{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,12]],"date-time":"2025-10-12T03:56:01Z","timestamp":1760241361927,"version":"build-2065373602"},"reference-count":252,"publisher":"MDPI AG","issue":"2","license":[{"start":{"date-parts":[[2018,2,2]],"date-time":"2018-02-02T00:00:00Z","timestamp":1517529600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"John Turner Cancer Research Funds"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>Approximately sixty per cent of ovarian cancer patients die within the first five years of diagnosis due to recurrence associated with chemoresistance. The metzincin family of metalloproteinases is enzymes involved in matrix remodeling in response to normal physiological changes and diseased states. Recently, there has been a mounting awareness of these proteinases and their endogenous inhibitors, the tissue inhibitors of metalloproteinases (TIMPs), as superb modulators of cellular communication and signaling regulating key biological processes in cancer progression. This review investigates the role of metzincins and their inhibitors in ovarian cancer. We propose that understanding the metzincins and TIMP biology in ovarian cancer may provide valuable insights in combating ovarian cancer progression and chemoresistance-mediated recurrence in patients.<\/jats:p>","DOI":"10.3390\/ijms19020450","type":"journal-article","created":{"date-parts":[[2018,2,2]],"date-time":"2018-02-02T08:25:30Z","timestamp":1517559930000},"page":"450","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":13,"title":["The Many Facets of Metzincins and Their Endogenous Inhibitors: Perspectives on Ovarian Cancer Progression"],"prefix":"10.3390","volume":"19","author":[{"given":"Ruth","family":"Escalona","sequence":"first","affiliation":[{"name":"Department of Obstetrics and Gynaecology, University of Melbourne, Parkville, VIC 3052, Australia"},{"name":"The Hudson Institute of Medical Research, Clayton, VIC 3168, Australia"},{"name":"Fiona Elsey Cancer Research Institute, Ballarat, VIC 3353, Australia"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Emily","family":"Chan","sequence":"additional","affiliation":[{"name":"Department of Obstetrics and Gynaecology, University of Melbourne, Parkville, VIC 3052, Australia"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"George","family":"Kannourakis","sequence":"additional","affiliation":[{"name":"Fiona Elsey Cancer Research Institute, Ballarat, VIC 3353, Australia"},{"name":"Federation University Australia, Ballarat, VIC 3010, Australia"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jock","family":"Findlay","sequence":"additional","affiliation":[{"name":"Department of Obstetrics and Gynaecology, University of Melbourne, Parkville, VIC 3052, Australia"},{"name":"The Hudson Institute of Medical Research, Clayton, VIC 3168, Australia"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Nuzhat","family":"Ahmed","sequence":"additional","affiliation":[{"name":"Department of Obstetrics and Gynaecology, University of Melbourne, Parkville, VIC 3052, Australia"},{"name":"The Hudson Institute of Medical Research, Clayton, VIC 3168, Australia"},{"name":"Fiona Elsey Cancer Research Institute, Ballarat, VIC 3353, Australia"},{"name":"Federation University Australia, Ballarat, VIC 3010, Australia"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"1968","published-online":{"date-parts":[[2018,2,2]]},"reference":[{"key":"ref_1","first-page":"119","article-title":"Structural and functional characteristics and properties of metzincins","volume":"2","author":"Balaban","year":"2012","journal-title":"Biochemistry"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"15337","DOI":"10.1523\/JNEUROSCI.3467-10.2010","article-title":"Metzincin Proteases and their Inhibitors, Foes or Friends in Nervous System Physiology?","volume":"30","author":"Rivera","year":"2010","journal-title":"J. Neurosci. Off. J. Soc. Neurosci."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"225","DOI":"10.3322\/caac.20006","article-title":"Cancer statistics, 2009","volume":"59","author":"Jemal","year":"2009","journal-title":"CA Cancer J. Clin."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"1604","DOI":"10.1038\/s41467-017-01781-0","article-title":"Decoding critical long non-coding RNA in ovarian cancer epithelial-to-mesenchymal transition","volume":"8","author":"Mitra","year":"2017","journal-title":"Nat. Commun."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"581","DOI":"10.1002\/jcp.21240","article-title":"Epithelial-mesenchymal interconversions in normal ovarian surface epithelium and ovarian carcinomas: An exception to the norm","volume":"213","author":"Ahmed","year":"2007","journal-title":"J. Cell. Physiol."},{"key":"ref_6","first-page":"255","article-title":"Ovarian surface epithelium: Biology, endocrinology, and pathology","volume":"22","author":"Auersperg","year":"2001","journal-title":"Endocr. Rev."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"5284","DOI":"10.1200\/JCO.2008.18.1107","article-title":"New insights into the pathogenesis of serous ovarian cancer and its clinical impact","volume":"26","author":"Levanon","year":"2008","journal-title":"J. Clin. Oncol."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"4160","DOI":"10.1200\/JCO.2008.16.4814","article-title":"Serous tubal intraepithelial carcinoma: Its potential role in primary peritoneal serous carcinoma and serous cancer prevention","volume":"26","author":"Carlson","year":"2008","journal-title":"J. Clin. Oncol."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"161","DOI":"10.1097\/01.pas.0000213335.40358.47","article-title":"Intraepithelial carcinoma of the fimbria and pelvic serous carcinoma: Evidence for a causal relationship","volume":"31","author":"Kindelberger","year":"2007","journal-title":"Am. J. Surg. Pathol."},{"key":"ref_10","doi-asserted-by":"crossref","unstructured":"Klymenko, Y., Kim, O., and Stack, M.S. (2017). Complex Determinants of Epithelial: Mesenchymal Phenotypic Plasticity in Ovarian Cancer. Cancers, 9.","DOI":"10.3390\/cancers9080104"},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"44","DOI":"10.1111\/his.12046","article-title":"Fallopian tube precursors of ovarian low- and high-grade serous neoplasms","volume":"62","author":"Vang","year":"2013","journal-title":"Histopathology"},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"3025","DOI":"10.1158\/0008-5472.CAN-04-3931","article-title":"Stem and progenitor-like cells contribute to the aggressive behavior of human epithelial ovarian cancer","volume":"65","author":"Bapat","year":"2005","journal-title":"Cancer Res."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"4311","DOI":"10.1158\/0008-5472.CAN-08-0364","article-title":"Identification and characterization of ovarian cancer-initiating cells from primary human tumors","volume":"68","author":"Zhang","year":"2008","journal-title":"Cancer Res."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"241","DOI":"10.1038\/nature11979","article-title":"Ovarian surface epithelium at the junction area contains a cancer-prone stem cell niche","volume":"495","author":"Hwang","year":"2013","journal-title":"Nature"},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"11154","DOI":"10.1073\/pnas.0603672103","article-title":"Ovarian cancer side population defines cells with stem cell-like characteristics and Mullerian Inhibiting Substance responsiveness","volume":"103","author":"Szotek","year":"2006","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"843","DOI":"10.1111\/j.1432-0436.2008.00268.x","article-title":"Putative stem cells with an embryonic character isolated from the ovarian surface epithelium of women with no naturally present follicles and oocytes","volume":"76","author":"Zech","year":"2008","journal-title":"Differentiation"},{"key":"ref_17","doi-asserted-by":"crossref","unstructured":"Bowen, N.J., Walker, L.D., Matyunina, L.V., Logani, S., Totten, K.A., Benigno, B.B., and McDonald, J.F. (2009). Gene expression profiling supports the hypothesis that human ovarian surface epithelia are multipotent and capable of serving as ovarian cancer initiating cells. BMC Med. Genom., 2.","DOI":"10.1186\/1755-8794-2-71"},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"46","DOI":"10.1186\/1479-5876-7-46","article-title":"Human fallopian tube: A new source of multipotent adult mesenchymal stem cells discarded in surgical procedures","volume":"7","author":"Jazedje","year":"2009","journal-title":"J. Transl. Med."