2005.02.011","article-title":"Expression of matrix metalloproteinases-2 and -9 in intestinal tissue of patients with inflammatory bowel diseases","volume":"37","author":"Gao","year":"2005","journal-title":"Digestive Liver Dis"},{"key":"B219","doi-asserted-by":"publisher","DOI":"10.1007\/s10620-006-9255-5","article-title":"Increased activity and expression of gelatinases in ischemic colitis","volume":"51","author":"Medina","year":"2006","journal-title":"Dig Dis Sci"},{"key":"B220","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0127063","article-title":"Selective allosteric inhibition of MMP9 is efficacious in preclinical models of ulcerative colitis and colorectal cancer","volume":"10","author":"Marshall","year":"2015","journal-title":"PLos One"},{"key":"B221","doi-asserted-by":"publisher","DOI":"10.1007\/s005350300075","article-title":"Mucosal expression of matrix metalloproteinases and their tissue inhibitors in ulcerative colitis patients","volume":"38","author":"Kusugami","year":"2003","journal-title":"J Gastroenterol"},{"key":"B222","doi-asserted-by":"crossref","DOI":"10.4049\/jimmunol.158.4.1582","article-title":"A major role for matrix metalloproteinases in T cell injury in the gut","volume":"158","author":"Pender","year":"1997","journal-title":"J Immunol"},{"key":"B223","doi-asserted-by":"publisher","DOI":"10.4049\/jimmunol.160.8.4098","article-title":"A P55 TNF receptor immunoadhesin prevents T cell-mediated intestinal injury by inhibiting matrix metalloproteinase production","volume":"160","author":"Pender","year":"1998","journal-title":"J Immunol"},{"key":"B224","doi-asserted-by":"publisher","DOI":"10.1136\/gut.2003.017442","article-title":"Expression and localisation of matrix metalloproteinases and their natural inhibitors in fistulae of patients with Crohn's disease","volume":"53","author":"Kirkegaard","year":"2004","journal-title":"Gut"},{"key":"B225","doi-asserted-by":"publisher","DOI":"10.1083\/jcb.137.6.1445","article-title":"The activity of collagenase-1 is required for keratinocyte migration on a type I collagen matrix","volume":"137","author":"Pilcher","year":"1997","journal-title":"J Cell Biol"},{"key":"B226","doi-asserted-by":"publisher","DOI":"10.1080\/00365520410003470","article-title":"Collagenase-1 (MMP-1), matrilysin-1 (MMP-7), and stromelysin-2 (MMP-10) are expressed by migrating enterocytes during intestinal wound healing","volume":"39","author":"Salmela","year":"2004","journal-title":"Scand J Gastroenterol"},{"key":"B227","doi-asserted-by":"publisher","DOI":"10.1016\/j.biocel.2007.10.024","article-title":"Metalloproteinases and their inhibitors: Regulators of wound healing","volume":"40","author":"Gill","year":"2008","journal-title":"Int J Biochem Cell Biol"},{"key":"B228","doi-asserted-by":"publisher","DOI":"10.1016\/j.jss.2010.03.002","article-title":"The role of matrix metalloproteinases in intestinal epithelial wound healing during normal and inflammatory states","volume":"168","author":"Hayden","year":"2011","journal-title":"J Surg Res"},{"key":"B229","doi-asserted-by":"publisher","DOI":"10.1007\/s00535-002-1101-8","article-title":"Matrix metalloproteinase-3 secretion from human colonic subepithelial myofibroblasts: Role of interleukin-17","volume":"38","author":"Bamba","year":"2003","journal-title":"J Gastroenterol"},{"key":"B230","doi-asserted-by":"publisher","DOI":"10.1006\/jsre.1999.5599","article-title":"Stromelysin-1-deficient fibroblasts display impaired contraction in vitro","volume":"84","author":"Bullard","year":"1999","journal-title":"J Surg Res"},{"key":"B231","doi-asserted-by":"publisher","DOI":"10.1097\/00000658-199908000-00017","article-title":"Impaired wound contraction in stromelysin-1-deficient mice","volume":"230","author":"Bullard","year":"1999","journal-title":"Ann Surg"},{"key":"B232","doi-asserted-by":"publisher","DOI":"10.1016\/j.bbagen.2014.03.007","article-title":"Matrix metalloproteinases in inflammation","volume":"1840","author":"Nissinen","year":"2014","journal-title":"Biochim