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"1103","DOI":"10.1038\/onc.2009.402","article-title":"Primary ex vivo cultures of human fallopian tube epithelium as a model for serous ovarian carcinogenesis","volume":"29","author":"Levanon","year":"2010","journal-title":"Oncogene"},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"625","DOI":"10.1038\/nrm4056","article-title":"Ovary and fimbrial stem cells: Biology, niche and cancer origins","volume":"16","author":"Ng","year":"2015","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"719","DOI":"10.1038\/nrc3144","article-title":"Rethinking ovarian cancer: Recommendations for improving outcomes","volume":"11","author":"Vaughan","year":"2011","journal-title":"Nat. Rev. Cancer"},{"key":"ref_22","first-page":"151","article-title":"Pathogenesis of ovarian cancer: Lessons from morphology and molecular biology and their clinical implications","volume":"27","author":"Kurman","year":"2008","journal-title":"Int. J. Gynecol. Pathol."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"932371","DOI":"10.1155\/2010\/932371","article-title":"Ovarian cancer pathogenesis: A model in evolution","volume":"2010","author":"Karst","year":"2010","journal-title":"J. Oncol."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"7547","DOI":"10.1073\/pnas.1017300108","article-title":"Modeling high-grade serous ovarian carcinogenesis from the fallopian tube","volume":"108","author":"Karst","year":"2011","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"277","DOI":"10.1007\/s12672-010-0054-2","article-title":"Microenvironment and pathogenesis of epithelial ovarian cancer","volume":"1","author":"Saad","year":"2010","journal-title":"Horm. Cancer"},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"256","DOI":"10.3389\/fonc.2013.00256","article-title":"Getting to know ovarian cancer ascites: Opportunities for targeted therapy-based translational research","volume":"3","author":"Ahmed","year":"2013","journal-title":"Front. Oncol."},{"key":"ref_27","first-page":"490","article-title":"An Electron Microscopic Study of the Invasion of Ascites Tumor Cells into the Abdominal Wall","volume":"25","author":"Birbeck","year":"1965","journal-title":"Cancer Res."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"110","DOI":"10.1016\/j.mam.2013.06.002","article-title":"Ovarian cancer stem cells: Molecular concepts and relevance as therapeutic targets","volume":"39","author":"Ahmed","year":"2014","journal-title":"Mol. Aspects Med."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1016\/j.ygyno.2008.11.032","article-title":"Multicellular spheroids in ovarian cancer metastases: Biology and pathology","volume":"113","author":"Shield","year":"2009","journal-title":"Gynecol. Oncol."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1007\/s12307-012-0104-0","article-title":"Soiling the seed: Microenvironment and epithelial mesenchymal plasticity","volume":"5","author":"Haviv","year":"2012","journal-title":"Cancer Microenviron."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"374","DOI":"10.1002\/jcp.21223","article-title":"Epithelial\u2014mesenchymal and mesenchymal\u2014epithelial transitions in carcinoma progression","volume":"213","author":"Hugo","year":"2007","journal-title":"J. Cell. Physiol."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"268","DOI":"10.2174\/156800910791190175","article-title":"Epithelial mesenchymal transition and cancer stem cell-like phenotypes facilitate chemoresistance in recurrent ovarian cancer","volume":"10","author":"Ahmed","year":"2010","journal-title":"Curr. Cancer Drug Targets"},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"24","DOI":"10.1186\/1476-4598-12-24","article-title":"Short-term single treatment of chemotherapy results in the enrichment of ovarian cancer stem cell-like cells leading to an increased tumor burden","volume":"12","author":"Abubaker","year":"2013","journal-title":"Mol. Cancer"},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"C1532","DOI":"10.1152\/ajpcell.00478.2005","article-title":"Molecular pathways regulating EGF-induced epithelio-mesenchymal transition in human ovarian surface epithelium","volume":"290","author":"Ahmed","year":"2006","journal-title":"Am. J. Physiol. Cell Physiol."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"161","DOI":"10.1007\/s10585-010-9315-2","article-title":"Mesenchymal-to-epithelial transition determinants as characteristics of ovarian carcinoma effusions","volume":"27","author":"Elloul","year":"2010","journal-title":"Clin. Exp. Metastasis"},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"415","DOI":"10.1038\/nrc2131","article-title":"Snail, Zeb and bHLH factors in tumour progression: An alliance against the epithelial phenotype?","volume":"7","author":"Peinado","year":"2007","journal-title":"Nat. Rev. Cancer"},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"a005058","DOI":"10.1101\/cshperspect.a005058","article-title":"Extracellular matrix degradation and remodeling in development and disease","volume":"3","author":"Lu","year":"2011","journal-title":"Cold Spring Harb. Perspect. Biol."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"800","DOI":"10.1038\/nrc2228","article-title":"Emerging roles of proteases in tumour suppression","volume":"7","author":"Matrisian","year":"2007","journal-title":"Nat. Rev. Cancer"},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"31493","DOI":"10.1074\/jbc.R109.052340","article-title":"A disintegrin-like and metalloprotease (reprolysin-type) with thrombospondin type 1 motif (ADAMTS) superfamily: Functions and mechanisms","volume":"284","author":"Apte","year":"2009","journal-title":"J. Biol. Chem."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.matbio.2015.04.005","article-title":"Metalloproteinases: A parade of functions in matrix biology and an outlook for the future","volume":"44\u201346","author":"Apte","year":"2015","journal-title":"Matrix Biol."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"20","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":"ref_42","doi-asserted-by":"crossref","first-page":"289","DOI":"10.1007\/s10555-008-9129-8","article-title":"MT4-(MMP17) and MT6-MMP (MMP25), A unique set of membrane-anchored matrix metalloproteinases: Properties and expression in cancer","volume":"27","author":"Sohail","year":"2008","journal-title":"Cancer Metastasis Rev."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"221","DOI":"10.1038\/nrm2125","article-title":"Matrix metalloproteinases and the regulation of tissue remodelling","volume":"8","author":"Ewald","year":"2007","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"367","DOI":"10.1016\/j.jceh.2017.09.004","article-title":"Matrix Metalloproteinases (MMPs) in Liver Diseases","volume":"7","author":"Naim","year":"2017","journal-title":"J. Clin. Exp. Hepatol."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1016\/j.ejphar.2005.12.082","article-title":"Matrix metalloproteinases (MMPs) and tissue inhibitors of MMPs in the respiratory tract: Potential implications in asthma and other lung diseases","volume":"533","author":"Gueders","year":"2006","journal-title":"Eur. J. Pharmacol."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"12","DOI":"10.5603\/FHC.2012.0002","article-title":"The role of matrix metalloproteinases (MMPs) and their inhibitors (TIMPs) in the development of esophageal cancer","volume":"50","author":"Groblewska","year":"2012","journal-title":"Folia Histochem. Cytobiol."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1385\/MB:22:1:051","article-title":"Molecular determinants of metalloproteinase substrate specificity: Matrix metalloproteinase substrate binding domains, modules, and exosites","volume":"22","author":"Overall","year":"2002","journal-title":"Mol. Biotechnol."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"473","DOI":"10.1083\/jcb.136.2.473","article-title":"A three-dimensional collagen lattice induces protein kinase C-zeta activity: Role in \u03b12 integrin and collagenase mRNA expression","volume":"136","author":"Xu","year":"1997","journal-title":"J. Cell Biol."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1186\/1476-4598-9-17","article-title":"CXCR4\/SDF1 mediate hypoxia induced chondrosarcoma cell invasion through ERK signaling and increased MMP1 expression","volume":"9","author":"Sun","year":"2010","journal-title":"Mol. Cancer"},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"1086","DOI":"10.1093\/jjco\/hyr108","article-title":"Correlation between MMP1-PAR1 axis and clinical outcome of primary gallbladder carcinoma","volume":"41","author":"Du","year":"2011","journal-title":"Jpn. J. Clin. Oncol."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1186\/1755-1536-3-3","article-title":"Insulin-like growth factor binding protein 5 enhances survival of LX2 human hepatic stellate cells","volume":"3","author":"Sokolovic","year":"2010","journal-title":"Fibrogenesis Tissue Repair"},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"558","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":"ref_53","doi-asserted-by":"crossref","first-page":"649","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":"ref_54","doi-asserted-by":"crossref","first-page":"959","DOI":"10.1157\/13109649","article-title":"Metalloproteases, vascular remodeling and atherothrombotic syndromes","volume":"60","author":"Rodriguez","year":"2007","journal-title":"Rev. Esp. Cardiol."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"477","DOI":"10.1111\/j.1440-1827.2010.02547.x","article-title":"Matrix metalloproteinases, a disintegrin and metalloproteinases, and a disintegrin and metalloproteinases with thrombospondin motifs in non-neoplastic diseases","volume":"60","author":"Shiomi","year":"2010","journal-title":"Pathol. Int."},{"key":"ref_56","doi-asserted-by":"crossref","unstructured":"Giebeler, N., and Zigrino, P. (2016). A Disintegrin and Metalloprotease (ADAM): Historical Overview of Their Functions. Toxins, 8.","DOI":"10.3390\/toxins8040122"},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"6362","DOI":"10.4049\/jimmunol.172.10.6362","article-title":"The transmembrane CXC-chemokine ligand 16 is induced by IFN-\u03b3 and TNF-\u03b1 and shed by the activity of the disintegrin-like metalloproteinase ADAM10","volume":"172","author":"Abel","year":"2004","journal-title":"J. Immunol."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"472","DOI":"10.1016\/j.ejcb.2011.09.003","article-title":"The role of ADAM-mediated shedding in vascular biology","volume":"91","author":"Dreymueller","year":"2012","journal-title":"Eur. J. Cell Biol."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"2594","DOI":"10.1002\/dvdy.22391","article-title":"ADAM10 is essential for early embryonic cardiovascular development","volume":"239","author":"Zhang","year":"2010","journal-title":"Dev. Dyn."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"532","DOI":"10.1016\/j.cellsig.2011.10.004","article-title":"EGF promotes the shedding of soluble E-cadherin in an ADAM10-dependent manner in prostate epithelial cells","volume":"24","author":"Grabowska","year":"2012","journal-title":"Cell Signal."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"332","DOI":"10.1158\/0008-5472.CAN-06-2470","article-title":"ADAM10 inhibition of human CD30 shedding increases specificity of targeted immunotherapy in vitro","volume":"67","author":"Eichenauer","year":"2007","journal-title":"Cancer Res."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"331","DOI":"10.1007\/s11882-007-0050-y","article-title":"CD23, an overlooked regulator of allergic disease","volume":"7","author":"Conrad","year":"2007","journal-title":"Curr. Allergy Asthma Rep."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"6339","DOI":"10.1074\/jbc.M116.746859","article-title":"Ectodomain shedding of the cell adhesion molecule Nectin-4 in ovarian cancer is mediated by ADAM10 and ADAM17","volume":"292","author":"Buchanan","year":"2017","journal-title":"J. Biol. Chem."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"2228","DOI":"10.1016\/j.bbamcr.2017.07.011","article-title":"Role of ADAM10 in intestinal crypt homeostasis and tumorigenesis","volume":"1864","author":"Dempsey","year":"2017","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"176","DOI":"10.1091\/mbc.e06-01-0014","article-title":"Substrate selectivity of epidermal growth factor-receptor ligand sheddases and their regulation by phorbol esters and calcium influx","volume":"18","author":"Horiuchi","year":"2007","journal-title":"Mol. Biol. Cell"},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"11738","DOI":"10.1074\/jbc.M805894200","article-title":"ADAM10, the rate-limiting protease of regulated intramembrane proteolysis of Notch and other proteins, is processed by ADAMs-9, ADAMs-15, and the \u03b3-secretase","volume":"284","author":"Tousseyn","year":"2009","journal-title":"J. Biol. Chem."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"511","DOI":"10.1006\/bbrc.2000.3835","article-title":"ADAM 12-S cleaves IGFBP-3 and IGFBP-5 and is inhibited by TIMP-3","volume":"278","author":"Loechel","year":"2000","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"845","DOI":"10.1515\/BC.2005.099","article-title":"GPCR-induced migration of breast carcinoma cells depends on both EGFR signal transactivation and EGFR-independent pathways","volume":"386","author":"Hart","year":"2005","journal-title":"Biol. Chem."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"60","DOI":"10.1016\/j.virol.2014.02.006","article-title":"Nuclear trafficking of the HIV-1 pre-integration complex depends on the ADAM10 intracellular domain","volume":"454\u2013455","author":"Endsley","year":"2014","journal-title":"Virology"},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"30469","DOI":"10.1074\/jbc.M213157200","article-title":"Catalytic activity of ADAM8, ADAM15, and MDC-L (ADAM28) on synthetic peptide substrates and in ectodomain cleavage of CD23","volume":"278","author":"Fourie","year":"2003","journal-title":"J. Biol. Chem."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"1114","DOI":"10.1093\/emboj\/cdg111","article-title":"TACE is required for the activation of the EGFR by TGF-\u03b1 in tumors","volume":"22","author":"Rojo","year":"2003","journal-title":"EMBO J."},{"key":"ref_72","doi-asserted-by":"crossref","unstructured":"Canault, M., Certel, K., Schatzberg, D., Wagner, D.D., and Hynes, R.O. (2010). The lack of ADAM17 activity during embryonic development causes hemorrhage and impairs vessel formation. PLoS ONE, 5.","DOI":"10.1371\/journal.pone.0013433"},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"342","DOI":"10.1002\/jnr.10737","article-title":"ADAMs family members as amyloid precursor protein \u03b1-secretases","volume":"74","author":"Allinson","year":"2003","journal-title":"J. Neurosci. Res."},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"2319","DOI":"10.2174\/138161209788682398","article-title":"ADAM17 as a therapeutic target in multiple diseases","volume":"15","author":"Arribas","year":"2009","journal-title":"Curr. Pharm. Des."},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1016\/j.semcdb.2014.01.005","article-title":"Amphiregulin","volume":"28","author":"Berasain","year":"2014","journal-title":"Semin. Cell Dev. Biol."},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"906","DOI":"10.1093\/jnci\/djs232","article-title":"Effect of ADAM28 on carcinoma cell metastasis by cleavage of von Willebrand factor","volume":"104","author":"Mochizuki","year":"2012","journal-title":"J. Natl. Cancer Inst."},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"3548","DOI":"10.4049\/jimmunol.0801695","article-title":"Expression of ADAM33 is a novel regulatory mechanism in IL-18-secreted process in gastric cancer","volume":"182","author":"Kim","year":"2009","journal-title":"J. Immunol."},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"32","DOI":"10.1038\/nrm1548","article-title":"ADAMs: Key components in EGFR signalling and development","volume":"6","author":"Blobel","year":"2005","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"641","DOI":"10.1096\/fj.07-8876rev","article-title":"ADAM-15: A metalloprotease that mediates inflammation","volume":"22","author":"Laboisse","year":"2008","journal-title":"FASEB J."},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1186\/s13059-015-0676-3","article-title":"The ADAMTS (A Disintegrin and Metalloproteinase with Thrombospondin motifs) family","volume":"16","author":"Kelwick","year":"2015","journal-title":"Genome Biol."},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1042\/BJ20040424","article-title":"The ADAMTS metalloproteinases","volume":"386","author":"Porter","year":"2005","journal-title":"Biochem. J."},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1016\/j.cca.2009.01.007","article-title":"The role of ADAMs in disease pathophysiology","volume":"403","author":"Duffy","year":"2009","journal-title":"Clin. Chim. Acta"},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1021\/pr100556z","article-title":"Active metalloproteases of the A Disintegrin and Metalloprotease (ADAM) family: Biological function and structure","volume":"10","author":"Klein","year":"2011","journal-title":"J. Proteome Res."},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1016\/S0168-9525(99)01926-5","article-title":"The ADAM gene family: Surface proteins with adhesion and protease activity","volume":"16","author":"Primakoff","year":"2000","journal-title":"Trends Genet."},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"929","DOI":"10.1038\/nrc2459","article-title":"The ADAMs: Signalling scissors in the tumour microenvironment","volume":"8","author":"Murphy","year":"2008","journal-title":"Nat. Rev. Cancer"},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"261","DOI":"10.1006\/bbrc.2000.3295","article-title":"Trafficking of human ADAM 12-L: Retention in the trans-Golgi network","volume":"275","author":"Hougaard","year":"2000","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1042\/bj3480021","article-title":"Cloning and characterization of ADAM28, evidence for autocatalytic pro-domain removal and for cell surface localization of mature ADAM28","volume":"348","author":"Howard","year":"2000","journal-title":"Biochem. J."},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1101\/gad.1039703","article-title":"The ADAMs family of metalloproteases: Multidomain proteins with multiple functions","volume":"17","author":"Seals","year":"2003","journal-title":"Genes Dev."