Biophys Acta"},{"key":"B233","doi-asserted-by":"publisher","DOI":"10.1111\/prd.12035","article-title":"Matrix metalloproteinase processing of signaling molecules to regulate inflammation","volume":"63","author":"Butler","year":"2013","journal-title":"Periodontol 2000"},{"key":"B234","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M107736200","article-title":"Matrix metalloproteinase activity inactivates the CXC chemokine stromal cell-derived factor-1","volume":"276","author":"McQuibban","year":"2001","journal-title":"J Biol Chem"},{"key":"B235","doi-asserted-by":"publisher","DOI":"10.1182\/blood.V100.4.1160.h81602001160_1160_1167","article-title":"Matrix metalloproteinase processing of monocyte chemoattractant proteins generates CC chemokine receptor antagonists with anti-inflammatory properties in vivo","volume":"100","author":"McQuibban","year":"2002","journal-title":"Blood"},{"key":"B236","doi-asserted-by":"publisher","DOI":"10.1046\/j.1432-1033.2003.03760.x","article-title":"Gelatinase B\/MMP-9 and neutrophil collagenase\/MMP-8 process the chemokines human GCP-2\/CXCl6, ENA-78\/CXCl5 and mouse GCP-2\/LIX and modulate their physiological activities","volume":"270","author":"Van Den Steen","year":"2003","journal-title":"Eur J Biochem"},{"key":"B237","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M111.314609","article-title":"Biochemical analysis of matrix metalloproteinase activation of chemokines CCL15 and CCL23 and increased glycosaminoglycan binding of CCL16","volume":"287","author":"Starr","year":"2012","journal-title":"J Biol Chem"},{"key":"B238","doi-asserted-by":"publisher","DOI":"10.1172\/JCI7091","article-title":"Matrix metalloproteinase-7-dependent release of tumor necrosis factor-alpha in a model of herniated disc resorption","volume":"105","author":"Haro","year":"2000","journal-title":"J Clin Invest"},{"key":"B239","doi-asserted-by":"publisher","DOI":"10.1016\/s0955-0674(00)00248-9","article-title":"Matrix metalloproteinases: They're not just for matrix anymore","volume":"13","author":"McCawley","year":"2001","journal-title":"Curr Opin Cell Biol"},{"key":"B240","doi-asserted-by":"publisher","DOI":"10.4049\/jimmunol.161.7.3340","article-title":"Generation of biologically active IL-1 beta by matrix metalloproteinases: A novel caspase-1-dependent pathway of IL-1 beta processing","volume":"161","author":"Sch\u00f6nbeck","year":"1998","journal-title":"J Immunol"},{"key":"B241","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.271.25.14657","article-title":"Degradation of interleukin 1beta by matrix metalloproteinases","volume":"271","author":"Ito","year":"1996","journal-title":"J Biol Chem"},{"key":"B242","doi-asserted-by":"publisher","DOI":"10.1007\/s10753-019-01007-z","article-title":"Sudachitin inhibits matrix metalloproteinase-1 and -3 production in tumor necrosis factor-\u03b1-stimulated human periodontal ligament cells","volume":"42","author":"Hosokawa","year":"2019","journal-title":"Inflammation"},{"key":"B243","doi-asserted-by":"publisher","DOI":"10.1902\/jop.2013.130063","article-title":"Tumor necrosis factor-\u03b1 induces matrix metalloproteinases-3, -10, and -13 in human periodontal ligament cells","volume":"85","author":"Ahn","year":"2014","journal-title":"J Periodontol"},{"key":"B244","doi-asserted-by":"publisher","DOI":"10.1177\/1535370216650940","article-title":"Induction of matrix metalloproteinase-1 by tumor necrosis factor-\u03b1 is mediated by interleukin-6 in cultured fibroblasts of keratoconus","volume":"241","author":"Du","year":"2016","journal-title":"Exp Biol Med"},{"key":"B245","doi-asserted-by":"publisher","first-page":"1991","DOI":"10.1053\/j.gastro.2005.09.017","article-title":"Targeted deletion of metalloproteinase 9 attenuates experimental colitis in mice: Central role of epithelial-derived MMP","volume":"129","author":"Castaneda","year":"2005","journal-title":"Gastroenterology"},{"key":"B246","doi-asserted-by":"publisher","DOI":"10.1007\/s10350-003-0050-5","article-title":"Up-regulation