},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"914","DOI":"10.1212\/WNL.0b013e31824c4728","article-title":"ADAM proteins, their ligands, and clinical implications","volume":"78","author":"Benarroch","year":"2012","journal-title":"Neurology"},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"1192","DOI":"10.1161\/CIRCRESAHA.107.169805","article-title":"ADAM10 regulates endothelial permeability and T cell transmigrstion by proteolysis of vascular endothelial cadherin","volume":"102","author":"Schulz","year":"2008","journal-title":"Circ. Res."},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"30475","DOI":"10.1074\/jbc.M103673200","article-title":"A dual signaling cascade that regulates the ectodomain shedding of heparin-binding epidermal growth factor-like growth factor","volume":"276","author":"Umata","year":"2001","journal-title":"J. Biol. Chem."},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"221","DOI":"10.1083\/jcb.200112026","article-title":"The metalloprotease Kuzbanian (ADAM-10) mediates transactivation of EGF receptor by G protein-coupled receptors","volume":"158","author":"Yan","year":"2002","journal-title":"J. Cell. Biol."},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1016\/j.febslet.2006.11.074","article-title":"Ectodomain shedding of the EGF-receptor ligand eigen is mediated by ADAM-17","volume":"581","author":"Sahin","year":"2007","journal-title":"FEBS Lett."},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"8135","DOI":"10.1158\/0008-5472.CAN-04-0811","article-title":"Heparin-binding EGF-like growth factor is a promising target for ovarian cancer therapy","volume":"64","author":"Miyamoto","year":"2004","journal-title":"Cancer Res."},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"1908","DOI":"10.2174\/1389450117666160727143618","article-title":"Targeting ADAM17 Sheddase Activity in Cancer","volume":"17","author":"Rossello","year":"2016","journal-title":"Curr. Drug Targets."},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"26059","DOI":"10.1074\/jbc.M115.649509","article-title":"Shedding of Endogenous Interleukin-6 Receptor (IL-6R) Is Governed by A Disintegrin and Metalloproteinase (ADAM) Proteases while a Full-length IL-6R Isoform Localizes to Circulating Microvesicles","volume":"290","author":"Schumacher","year":"2015","journal-title":"J. Biol. Chem."},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"3758","DOI":"10.1038\/onc.2010.130","article-title":"Novel alternatively spliced ADAM8 isoforms contribute to the aggressive bone metastatic phenotype of lung cancer","volume":"29","author":"Hernandez","year":"2010","journal-title":"Oncogene"},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"720","DOI":"10.2174\/156800908786733478","article-title":"ADAM proteins-therapeutic potential in cancer","volume":"8","author":"Lu","year":"2008","journal-title":"Curr. Cancer Drug Targets"},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"579","DOI":"10.1242\/jcs.112.4.579","article-title":"Interaction of metargidin (ADAM-15) with \u03b1v\u03b23 and \u03b15\u03b21 integrins on different haemopoietic cells","volume":"112","author":"Nath","year":"1999","journal-title":"J. Cell Sci."},{"key":"ref_100","first-page":"851","article-title":"A mechanism for modulation of cellular responses to VEGF: Activation of the integrins","volume":"6","author":"Byzova","year":"2000","journal-title":"Mol. Cell"},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"6238","DOI":"10.1038\/sj.onc.1210429","article-title":"Prostate cancer specific integrin \u03b1v\u03b23 modulates bone metastatic growth and tissue remodeling","volume":"26","author":"McCabe","year":"2007","journal-title":"Oncogene"},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"275","DOI":"10.1083\/jcb.131.2.275","article-title":"ADAM, a novel family of membrane proteins containing a Disintegrin and Metalloprotease domain: Multipotential functions in cell-cell and cell-matrix interactions","volume":"131","author":"Wolfsberg","year":"1995","journal-title":"J. Cell Biol."},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"4728","DOI":"10.1158\/0008-5472.CAN-04-4449","article-title":"A secreted form of ADAM9 promotes carcinoma invasion through tumor-stromal interactions","volume":"65","author":"Mazzocca","year":"2005","journal-title":"Cancer Res."},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"661","DOI":"10.1083\/jcb.200101099","article-title":"Ectodomain shedding of L1 adhesion molecule promotes cell migration by autocrine binding to integrins","volume":"155","author":"Mechtersheimer","year":"2001","journal-title":"J. Cell Biol."},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"3271","DOI":"10.1182\/blood-2005-09-3830","article-title":"ADAM-9 (MDC-9\/meltrin-\u03b3), a member of the a disintegrin and metalloproteinase family, regulates myeloma-cell-induced interleukin-6 production in osteoblasts by direct interaction with the \u03b1v\u03b25 integrin","volume":"107","author":"Karadag","year":"2006","journal-title":"Blood"},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"271","DOI":"10.1042\/bj3550271","article-title":"Transgenic mice with inactive alleles for procollagen N-proteinase (ADAMTS-2) develop fragile skin and male sterility","volume":"355","author":"Li","year":"2001","journal-title":"Biochem. J."},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"31502","DOI":"10.1074\/jbc.M103466200","article-title":"Procollagen II amino propeptide processing by ADAMTS-3. Insights on dermatosparaxis","volume":"276","author":"Fernandes","year":"2001","journal-title":"J. Biol. Chem."},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"221","DOI":"10.1016\/S0167-4781(01)00329-3","article-title":"Characterization of ADAMTS14, a novel member of the ADAMTS metalloproteinase family","volume":"1522","author":"Bolz","year":"2001","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"5756","DOI":"10.1074\/jbc.M105601200","article-title":"Cloning and characterization of ADAMTS-14, a novel ADAMTS displaying high homology with ADAMTS-2 and ADAMTS-3","volume":"277","author":"Colige","year":"2002","journal-title":"J. Biol. Chem."},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"501","DOI":"10.1016\/S0006-291X(02)00254-1","article-title":"ADAMTS1 cleaves aggrecan at multiple sites and is differentially inhibited by metalloproteinase inhibitors","volume":"293","author":"Westling","year":"2002","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"23443","DOI":"10.1074\/jbc.274.33.23443","article-title":"Cloning and characterization of ADAMTS11, an aggrecanase from the ADAMTS family","volume":"274","author":"Abbaszade","year":"1999","journal-title":"J. Biol. Chem."},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"9503","DOI":"10.1074\/jbc.M211009200","article-title":"Characterization of ADAMTS-9 and ADAMTS-20 as a distinct ADAMTS subfamily related to Caenorhabditis elegans GON-1","volume":"278","author":"Somerville","year":"2003","journal-title":"J. Biol. Chem."},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"1664","DOI":"10.1126\/science.284.5420.1664","article-title":"Purification and cloning of aggrecanase-1, a member of the ADAMTS family of proteins","volume":"284","author":"Tortorella","year":"1999","journal-title":"Science"},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"2487","DOI":"10.3892\/mmr.2015.3667","article-title":"Downregulation of A disintegrin and metallopeptidase with thrombospondin motif type 1 by DNA hypermethylation in human gastric cancer","volume":"12","author":"Chen","year":"2015","journal-title":"Mol. Med. Rep."},{"key":"ref_115","doi-asserted-by":"crossref","first-page":"656","DOI":"10.1111\/j.0022-202X.2004.23406.x","article-title":"Novel types of mutation responsible for the dermatosparactic type of Ehlers-Danlos syndrome (Type VIIC) and common polymorphisms in the ADAMTS2 gene","volume":"123","author":"Colige","year":"2004","journal-title":"J. Invest. Dermatol."},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"24","DOI":"10.1016\/j.matbio.2015.03.001","article-title":"Insights on ADAMTS proteases and ADAMTS-like proteins from mammalian genetics","volume":"44\u201346","author":"Dubail","year":"2015","journal-title":"Matrix Biol."},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"46","DOI":"10.1016\/j.matbio.2015.04.001","article-title":"The procollagen N-proteinases ADAMTS2, 3 and 14 in pathophysiology","volume":"44\u201346","author":"Bekhouche","year":"2015","journal-title":"Matrix Biol."},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"401","DOI":"10.1007\/s00592-012-0443-9","article-title":"PPARG2 Pro12Ala and ADAMTS9 rs4607103 as \u201cinsulin resistance loci\u201d and \u201cinsulin secretion loci\u201d in Italian individuals. The GENFIEV study and the Verona Newly Diagnosed Type 2 Diabetes Study (VNDS) 4","volume":"50","author":"Trombetta","year":"2013","journal-title":"Acta Diabetol."},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"109","DOI":"10.1016\/j.cca.2016.10.017","article-title":"Update on ADAMTS13 and VWF in cardiovascular and hematological disorders","volume":"463","author":"Akyol","year":"2016","journal-title":"Clin. Chim. Acta"},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"1481","DOI":"10.1002\/art.39086","article-title":"Semaphorin 4D Contributes to Rheumatoid Arthritis by Inducing Inflammatory Cytokine Production: Pathogenic and Therapeutic Implications","volume":"67","author":"Yoshida","year":"2015","journal-title":"Arthritis Rheumatol."},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"1454","DOI":"10.3899\/jrheum.091285","article-title":"ADAMTS5 is a biomarker for prediction of response to infliximab in patients with rheumatoid arthritis","volume":"37","author":"Tsuzaka","year":"2010","journal-title":"J. Rheumatol."},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"9642","DOI":"10.4238\/2014.November.14.9","article-title":"Increased serum ADAMTS-4 in knee osteoarthritis: A potential indicator for the diagnosis of osteoarthritis in early stages","volume":"13","author":"Li","year":"2014","journal-title":"Genet. Mol. Res."},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"8781","DOI":"10.1016\/j.bmc.2008.08.058","article-title":"Specific targeting of metzincin family members with small-molecule inhibitors: Progress toward a multifarious challenge","volume":"16","author":"Georgiadis","year":"2008","journal-title":"Bioorg. Med. Chem."},{"key":"ref_124","doi-asserted-by":"crossref","first-page":"904","DOI":"10.1038\/nrd4390","article-title":"Is there new hope for therapeutic matrix metalloproteinase inhibition?","volume":"13","author":"Vandenbroucke","year":"2014","journal-title":"Nat. Rev. Drug Discov."},{"key":"ref_125","doi-asserted-by":"crossref","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":"ref_126","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1016\/j.canlet.2012.03.040","article-title":"Tissue inhibitor of metalloproteinases in oral squamous cell carcinomas\u2014A therapeutic target?","volume":"323","year":"2012","journal-title":"Cancer Lett."},{"key":"ref_127","doi-asserted-by":"crossref","first-page":"71","DOI":"10.2174\/1573406053402569","article-title":"Protease inhibitors in the clinic","volume":"1","author":"Abbenante","year":"2005","journal-title":"Med. Chem."},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1023\/B:HREV.0000011395.11179.af","article-title":"Matrix metalloproteinase inhibitor development and the remodeling of drug discovery","volume":"9","author":"Peterson","year":"2004","journal-title":"Heart Fail. Rev."},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"657","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":"ref_130","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/S1357-2725(01)00097-8","article-title":"Tumor necrosis factor-\u03b1 converting enzyme","volume":"34","author":"Black","year":"2002","journal-title":"Int. J. Biochem. Cell Biol."},{"key":"ref_131","doi-asserted-by":"crossref","first-page":"625","DOI":"10.18388\/abp.2003_3656","article-title":"Structure and functions of tumor necrosis factor-\u03b1 converting enzyme","volume":"50","author":"Mezyk","year":"2003","journal-title":"Acta Biochim. Pol."},{"key":"ref_132","first-page":"598","article-title":"BMS-561392. Bristol-Myers Squibb","volume":"4","author":"Grootveld","year":"2003","journal-title":"Curr. Opin. Investig. Drugs"},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"117","DOI":"10.1080\/09674845.2009.11730257","article-title":"ADAMs and ADAMTSs in cancer","volume":"66","author":"Turner","year":"2009","journal-title":"Br. J. Biomed. Sci."},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"451","DOI":"10.7150\/ijbs.4038","article-title":"The silencing of RECK gene is associated with promoter hypermethylation and poor survival in hepatocellular carcinoma","volume":"8","author":"Zhang","year":"2012","journal-title":"Int. J. Biol. Sci."},{"key":"ref_135","doi-asserted-by":"crossref","first-page":"191","DOI":"10.1002\/jcp.24434","article-title":"RECK inhibits stemness gene expression and tumorigenicity of gastric cancer cells by suppressing ADAM-mediated Notch1 activation","volume":"229","author":"Hong","year":"2014","journal-title":"J. Cell. Physiol."},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"2189","DOI":"10.1038\/onc.2014.175","article-title":"RECK controls breast cancer metastasis by modulating a convergent, STAT3-dependent neoangiogenic switch","volume":"34","author":"Walsh","year":"2015","journal-title":"Oncogene"},{"key":"ref_137","doi-asserted-by":"crossref","unstructured":"Zhang, B., Zhang, J., Xu, Z.Y., and Xie, H.L. (2009). Expression of RECK and matrix metalloproteinase-2 in ameloblastoma. BMC Cancer, 9.","DOI":"10.1186\/1471-2407-9-427"},{"key":"ref_138","doi-asserted-by":"crossref","first-page":"4007","DOI":"10.7314\/APJCP.2015.16.9.4007","article-title":"Expression of RECK and MMPs in Hepatoblastoma and Neuroblastoma and Comparative Analysis on the Tumor Metastasis","volume":"16","author":"Xu","year":"2015","journal-title":"Asian Pac. J. Cancer Prev."},{"key":"ref_139","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1016\/j.bbamcr.2010.01.003","article-title":"The tissue inhibitors of metalloproteinases (TIMPs): An ancient family with structural and functional diversity","volume":"1803","author":"Brew","year":"2010","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_140","doi-asserted-by":"crossref","unstructured":"Foidart, J.M., and Muschel, R.J. (2002). Tissue Inhibitors of Metalloproteinases in cancer. Cancer Metastasis\u2014Biology and Treatment, Springer.","DOI":"10.1007\/1-4020-2008-2"},{"key":"ref_141","doi-asserted-by":"crossref","first-page":"3531","DOI":"10.1002\/jcb.26185","article-title":"Therapeutic Potential of Matrix Metalloproteinase Inhibition in Breast Cancer","volume":"118","author":"Radisky","year":"2017","journal-title":"J. Cell. Biochem."},{"key":"ref_142","doi-asserted-by":"crossref","first-page":"16778","DOI":"10.1074\/jbc.273.27.16778","article-title":"Localization of the functional domains of human tissue inhibitor of metalloproteinases-3 and the effects of a Sorsby\u2019s fundus dystrophy mutation","volume":"273","author":"Langton","year":"1998","journal-title":"J. Biol. Chem."},{"key":"ref_143","doi-asserted-by":"crossref","first-page":"100","DOI":"10.1006\/bbrc.1997.6859","article-title":"The C-terminal domain of tissue inhibitor of metalloproteinases-2 is required for cell binding but not for antimetalloproteinase activity","volume":"236","author":"Ko","year":"1997","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_144","doi-asserted-by":"crossref","first-page":"99","DOI":"10.1007\/s10555-006-7893-x","article-title":"Novel functions of TIMPs in cell signaling","volume":"25","author":"Chirco","year":"2006","journal-title":"Cancer Metastasis Rev."},{"key":"ref_145","doi-asserted-by":"crossref","first-page":"24487","DOI":"10.1074\/jbc.M110.136820","article-title":"Mice with tissue inhibitor of metalloproteinases 4 (Timp4) deletion succumb to induced myocardial infarction but not to cardiac pressure overload","volume":"285","author":"Koskivirta","year":"2010","journal-title":"J. Biol. Chem."},{"key":"ref_146","doi-asserted-by":"crossref","first-page":"247","DOI":"10.1016\/j.matbio.2015.03.005","article-title":"The role of TIMPs in regulation of extracellular matrix proteolysis","volume":"44\u201346","author":"Arpino","year":"2015","journal-title":"Matrix Biol."},{"key":"ref_147","doi-asserted-by":"crossref","unstructured":"Adamson, A., Ghoreschi, K., Rittler, M., Chen, Q., Sun, H.W., Vahedi, G., Kanno, Y., Stetler-Stevenson, W.G., O\u2019Shea, J.J., and Laurence, A. (2013). Tissue inhibitor of metalloproteinase 1 is preferentially expressed in Th1 and Th17 T-helper cell subsets and is a direct STAT target gene. PLoS ONE, 8.","DOI":"10.1371\/journal.pone.0059367"},{"key":"ref_148","first-page":"127","article-title":"Influence of LPS, TNF, TGF-ss1 and IL-4 on the expression of MMPs, TIMPs and selected cytokines in rat synovial membranes incubated in vitro","volume":"27","author":"Hyc","year":"2011","journal-title":"Int. J. Mol. Med."},{"key":"ref_149","doi-asserted-by":"crossref","first-page":"566","DOI":"10.1007\/s10495-013-0827-5","article-title":"Hepatic apoptosis can modulate liver fibrosis through TIMP1 pathway","volume":"18","author":"Wang","year":"2013","journal-title":"Apoptosis"},{"key":"ref_150","doi-asserted-by":"crossref","first-page":"57","DOI":"10.1007\/s10555-007-9105-8","article-title":"The tumor microenvironment: Regulation by MMP-independent effects of tissue inhibitor of metalloproteinases-2","volume":"27","year":"2008","journal-title":"Cancer Metastasis Rev."},{"key":"ref_151","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1186\/2052-8426-2-17","article-title":"Molecular mechanisms of tissue inhibitor of metalloproteinase 2 in the tumor microenvironment","volume":"2","author":"Remillard","year":"2014","journal-title":"Mol. Cell. Ther."