of collagen and tissue inhibitors of matrix metalloproteinase in colonic diverticular disease","volume":"47","author":"Mimura","year":"2004","journal-title":"Dis Colon Rectum"},{"key":"B247","doi-asserted-by":"publisher","DOI":"10.1097\/00005176-200501000-00011","article-title":"Matrilysins-1 and -2 (MMP-7 and -26) and metalloelastase (MMP-12), unlike MMP-19, are up-regulated in necrotizing enterocolitis","volume":"40","author":"Bister","year":"2005","journal-title":"J Pediatr Gastroenterol Nutr"},{"key":"B248","doi-asserted-by":"publisher","DOI":"10.4049\/jimmunol.161.7.3340","article-title":"Human neutrophil collagenase. a distinct gene product with homology to other matrix metalloproteinases","volume":"265","author":"Hasty","year":"1990","journal-title":"J Biol Chem"},{"key":"B249","doi-asserted-by":"publisher","DOI":"10.1038\/nature08181","article-title":"Macrophage elastase kills bacteria within murine macrophages","volume":"460","author":"Houghton","year":"2009","journal-title":"Nature"},{"key":"B250","doi-asserted-by":"publisher","DOI":"10.1126\/science.286.5437.113","article-title":"Regulation of intestinal alpha-defensin activation by the metalloproteinase matrilysin in innate host defense","volume":"286","author":"Wilson","year":"1999","journal-title":"Science"},{"key":"B251","doi-asserted-by":"publisher","DOI":"10.1111\/j.1365-2567.2005.02281.x","article-title":"Role of matrix metalloproteinase-7 in the modulation of a chlamydia trachomatis infection","volume":"117","author":"Pal","year":"2006","journal-title":"Immunology"},{"key":"B252","doi-asserted-by":"publisher","DOI":"10.15252\/emmm.201910862","article-title":"Endothelial MT1-MMP targeting limits intussusceptive angiogenesis and colitis via TSP1\/Nitric oxide axis","volume":"12","author":"Esteban","year":"2020","journal-title":"EMBO Mol Med"},{"key":"B253","doi-asserted-by":"publisher","DOI":"10.1158\/0008-5472.CAN-16-2501","article-title":"Heme-Oxygenase-1 production by intestinal CX3CR1 macrophages helps to resolve inflammation and prevents carcinogenesis","volume":"77","author":"Marelli","year":"2017","journal-title":"Cancer Res"},{"key":"B254","doi-asserted-by":"publisher","DOI":"10.1172\/JCI59150","article-title":"CX3CR1 regulates intestinal macrophage homeostasis, bacterial translocation, and colitogenic Th17 responses in mice","volume":"121","author":"Medina-Contreras","year":"2011","journal-title":"J Clin Invest"},{"key":"B255","doi-asserted-by":"publisher","DOI":"10.2174\/1389203720666190305165722","article-title":"Crosstalk between the CX3CL1\/CX3CR1 axis and inflammatory signaling pathways in tissue injury","volume":"20","author":"Zhuang","year":"2019","journal-title":"Curr Protein Pept Sci"},{"key":"B256","doi-asserted-by":"publisher","DOI":"10.1097\/mib.0000000000000068","article-title":"Neutrophil gelatinase B-associated lipocalin and matrix metalloproteinase-9 complex as a surrogate serum marker of mucosal healing in ulcerative colitis","volume":"20","author":"de Bruyn","year":"2014","journal-title":"Inflamm Bowel Dis"},{"key":"B257","doi-asserted-by":"publisher","DOI":"10.1093\/ecco-jcc\/jjv005","article-title":"The diagnostic value of a new fecal marker, matrix metalloprotease-9, in different types of inflammatory bowel diseases","volume":"9","author":"Farkas","year":"2015","journal-title":"J Crohns Colitis"},{"key":"B258","doi-asserted-by":"publisher","DOI":"10.1002\/ibd.22996","article-title":"Fecal MMP-9: A new noninvasive differential diagnostic and activity marker in ulcerative colitis","volume":"19","author":"Annah\u00e1zi","year":"2013","journal-title":"Inflamm Bowel Dis"},{"key":"B259","doi-asserted-by":"publisher","DOI":"10.1038\/ajg.2013.354","article-title":"Emerging BiomARKers in inflammatory bowel disease (EMBARK) study identifies fecal calprotectin, serum MMP9, and serum IL-22 as a novel combination of biomarkers for Crohn's disease activity: Role of cross-sectional imaging","volume":"108","author":"Faubion","year":"2013","journal-title":"Am J Gastroenterol"},{"key":"B260","doi-asserted-by":"publisher","DOI":"10.1016\/j.mam.2005.07.009","article-title":"Role of matrix metalloproteinases in inflammatory bowel disease","volume":"26","author":"Naito","year":"2005","journal-title":"Mol Aspects Med"},{"key":"B261","doi-asserted-by":"publisher","DOI":"10.1016\/0016-5085(92)91163-x","article-title":"Colorectal cancer risk and mortality in patients with ulcerative colitis","volume":"103","author":"Langholz","year":"1992","journal-title":"Gastroenterology"},{"key":"B262","doi-asserted-by":"publisher","DOI":"10.1016\/s0140-6736(70)91213-4","article-title":"Mortality in Crohn's disease","volume":"1","author":"Prior","year":"1970","journal-title":"Lancet"},{"key":"B263","doi-asserted-by":"publisher","DOI":"10.1093\/ibd\/izy221","article-title":"An overview of molecular profiles in ulcerative colitis-related cancer","volume":"24","author":"Xue","year":"2018","journal-title":"Inflammation Bowel Dis"},{"key":"B264","doi-asserted-by":"publisher","DOI":"10.23736\/S0026-4733.17.07437-5","article-title":"Colitis-associated colorectal cancer in patients with inflammatory bowel disease","volume":"72","author":"Baek","year":"2017","journal-title":"Minerva Chir"},{"key":"B265","doi-asserted-by":"publisher","first-page":"715","DOI":"10.1053\/j.gastro.2021.10.035","article-title":"Colorectal cancer in inflammatory bowel disease: Mechanisms and management","volume":"162","author":"Shah","year":"2022","journal-title":"Gastroenterology"},{"key":"B266","doi-asserted-by":"publisher","first-page":"G7","DOI":"10.1152\/ajpgi.00079.2004","article-title":"Inflammation and Cancer IV. Colorectal cancer in inflammatory bowel disease: the role of inflammation","volume":"287","author":"Itzkowitz","year":"2004","journal-title":"Am J Physiol Gastrointest Liver Physiol"},{"key":"B267","doi-asserted-by":"publisher","first-page":"1694","DOI":"10.1053\/j.gastro.2020.12.059","article-title":"Colonic epithelial-derived Selenoprotein P is the source for antioxidant-mediated protection in colitis-associated cancer","volume":"160","author":"Short","year":"2021","journal-title":"Gastroenterology"},{"key":"B268","doi-asserted-by":"publisher","DOI":"10.1053\/j.gastro.2011.06.056","article-title":"Notch1 regulates the effects of matrix metalloproteinase-9 on colitis-associated cancer in mice","volume":"141","author":"Garg","year":"2011","journal-title":"Gastroenterology"},{"key":"B269","doi-asserted-by":"publisher","DOI":"10.1101\/cshperspect.a012559","article-title":"DNA base damage by reactive oxygen species, oxidizing agents, and UV radiation","volume":"5","author":"Cadet","year":"2013","journal-title":"Cold Spring Harb Perspect Biol"},{"key":"B270","doi-asserted-by":"publisher","DOI":"10.1053\/j.gastro.2018.11.036","article-title":"Histone demethylase JMJD2D interacts with \u03b2-catenin to induce transcription and activate colorectal cancer cell proliferation and tumor growth in mice","volume":"156","author":"Peng","year":"2019","journal-title":"Gastroenterology"},{"key":"B271","doi-asserted-by":"publisher","DOI":"10.1158\/0008-5472.Can-14-2036","article-title":"Suppressing TGF\u03b2 signaling in regenerating epithelia in an inflammatory microenvironment is sufficient to cause invasive intestinal cancer","volume":"75","author":"Oshima","year":"2015","journal-title":"Cancer Res"},{"key":"B272","doi-asserted-by":"publisher","DOI":"10.1016\/j.bbrc.2011.08.029","article-title":"Protein kinase D1 mediates synergistic MMP-3 expression induced by TNF-\u03b1 and bradykinin in human colonic myofibroblasts","volume":"413","author":"Yoo","year":"2011","journal-title":"Biochem Biophys Res Commun"},{"key":"B273","doi-asserted-by":"publisher","DOI":"10.1158\/1078-0432.CCR-0431-03","article-title":"Subepithelial myofibroblasts express cyclooxygenase-2 in colorectal tubular