},{"key":"ref_152","doi-asserted-by":"crossref","unstructured":"Fussbroich, B., Wagener, N., Macher-Goeppinger, S., Benner, A., Falth, M., Sultmann, H., Holzer, A., Hoppe-Seyler, K., and Hoppe-Seyler, F. (2011). EZH2 depletion blocks the proliferation of colon cancer cells. PLoS ONE, 6.","DOI":"10.1371\/journal.pone.0021651"},{"key":"ref_153","doi-asserted-by":"crossref","first-page":"166","DOI":"10.18632\/oncotarget.801","article-title":"TIMP-2 modulates cancer cell transcriptional profile and enhances E-cadherin\/\u03b2-catenin complex expression in A549 lung cancer cells","volume":"4","author":"Bourboulia","year":"2013","journal-title":"Oncotarget"},{"key":"ref_154","doi-asserted-by":"crossref","first-page":"3855","DOI":"10.3892\/mmr.2015.3810","article-title":"Suppressor of cytokine signaling 1-modulated metalloproteinases and tissue inhibitor of metalloproteinase in pulmonary fibrosis","volume":"12","author":"Zhang","year":"2015","journal-title":"Mol. Med. Rep."},{"key":"ref_155","doi-asserted-by":"crossref","unstructured":"Qi, J.H., Ebrahem, Q., Ali, M., Cutler, A., Bell, B., Prayson, N., Sears, J., Knauper, V., Murphy, G., and Anand-Apte, B. (2013). Tissue inhibitor of metalloproteinases-3 peptides inhibit angiogenesis and choroidal neovascularization in mice. PLoS ONE, 8.","DOI":"10.1371\/journal.pone.0055667"},{"key":"ref_156","doi-asserted-by":"crossref","first-page":"588","DOI":"10.1002\/jcb.21434","article-title":"Interleukin-4 antagonizes oncostatin M and transforming growth factor \u03b2-induced responses in articular chondrocytes","volume":"103","author":"Qureshi","year":"2008","journal-title":"J. Cell. Biochem."},{"key":"ref_157","doi-asserted-by":"crossref","first-page":"507","DOI":"10.1016\/j.bbrc.2015.12.020","article-title":"The imbalance between TIMP3 and matrix-degrading enzymes plays an important role in intervertebral disc degeneration","volume":"469","author":"Li","year":"2016","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_158","doi-asserted-by":"crossref","first-page":"1831","DOI":"10.1002\/pros.23056","article-title":"Timp3 loss accelerates tumour invasion and increases prostate inflammation in a mouse model of prostate cancer","volume":"75","author":"Adissu","year":"2015","journal-title":"Prostate"},{"key":"ref_159","doi-asserted-by":"crossref","first-page":"381","DOI":"10.1016\/j.matbio.2008.01.008","article-title":"Molecular dissection of TIMP3 mutation S156C associated with Sorsby fundus dystrophy","volume":"27","author":"Fogarasi","year":"2008","journal-title":"Matrix Biol."},{"key":"ref_160","first-page":"re6","article-title":"Tissue inhibitors of metalloproteinases in cell signaling: Metalloproteinase-independent biological activities","volume":"1","year":"2008","journal-title":"Sci. Signal."},{"key":"ref_161","doi-asserted-by":"crossref","first-page":"3041","DOI":"10.1038\/sj.onc.1209336","article-title":"TIMP-1 regulation of cell cycle in human breast epithelial cells via stabilization of p27KIP1 protein","volume":"25","author":"Taube","year":"2006","journal-title":"Oncogene"},{"key":"ref_162","doi-asserted-by":"crossref","first-page":"13453","DOI":"10.1074\/jbc.270.22.13453","article-title":"Tissue inhibitor of metalloproteinase-2 stimulates fibroblast proliferation via a cAMP-dependent mechanism","volume":"270","author":"Corcoran","year":"1995","journal-title":"J. Biol. Chem."},{"key":"ref_163","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1016\/0014-5793(96)01066-6","article-title":"Tyrosine phosphorylation is crucial for growth signaling by tissue inhibitors of metalloproteinases (TIMP-1 and TIMP-2)","volume":"396","author":"Yamashita","year":"1996","journal-title":"FEBS Lett."},{"key":"ref_164","doi-asserted-by":"crossref","first-page":"201","DOI":"10.1016\/S0006-291X(02)00741-6","article-title":"Both tissue inhibitors of metalloproteinases-1 (TIMP-1) and TIMP-2 activate Ras but through different pathways","volume":"296","author":"Wang","year":"2002","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_165","doi-asserted-by":"crossref","first-page":"13","DOI":"10.3109\/03008207.2013.867339","article-title":"Normalization of the tumor microenvironment: Evidence for tissue inhibitor of metalloproteinase-2 as a cancer therapeutic","volume":"55","author":"Gavil","year":"2014","journal-title":"Connect. Tissue Res."},{"key":"ref_166","doi-asserted-by":"crossref","first-page":"171","DOI":"10.1016\/S0092-8674(03)00551-8","article-title":"TIMP-2 mediated inhibition of angiogenesis: An MMP-independent mechanism","volume":"114","author":"Seo","year":"2003","journal-title":"Cell"},{"key":"ref_167","doi-asserted-by":"crossref","first-page":"3711","DOI":"10.1074\/jbc.M509932200","article-title":"Shp-1 mediates the antiproliferative activity of tissue inhibitor of metalloproteinase-2 in human microvascular endothelial cells","volume":"281","author":"Seo","year":"2006","journal-title":"J. Biol. Chem."},{"key":"ref_168","doi-asserted-by":"crossref","first-page":"41886","DOI":"10.1074\/jbc.M110.166439","article-title":"The anti-angiogenic peptide, loop 6, binds insulin-like growth factor-1 receptor","volume":"285","author":"Fernandez","year":"2010","journal-title":"J. Biol. Chem."},{"key":"ref_169","doi-asserted-by":"crossref","first-page":"3934","DOI":"10.1038\/sj.emboj.7601281","article-title":"Identification of CD63 as a tissue inhibitor of metalloproteinase-1 interacting cell surface protein","volume":"25","author":"Jung","year":"2006","journal-title":"EMBO J."},{"key":"ref_170","doi-asserted-by":"crossref","first-page":"4917","DOI":"10.1523\/JNEUROSCI.5066-04.2005","article-title":"Tissue inhibitor of metalloproteinase-2 promotes neuronal differentiation by acting as an anti-mitogenic signal","volume":"25","author":"Jaworski","year":"2005","journal-title":"J. Neurosci."},{"key":"ref_171","doi-asserted-by":"crossref","first-page":"464","DOI":"10.3171\/jns.2001.94.3.0464","article-title":"Roles of membrane type 1 matrix metalloproteinase and tissue inhibitor of metalloproteinases 2 in invasion and dissemination of human malignant glioma","volume":"94","author":"Nakada","year":"2001","journal-title":"J. Neurosurg."},{"key":"ref_172","doi-asserted-by":"crossref","first-page":"555","DOI":"10.1023\/A:1006760632766","article-title":"Expression of matrix metalloproteinases and their inhibitors in human brain tumors","volume":"17","author":"Kachra","year":"1999","journal-title":"Clin. Exp. Metastasis"},{"key":"ref_173","doi-asserted-by":"crossref","first-page":"890","DOI":"10.3892\/etm.2012.859","article-title":"The expression and clinical significance of matrix metalloproteinase 7 and tissue inhibitor of matrix metalloproteinases 2 in clear cell renal cell carcinoma","volume":"5","author":"Lu","year":"2013","journal-title":"Exp. Ther. Med."},{"key":"ref_174","doi-asserted-by":"crossref","first-page":"896","DOI":"10.1007\/s00595-004-2853-y","article-title":"Serum tissue inhibitors of metalloproteinase-1 and -2 in patients with non-small cell lung cancer","volume":"34","author":"Suemitsu","year":"2004","journal-title":"Surg. Today"},{"key":"ref_175","doi-asserted-by":"crossref","first-page":"935","DOI":"10.1007\/s13277-012-0321-7","article-title":"Immunoreactivity for TIMP-2 is associated with a favorable prognosis in endometrial carcinoma","volume":"33","author":"Soini","year":"2012","journal-title":"Tumour Biol."},{"key":"ref_176","doi-asserted-by":"crossref","first-page":"87","DOI":"10.1007\/s12079-011-0157-8","article-title":"Analysis of the MMP-dependent and independent functions of tissue inhibitor of metalloproteinase-2 on the invasiveness of breast cancer cells","volume":"6","author":"Walsh","year":"2012","journal-title":"J. Cell Commun. Signal."},{"key":"ref_177","doi-asserted-by":"crossref","first-page":"42905","DOI":"10.18632\/oncotarget.5466","article-title":"Growth-stimulatory activity of TIMP-2 is mediated through c-Src activation followed by activation of FAK, PI3-kinase\/AKT, and ERK1\/2 independent of MMP inhibition in lung adenocarcinoma cells","volume":"6","author":"Kim","year":"2015","journal-title":"Oncotarget"},{"key":"ref_178","doi-asserted-by":"crossref","first-page":"12061","DOI":"10.18632\/oncotarget.3616","article-title":"TIMP-1 activated carcinoma-associated fibroblasts inhibit tumor apoptosis by activating SDF1\/CXCR4 signaling in hepatocellular carcinoma","volume":"6","author":"Song","year":"2015","journal-title":"Oncotarget"},{"key":"ref_179","doi-asserted-by":"crossref","first-page":"483","DOI":"10.1369\/0022155416656173","article-title":"Tissue Inhibitor of Metalloproteinase-1 Is Confined to Tumor-Associated Myofibroblasts and Is Increased With Progression in Gastric Adenocarcinoma","volume":"64","author":"Laerum","year":"2016","journal-title":"J. Histochem. Cytochem."