adenomas","volume":"10","author":"Adegboyega","year":"2004","journal-title":"Clin Cancer Res"},{"key":"B274","doi-asserted-by":"publisher","DOI":"10.1002\/ijc.22729","article-title":"Interferon-gamma regulation of TNF alpha-induced matrix metalloproteinase 3 expression and migration of human glioma T98G cells","volume":"121","author":"Cheng","year":"2007","journal-title":"Int J Cancer"},{"key":"B275","doi-asserted-by":"publisher","first-page":"59","DOI":"10.1002\/mc.10049","article-title":"Matrilysin (Matrix metalloproteinase-7) expression in ulcerative colitis-related tumorigenesis","volume":"34","author":"Newell","year":"2002","journal-title":"Mol Carcinog"},{"key":"B276","doi-asserted-by":"publisher","first-page":"22","DOI":"10.7178\/ig.29","article-title":"Role of matrix metalloproteinases in Inflammation\/Colitis-associated colon cancer","volume":"2","author":"Walter","year":"2013","journal-title":"ImmunoGastroenterology"},{"key":"B277","article-title":"Expression of Tcf-4, MMP-7 and survivin in colorectal cancer and its clinical significance","volume":"46","author":"Ou","year":"2015","journal-title":"J Sichuan Univ Med Sci Edition"},{"key":"B278","doi-asserted-by":"publisher","DOI":"10.1111\/cas.12745","article-title":"FGF-1\/-3\/FGFR4 signaling in cancer-associated fibroblasts promotes tumor progression in colon cancer through ERK and MMP-7","volume":"106","author":"Bai","year":"2015","journal-title":"Cancer Sci"},{"key":"B279","doi-asserted-by":"publisher","DOI":"10.18632\/oncotarget.13406","article-title":"Epithelial derived-matrix metalloproteinase (MMP9) exhibits a novel defensive role of tumor suppressor in colitis associated cancer by activating MMP9-Notch1-ARF-P53 axis","volume":"8","author":"Walter","year":"2017","journal-title":"Oncotarget"},{"key":"B280","doi-asserted-by":"publisher","DOI":"10.1038\/sj.onc.1205045","article-title":"Low plasma levels of matrix metalloproteinase 9 permit increased tumor angiogenesis","volume":"21","author":"Pozzi","year":"2002","journal-title":"Oncogene"},{"key":"B281","doi-asserted-by":"publisher","DOI":"10.1242\/dmm.005801","article-title":"MMP9 is protective against lethal inflammatory mass lesions in the mouse colon","volume":"4","author":"Hald","year":"2011","journal-title":"Dis Model Mech"},{"key":"B282","doi-asserted-by":"publisher","DOI":"10.18632\/oncotarget.21841","article-title":"Matrix metalloproteinase MMP9 maintains epithelial barrier function and preserves mucosal lining in colitis associated cancer","volume":"8","author":"Pujada","year":"2017","journal-title":"Oncotarget"},{"key":"B283","doi-asserted-by":"publisher","first-page":"53","DOI":"10.1016\/j.canlet.2021.12.033","article-title":"Elevated MMP10\/13 mediated barrier disruption and NF-\u03baB activation aggravate colitis and colon tumorigenesis in both individual or full miR-148\/152 family knockout mice","volume":"529","author":"Tang","year":"2022","journal-title":"Cancer Lett"},{"key":"B284","doi-asserted-by":"publisher","DOI":"10.1158\/1940-6207.CAPR-10-0033","article-title":"Novel application of proton pump inhibitor for the prevention of colitis-induced colorectal carcinogenesis beyond acid suppression","volume":"3","author":"Kim","year":"2010","journal-title":"Cancer Prev Res"},{"key":"B285","doi-asserted-by":"publisher","DOI":"10.1158\/1940-6207.CAPR-09-0272","article-title":"Prevention of colitis-associated carcinogenesis with infliximab","volume":"3","author":"Kim","year":"2010","journal-title":"Cancer Prev Res"},{"key":"B286","doi-asserted-by":"publisher","DOI":"10.5009\/gnl.2010.4.4.488","article-title":"Near-infrared fluorescence imaging using a protease-specific probe for the detection of colon tumors","volume":"4","author":"Yoon","year":"2010","journal-title":"Gut Liver"},{"key":"B287","doi-asserted-by":"publisher","DOI":"10.1016\/j.biopha.2014.07.006","article-title":"The PI3K\/Akt pathway in colitis associated colon cancer and its chemoprevention with celecoxib, a Cox-2 selective