},{"key":"ref_180","doi-asserted-by":"crossref","first-page":"494","DOI":"10.3892\/or.2016.4818","article-title":"Expression and inhibitory role of TIMP-3 in hepatocellular carcinoma","volume":"36","author":"Shen","year":"2016","journal-title":"Oncol. Rep."},{"key":"ref_181","doi-asserted-by":"crossref","first-page":"331","DOI":"10.1007\/978-1-4757-3587-1_16","article-title":"Ovarian cancer-associated proteinases","volume":"107","author":"Ghosh","year":"2002","journal-title":"Cancer Treat. Res."},{"key":"ref_182","doi-asserted-by":"crossref","first-page":"e6104","DOI":"10.1590\/1414-431x20176104","article-title":"Relationship between matrix metalloproteinases and the occurrence and development of ovarian cancer","volume":"50","author":"Zhang","year":"2017","journal-title":"Braz. J. Med. Biol. Res."},{"key":"ref_183","doi-asserted-by":"crossref","first-page":"356","DOI":"10.1097\/IGC.0000000000000386","article-title":"The expression of tumor-derived and stromal-derived matrix metalloproteinase 2 predicted prognosis of ovarian cancer","volume":"25","author":"Fu","year":"2015","journal-title":"Int. J. Gynecol. Cancer"},{"key":"ref_184","doi-asserted-by":"crossref","first-page":"226","DOI":"10.1309\/49LA9XCBGWJ8F2KM","article-title":"Role of immunohistochemical overexpression of matrix metalloproteinases MMP-2 and MMP-11 in the prognosis of death by ovarian cancer","volume":"129","author":"Perigny","year":"2008","journal-title":"Am. J. Clin. Pathol."},{"key":"ref_185","doi-asserted-by":"crossref","first-page":"106","DOI":"10.1006\/gyno.2000.5856","article-title":"Expression of matrix metalloproteinases and related tissue inhibitors in the cyst fluids of ovarian mucinous neoplasms","volume":"78","author":"Furuya","year":"2000","journal-title":"Gynecol. Oncol."},{"key":"ref_186","doi-asserted-by":"crossref","first-page":"190","DOI":"10.1186\/1746-1596-8-190","article-title":"Clinicopathologic significance of claudin-6, occludin, and matrix metalloproteinases-2 expression in ovarian carcinoma","volume":"8","author":"Wang","year":"2013","journal-title":"Diagn. Pathol."},{"key":"ref_187","doi-asserted-by":"crossref","first-page":"739","DOI":"10.1016\/j.humpath.2015.01.014","article-title":"Prognostic significance of TIMP-2, MMP-2, and MMP-9 on high-grade serous ovarian carcinoma using digital image analysis","volume":"46","author":"Desmeules","year":"2015","journal-title":"Hum. Pathol."},{"key":"ref_188","doi-asserted-by":"crossref","first-page":"1049","DOI":"10.3892\/or.2011.1608","article-title":"Expression of MMP-2, -7, -9, MT1-MMP and TIMP-1 and -2 has no prognostic relevance in patients with advanced epithelial ovarian cancer","volume":"27","author":"Brun","year":"2012","journal-title":"Oncol. Rep."},{"key":"ref_189","doi-asserted-by":"crossref","first-page":"491","DOI":"10.1369\/0022155412446978","article-title":"Enhanced immunoreactivity of TIMP-2 in the stromal compartment of tumor as a marker of favorable prognosis in ovarian cancer patients","volume":"60","author":"Halon","year":"2012","journal-title":"J. Histochem. Cytochem."},{"key":"ref_190","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1155\/2001\/418547","article-title":"Ovarian carcinoma and serous effusions. Changing views regarding tumor progression and review of current literature","volume":"23","author":"Davidson","year":"2001","journal-title":"Anal. Cell. Pathol."},{"key":"ref_191","first-page":"1239","article-title":"Serous and mucinous ovarian tumors express different profiles of MMP-2, -7, -9, MT1-MMP, and TIMP-1 and -2","volume":"33","author":"Brun","year":"2008","journal-title":"Int. J. Oncol."},{"key":"ref_192","doi-asserted-by":"crossref","first-page":"298","DOI":"10.2174\/1574892810999150827153642","article-title":"Angiogenesis Markers in Gynecological Tumors and Patents for Anti-Angiogenic Approach: Review","volume":"10","author":"Abdalla","year":"2015","journal-title":"Recent Pat. Anticancer Drug Discov."},{"key":"ref_193","doi-asserted-by":"crossref","first-page":"2978","DOI":"10.4238\/2014.April.16.6","article-title":"Screening of the residual normal ovarian tissue adjacent to orthotopic epithelial ovarian carcinomas in nude mice","volume":"13","author":"Zhu","year":"2014","journal-title":"Genet. Mol. Res."},{"key":"ref_194","doi-asserted-by":"crossref","first-page":"799","DOI":"10.1023\/A:1006723011835","article-title":"High levels of MMP-2, MMP-9, MT1-MMP and TIMP-2 mRNA correlate with poor survival in ovarian carcinoma","volume":"17","author":"Davidson","year":"1999","journal-title":"Clin. Exp. Metastasis"},{"key":"ref_195","doi-asserted-by":"crossref","first-page":"13111","DOI":"10.1074\/jbc.M117.800904","article-title":"Post-translational modification of the membrane type 1 matrix metalloproteinase (MT1-MMP) cytoplasmic tail impacts ovarian cancer multicellular aggregate dynamics","volume":"292","author":"Yang","year":"2017","journal-title":"J. Biol. Chem."},{"key":"ref_196","doi-asserted-by":"crossref","first-page":"2040","DOI":"10.1016\/S0959-8049(01)00235-0","article-title":"Ovarian carcinoma cells in serous effusions show altered MMP-2 and TIMP-2 mRNA levels","volume":"37","author":"Davidson","year":"2001","journal-title":"Eur. J. Cancer"},{"key":"ref_197","doi-asserted-by":"crossref","first-page":"267","DOI":"10.1016\/j.tranon.2014.02.013","article-title":"Clinical Relevance of Increased Endothelial and Mesothelial Expression of Proangiogenic Proteases and VEGFA in the Omentum of Patients with Metastatic Ovarian High-Grade Serous Carcinoma","volume":"7","author":"Winiarski","year":"2014","journal-title":"Transl. Oncol."},{"key":"ref_198","doi-asserted-by":"crossref","first-page":"3006","DOI":"10.1158\/0008-5472.CAN-05-1292","article-title":"Lysophosphatidic acid is constitutively produced by human peritoneal mesothelial cells and enhances adhesion, migration, and invasion of ovarian cancer cells","volume":"66","author":"Ren","year":"2006","journal-title":"Cancer Res."},{"key":"ref_199","doi-asserted-by":"crossref","first-page":"719","DOI":"10.1001\/jama.280.8.719","article-title":"Lysophosphatidic acid as a potential biomarker for ovarian and other gynecologic cancers","volume":"280","author":"Xu","year":"1998","journal-title":"JAMA"},{"key":"ref_200","first-page":"3194","article-title":"Lysophosphatidic acid promotes matrix metalloproteinase (MMP) activation and MMP-dependent invasion in ovarian cancer cells","volume":"61","author":"Fishman","year":"2001","journal-title":"Cancer Res."},{"key":"ref_201","doi-asserted-by":"crossref","first-page":"22143","DOI":"10.1074\/jbc.M115.641092","article-title":"Lysophosphatidic Acid Initiates Epithelial to Mesenchymal Transition and Induces \u03b2-Catenin-mediated Transcription in Epithelial Ovarian Carcinoma","volume":"290","author":"Burkhalter","year":"2015","journal-title":"J. Biol. Chem."},{"key":"ref_202","doi-asserted-by":"crossref","first-page":"795","DOI":"10.1159\/000458744","article-title":"Lysophosphatidic Acid Promotes Epithelial to Mesenchymal Transition in Ovarian Cancer Cells by Repressing SIRT1","volume":"41","author":"Ray","year":"2017","journal-title":"Cell Physiol. Biochem."},{"key":"ref_203","doi-asserted-by":"crossref","first-page":"361","DOI":"10.1016\/j.ygyno.2007.10.027","article-title":"Lysophosphatidic acid (LPA) promotes E-cadherin ectodomain shedding and OVCA429 cell invasion in an uPA-dependent manner","volume":"108","author":"Gil","year":"2008","journal-title":"Gynecol. Oncol."},{"key":"ref_204","doi-asserted-by":"crossref","first-page":"501492","DOI":"10.1155\/2012\/501492","article-title":"Lysophosphatidic Acid disrupts junctional integrity and epithelial cohesion in ovarian cancer cells","volume":"2012","author":"Liu","year":"2012","journal-title":"J. Oncol."},{"key":"ref_205","doi-asserted-by":"crossref","first-page":"4606","DOI":"10.1158\/0008-5472.CAN-07-5046","article-title":"Matrix metalloproteinase 9 is a mediator of epidermal growth factor-dependent e-cadherin loss in ovarian carcinoma cells","volume":"68","author":"Symowicz","year":"2008","journal-title":"Cancer Res."},{"key":"ref_206","doi-asserted-by":"crossref","first-page":"2030","DOI":"10.1158\/0008-5472.CAN-06-2808","article-title":"Engagement of collagen-binding integrins promotes matrix metalloproteinase-9-dependent E-cadherin ectodomain shedding in ovarian carcinoma cells","volume":"67","author":"Symowicz","year":"2007","journal-title":"Cancer Res."},{"key":"ref_207","doi-asserted-by":"crossref","first-page":"393","DOI":"10.1002\/ijc.2910580315","article-title":"Differential expression of the cell-cell adhesion molecule E-cadherin in ascites and solid human ovarian tumor cells","volume":"58","author":"Veatch","year":"1994","journal-title":"Int. J. Cancer"},{"key":"ref_208","first-page":"65","article-title":"Higher levels of soluble E-cadherin in cyst fluid from malignant ovarian tumours than in benign cysts","volume":"21","author":"Sundfeldt","year":"2001","journal-title":"Anticancer Res."