inhibitor","volume":"68","author":"Setia","year":"2014","journal-title":"BioMed Pharmacother"},{"key":"B288","doi-asserted-by":"publisher","DOI":"10.1038\/onc.2013.102","article-title":"Inactivation of TGF-\u03b2 signaling and loss of PTEN cooperate to induce colon cancer in vivo","volume":"33","author":"Yu","year":"2014","journal-title":"Oncogene"},{"key":"B289","doi-asserted-by":"publisher","first-page":"1680","DOI":"10.1053\/j.gastro.2009.01.066","article-title":"TGF-\u03b2 receptor inactivation and mutant kras induce intestinal neoplasms in mice via a \u03b2-catenin-independent pathway","volume":"136","author":"Trobridge","year":"2009","journal-title":"Gastroenterology"},{"key":"B290","doi-asserted-by":"publisher","DOI":"10.1002\/emmm.201201773","article-title":"Antimicrobial peptides and gut microbiota in homeostasis and pathology","volume":"5","author":"Ostaff","year":"2013","journal-title":"EMBO Mol Med"},{"key":"B291","doi-asserted-by":"publisher","DOI":"10.1128\/CMR.19.2.315-337.2006","article-title":"The front line of enteric host defense against unwelcome intrusion of harmful microorganisms: Mucins, antimicrobial peptides, and microbiota","volume":"19","author":"Li\u00e9vin-Le Moal","year":"2006","journal-title":"Clin Microbiol Rev"},{"key":"B292","doi-asserted-by":"publisher","DOI":"10.1038\/nri3228","article-title":"Epithelial antimicrobial defence of the skin and intestine","volume":"12","author":"Gallo","year":"2012","journal-title":"Nat Rev Immunol"},{"key":"B293","doi-asserted-by":"publisher","DOI":"10.18632\/oncotarget.3027","article-title":"Up-regulation of matrix metalloproteinases in a mouse model of chemically induced colitis-associated cancer: The role of micrornas","volume":"6","author":"Ai","year":"2015","journal-title":"Oncotarget"},{"key":"B294","doi-asserted-by":"publisher","DOI":"10.1002\/ijc.26435","article-title":"Serum MMP-8 levels increase in colorectal cancer and correlate with disease course and inflammatory properties of primary tumors","volume":"131","author":"V\u00e4yrynen","year":"2012","journal-title":"Int J Cancer"},{"key":"B295","doi-asserted-by":"publisher","DOI":"10.1016\/j.cytogfr.2006.04.001","article-title":"Matrix metalloproteinase-8: Cleavage can be decisive","volume":"17","author":"Van Lint","year":"2006","journal-title":"Cytokine Growth Factor Rev"},{"key":"B296","doi-asserted-by":"publisher","DOI":"10.4049\/jimmunol.175.11.7642","article-title":"Resistance of collagenase-2 (Matrix metalloproteinase-8)-Deficient mice to TNF-induced lethal hepatitis","volume":"175","author":"Van Lint","year":"2005","journal-title":"J Immunol"},{"key":"B297","doi-asserted-by":"publisher","DOI":"10.2217\/imt-2021-0298","article-title":"Multiple high-grade and rare immune-related adverse events in a colon cancer patient with genomic and cytokine profiling","volume":"14","author":"Tyan","year":"2022","journal-title":"Immunotherapy"},{"key":"B298","doi-asserted-by":"publisher","DOI":"10.1186\/s12876-014-0189-7","article-title":"Intestinal permeability\u2013a new target for disease prevention and therapy","volume":"14","author":"Bischoff","year":"2014","journal-title":"BMC Gastroenterol"},{"key":"B299","doi-asserted-by":"publisher","DOI":"10.3389\/fimmu.2016.00054","article-title":"Innate sensing of the gut microbiota: Modulation of inflammatory and autoimmune diseases","volume":"7","author":"Ignacio","year":"2016","journal-title":"Front Immunol"},{"key":"B300","doi-asserted-by":"publisher","DOI":"10.1155\/2014\/149185","article-title":"Chronic inflammation and cytokines in the tumor microenvironment","volume":"2014","author":"Landskron","year":"2014","journal-title":"J Immunol Res"},{"key":"B301","doi-asserted-by":"publisher","DOI":"10.1038\/nri3896","article-title":"Emerging cytokine networks in colorectal cancer","volume":"15","author":"West","year":"2015","journal-title":"Nat Rev Immunol"},{"key":"B302","doi-asserted-by":"publisher","DOI":"10.1038\/s41416-018-0136-4","article-title":"High-serum MMP-8 levels are associated with decreased survival and systemic inflammation in colorectal cancer","volume":"119","author":"Sirni\u00f6","year":"2018","journal-title":"Br J Cancer"},{"key":"B303","doi-asserted-by":"publisher","DOI":"10.1016\/j.carbpol.2016.02.077","article-title":"Chitosan oligosaccharide suppresses tumor progression in a mouse model of colitis-associated colorectal cancer through AMPK activation and suppression of NF-\u03baB and mTOR signaling","volume":"145","author":"Mattaveewong","year":"2016","journal-title":"Carbohydr Polymers"},{"key":"B304","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0051848","article-title":"Crucial involvement of tumor-associated neutrophils in the regulation of chronic colitis-associated carcinogenesis in mice","volume":"7","author":"Shang","year":"2012","journal-title":"PLos One"},{"key":"B305","doi-asserted-by":"publisher","DOI":"10.1038\/33340","article-title":"Chemokines and leukocyte traffic","volume":"392","author":"Baggiolini","year":"1998","journal-title":"Nature"},{"key":"B306","doi-asserted-by":"publisher","DOI":"10.1038\/nri1841","article-title":"Neutrophil serine proteases: Specific regulators of inflammation","volume":"6","author":"Pham","year":"2006","journal-title":"Nat Rev Immunol"},{"key":"B307","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.270.45.27348","article-title":"The functional role of the elr motif in CXC chemokine-mediated angiogenesis","volume":"270","author":"Strieter","year":"1995","journal-title":"J Biol Chem"},{"key":"B308","doi-asserted-by":"publisher","DOI":"10.1007\/s00535-007-2091-3","article-title":"Inflammatory responses induced by interleukin-17 family members in human colonic subepithelial myofibroblasts","volume":"42","author":"Yagi","year":"2007","journal-title":"J Gastroenterol"},{"key":"B309","doi-asserted-by":"publisher","DOI":"10.1136\/gut.2006.093187","article-title":"Control of matrix metalloproteinase production in human intestinal fibroblasts by interleukin 21","volume":"55","author":"Monteleone","year":"2006","journal-title":"Gut"},{"key":"B310","doi-asserted-by":"publisher","DOI":"10.2147\/dddt.S79431","article-title":"Human colon carcinogenesis is associated with increased interleukin-17-Driven inflammatory responses","volume":"9","author":"Xie","year":"2015","journal-title":"Drug design Dev Ther"},{"key":"B311","doi-asserted-by":"publisher","DOI":"10.1152\/ajpgi.00494.2001","article-title":"Il-17 stimulates inflammatory responses via nf-\u03baB and MAP kinase pathways in human colonic myofibroblasts","volume":"282","author":"Hata","year":"2002","journal-title":"Am J Physiol Gastrointestinal Liver Physiol"},{"key":"B312","first-page":"B4973","article-title":"Development, validation and implementation of an in vitro model for the study of metabolic and immune function in normal and inflamed human colonic epithelium","volume":"62","author":"Pedersen","year":"2015","journal-title":"Danish Med J"},{"key":"B313","doi-asserted-by":"publisher","DOI":"10.1093\/ecco-jcc\/jjv123","article-title":"Fragments of citrullinated and MMP-degraded vimentin and MMP-degraded type iii collagen are novel serological biomarkers to differentiate Crohn's disease from ulcerative colitis","volume":"9","author":"Mortensen","year":"2015","journal-title":"J Crohns Colitis"},{"key":"B314","doi-asserted-by":"publisher","DOI":"10.1038\/bjc.2012.80","article-title":"MMP-2 and MMP-9 in normal mucosa are independently associated with outcome of colorectal cancer patients","volume":"106","author":"Langers","year":"2012","journal-title":"Br J Cancer"},{"key":"B315","doi-asserted-by":"publisher","DOI":"10.1002\/ijc.22799","article-title":"Serum matrix metalloproteinase 7 levels identifies poor prognosis advanced colorectal cancer patients","volume":"121","author":"Maurel","year":"2007","journal-title":"Int J Cancer"},{"key":"B316","doi-asserted-by":"publisher","DOI":"10.1245\/s10434-009-0405-9","article-title":"Serum matrilysin levels predict outcome in curatively resected colorectal cancer patients","volume":"16","author":"Mart\u00ednez-Fernandez","year":"2009","journal-title":"Ann Surg Oncol"},{"key":"B317","doi-asserted-by":"publisher","DOI":"10.1007\/s00464-014-3612-9","article-title":"Minimally invasive colorectal resection is associated with significantly elevated levels of plasma matrix metalloproteinase 3 (MMP-3) during the first month after surgery which may promote the growth of residual metastases","volume":"28","author":"Shantha Kumara","year":"2014","journal-title":"Surg Endosc"},{"key":"B318","doi-asserted-by":"publisher","DOI":"10.1023\/a:1011183905848","article-title":"Phase I study of the matrix metalloproteinase inhibitor, BAY12-9566","volume":"12","author":"Erlichman","year":"2001","journal-title":"Ann Oncol"},{"key":"B319","doi-asserted-by":"publisher","DOI":"10.1007\/s002800100330","article-title":"Phase I trial of the matrix metalloproteinase inhibitor BAY12-9566 in patients with advanced solid tumors","volume":"48","author":"Heath","year":"2001","journal-title":"Cancer Chemother Pharmacol"},{"key":"B320","doi-asserted-by":"publisher","DOI":"10.1158\/1078-0432.ccr-1183-02","article-title":"A phase I study of oral bms-275291, a novel nonhydroxamate sheddase-sparing matrix metalloproteinase inhibitor, in patients with advanced or metastatic cancer","volume":"10","author":"Rizvi","year":"2004","journal-title":"Clin Cancer Res"},{"key":"B321","doi-asserted-by":"publisher","first-page":"496","DOI":"10.1177\/1534735413485417","article-title":"Effect of conjugated linoleic acid supplementation on inflammatory factors and matrix metalloproteinase enzymes in rectal cancer patients undergoing chemoradiotherapy","volume":"12","author":"Mohammadzadeh","year":"2013","journal-title":"Integr Cancer Ther"},{"key":"B322","doi-asserted-by":"publisher","DOI":"10.1039\/c7fo01898c","article-title":"Effect of fisetin supplementation on inflammatory factors and matrix metalloproteinase enzymes in colorectal cancer patients","volume":"9","author":"Farsad-Naeimi","year":"2018","journal-title":"Food Funct"},{"key":"B323","doi-asserted-by":"publisher","DOI":"10.1016\/j.bbamcr.2017.06.009","article-title":"Next generation matrix metalloproteinase inhibitors - novel strategies bring new prospects","volume":"1864","author":"Levin","year":"2017","journal-title":"Biochim Biophys Acta Mol Cell Res"},{"key":"B324","doi-asserted-by":"publisher","DOI":"10.1038\/sj.onc.1204097","article-title":"Critical appraisal of the use of matrix metalloproteinase inhibitors in cancer treatment","volume":"19","author":"Zucker","year":"2000","journal-title":"Oncogene"},{"key":"B325","doi-asserted-by":"publisher","DOI":"10.1016\/j.impact.2021.100293","article-title":"Matrix metalloproteinase inhibitors (MMPIS) as attractive therapeutic targets: Recent progress and current challenges","volume":"21","author":"Shi","year":"2021","journal-title":"NanoImpact"},{"key":"B326","doi-asserted-by":"publisher","DOI":"10.1158\/1535-7163.Mct-17-0646","article-title":"Matrix metalloproteinase inhibitors in cancer therapy: Turning past failures into future successes","volume":"17","author":"Winer","year":"2018","journal-title":"Mol Cancer Ther"}],"container-title":["Frontiers in Immunology"],"original-title":[],"link":[{"URL":"https:\/\/www.frontiersin.org\/articles\/10.3389\/fimmu.2022.1093990\/full","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,1,26]],"date-time":"2023-01-26T14:28:59Z","timestamp":1674743339000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.frontiersin.org\/articles\/10.3389\/fimmu.2022.1093990\/full"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2023,1,19]]},"references-count":326,"alternative-id":["10.3389\/fimmu.2022.1093990"],"URL":"https:\/\/doi.org\/10.3389\/fimmu.2022.1093990","relation":{},"ISSN":["1664-3224"],"issn-type":[{"value":"1664-3224","type":"electronic"}],"subject":[],"published":{"date-parts":[[2023,1,19]]},"article-number":"1093990"}}