},{"key":"ref_209","doi-asserted-by":"crossref","unstructured":"Mahner, S., Woelber, L., Eulenburg, C., Schwarz, J., Carney, W., Jaenicke, F., Milde-Langosch, K., and Mueller, V. (2010). TIMP-1 and VEGF-165 serum concentration during first-line therapy of ovarian cancer patients. BMC Cancer, 10.","DOI":"10.1186\/1471-2407-10-139"},{"key":"ref_210","first-page":"919","article-title":"Gene expression patterns of chemoresistant and chemosensitive serous epithelial ovarian tumors with possible predictive value in response to initial chemotherapy","volume":"29","author":"Bachvarov","year":"2006","journal-title":"Int. J. Oncol."},{"key":"ref_211","doi-asserted-by":"crossref","first-page":"2941","DOI":"10.1158\/1078-0432.CCR-14-3111","article-title":"Upregulation of Periostin and Reactive Stroma Is Associated with Primary Chemoresistance and Predicts Clinical Outcomes in Epithelial Ovarian Cancer","volume":"21","author":"Ryner","year":"2015","journal-title":"Clin. Cancer Res."},{"key":"ref_212","doi-asserted-by":"crossref","first-page":"5880","DOI":"10.1158\/0008-5472.CAN-09-4341","article-title":"Identification of a metalloprotease-chemokine signaling system in the ovarian cancer microenvironment: Implications for antiangiogenic therapy","volume":"70","author":"Agarwal","year":"2010","journal-title":"Cancer Res."},{"key":"ref_213","doi-asserted-by":"crossref","first-page":"247","DOI":"10.1016\/j.ygyno.2010.10.032","article-title":"MMP-1-PAR1 axis mediates LPA-induced epithelial ovarian cancer (EOC) invasion","volume":"120","author":"Wang","year":"2011","journal-title":"Gynecol. Oncol."},{"key":"ref_214","doi-asserted-by":"crossref","first-page":"1641","DOI":"10.1016\/j.yexcr.2012.05.002","article-title":"Mixed lineage kinase 3 is required for matrix metalloproteinase expression and invasion in ovarian cancer cells","volume":"318","author":"Zhan","year":"2012","journal-title":"Exp. Cell Res."},{"key":"ref_215","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1002\/ijc.20697","article-title":"Matrilysin (MMP-7) promotes invasion of ovarian cancer cells by activation of progelatinase","volume":"114","author":"Wang","year":"2005","journal-title":"Int. J. Cancer"},{"key":"ref_216","doi-asserted-by":"crossref","first-page":"293","DOI":"10.1042\/BJ20110282","article-title":"Mesothelin enhances invasion of ovarian cancer by inducing MMP-7 through MAPK\/ERK and JNK pathways","volume":"442","author":"Chang","year":"2012","journal-title":"Biochem. J."},{"key":"ref_217","doi-asserted-by":"crossref","first-page":"331","DOI":"10.1002\/(SICI)1097-0215(19981029)78:3<331::AID-IJC13>3.0.CO;2-9","article-title":"Proteinase requirements of epidermal growth factor-induced ovarian cancer cell invasion","volume":"78","author":"Ellerbroek","year":"1998","journal-title":"Int. J. Cancer"},{"key":"ref_218","doi-asserted-by":"crossref","first-page":"3912","DOI":"10.1158\/0008-5472.CAN-05-1785","article-title":"Gonadotropins activate proteolysis and increase invasion through protein kinase A and phosphatidylinositol 3-kinase pathways in human epithelial ovarian cancer cells","volume":"66","author":"Choi","year":"2006","journal-title":"Cancer Res."},{"key":"ref_219","doi-asserted-by":"crossref","first-page":"994","DOI":"10.1097\/IGC.0000000000000746","article-title":"Docosahexaenoic Acid Modulates Invasion and Metastasis of Human Ovarian Cancer via Multiple Molecular Pathways","volume":"26","author":"Wang","year":"2016","journal-title":"Int. J. Gynecol. Cancer"},{"key":"ref_220","doi-asserted-by":"crossref","first-page":"28773","DOI":"10.1038\/srep28773","article-title":"Bisdemethoxycurcumin inhibits ovarian cancer via reducing oxidative stress mediated MMPs expressions","volume":"6","author":"Pei","year":"2016","journal-title":"Sci. Rep."},{"key":"ref_221","first-page":"127","article-title":"Shedding of membrane vesicles by tumor and endothelial cells","volume":"110","author":"Dolo","year":"2005","journal-title":"Ital. J. Anat. Embryol."},{"key":"ref_222","doi-asserted-by":"crossref","first-page":"4783","DOI":"10.1158\/1078-0432.CCR-04-1426","article-title":"Clinical significance of heparin-binding epidermal growth factor-like growth factor and a disintegrin and metalloprotease 17 expression in human ovarian cancer","volume":"11","author":"Tanaka","year":"2005","journal-title":"Clin. Cancer Res."},{"key":"ref_223","first-page":"673","article-title":"The role of CDCP1 (CUB domain-containing protein 1) and ADAM12 (a disintegrin and metalloproteinase 12) in ovarian cancer","volume":"20","author":"Vlad","year":"2015","journal-title":"J. BUON"},{"key":"ref_224","doi-asserted-by":"crossref","first-page":"88410","DOI":"10.18632\/oncotarget.11120","article-title":"ADAMTS16 mutations sensitize ovarian cancer cells to platinum-based chemotherapy","volume":"8","author":"Yasukawa","year":"2016","journal-title":"Oncotarget"},{"key":"ref_225","doi-asserted-by":"crossref","first-page":"30061","DOI":"10.1038\/srep30061","article-title":"Unique proteome signature of post-chemotherapy ovarian cancer ascites-derived tumor cells","volume":"6","author":"Ahmed","year":"2016","journal-title":"Sci. Rep."},{"key":"ref_226","doi-asserted-by":"crossref","unstructured":"Latifi, A., Luwor, R.B., Bilandzic, M., Nazaretian, S., Stenvers, K., Pyman, J., Zhu, H., Thompson, E.W., Quinn, M.A., and Findlay, J.K. (2012). Isolation and characterization of tumor cells from the ascites of ovarian cancer patients: Molecular phenotype of chemoresistant ovarian tumors. PLoS ONE, 7.","DOI":"10.1371\/journal.pone.0046858"},{"key":"ref_227","doi-asserted-by":"crossref","first-page":"316","DOI":"10.1159\/000446244","article-title":"Prognostic Value of ADAMTS Proteases and Their Substrates in Epithelial Ovarian Cancer","volume":"83","author":"Lima","year":"2016","journal-title":"Pathobiology"},{"key":"ref_228","doi-asserted-by":"crossref","first-page":"711","DOI":"10.1158\/1078-0432.CCR-13-1256","article-title":"A collagen-remodeling gene signature regulated by TGF-\u03b2 signaling is associated with metastasis and poor survival in serous ovarian cancer","volume":"20","author":"Cheon","year":"2014","journal-title":"Clin. Cancer Res."},{"key":"ref_229","doi-asserted-by":"crossref","first-page":"259","DOI":"10.2217\/14796694.5.2.259","article-title":"The TGF-\u03b2 paradox in human cancer: An update","volume":"5","author":"Tian","year":"2009","journal-title":"Future Oncol."},{"key":"ref_230","doi-asserted-by":"crossref","first-page":"163","DOI":"10.1101\/gad.14.2.163","article-title":"Cell surface-localized matrix metalloproteinase-9 proteolytically activates TGF-\u03b2 and promotes tumor invasion and angiogenesis","volume":"14","author":"Yu","year":"2000","journal-title":"Genes Dev."},{"key":"ref_231","doi-asserted-by":"crossref","first-page":"85","DOI":"10.1186\/s12935-017-0454-2","article-title":"Blocking ERK1\/2 signaling impairs TGF-\u03b21 tumor promoting function but enhances its tumor suppressing role in intrahepatic cholangiocarcinoma cells","volume":"17","author":"Sritananuwat","year":"2017","journal-title":"Cancer Cell Int."},{"key":"ref_232","doi-asserted-by":"crossref","unstructured":"Alsina-Sanch\u00eds, E., Figueras, A., Lahiguera, A., Gil-Mart\u00edn, M., Pardo, B., Piulats, J.M., Mart\u00ed, L., Ponce, J., Matias-Guiu, X., Vidal, A., Villanueva, A., and Vi\u00f1als, F. (2017). TGF\u03b2 controls ovarian cancer cell proliferation. Int. J. Mol. Sci., 18.","DOI":"10.3390\/ijms18081658"},{"key":"ref_233","doi-asserted-by":"crossref","first-page":"2850","DOI":"10.1002\/jcb.23199","article-title":"Cisplatin treatment of primary and metastatic epithelial ovarian carcinomas generates residual cells with mesenchymal stem cell-like profile","volume":"112","author":"Latifi","year":"2011","journal-title":"J. Cell. Biochem."},{"key":"ref_234","doi-asserted-by":"crossref","unstructured":"Abubaker, K., Luwor, R.B., Zhu, H., McNally, O., Quinn, M.A., Burns, C.J., Thompson, E.W., Findlay, J.K., and Ahmed, N. (2014). Inhibition of the JAK2\/STAT3 pathway in ovarian cancer results in the loss of cancer stem cell-like characteristics and a reduced tumor burden. BMC Cancer, 14.","DOI":"10.1186\/1471-2407-14-317"},{"key":"ref_235","first-page":"e1006","article-title":"Distinct molecular signature of recurrent ovarian tumor cells isolated from the ascites of advanced-stage serous ovarian cancer patients","volume":"2","author":"Latifi","year":"2015","journal-title":"J. Cancer Stem Cell Res."},{"key":"ref_236","doi-asserted-by":"crossref","unstructured":"Chan, E., Luwor, R., Burns, C., Kannourakis, G., Findlay, J., and Ahmed, N. (2018). Momelotinib decreased tumor burden and prolonged disease-free remission period in a mouse model of ovarian cancer, submitted.","DOI":"10.18632\/oncotarget.24615"},{"key":"ref_237","doi-asserted-by":"crossref","unstructured":"Valacca, C., Tassone, E., and Mignatti, P. (2015). TIMP-2 Interaction with MT1-MMP Activates the AKT Pathway and Protects Tumor Cells from Apoptosis. PLoS ONE, 10.","DOI":"10.1371\/journal.pone.0136797"},{"key":"ref_238","doi-asserted-by":"crossref","first-page":"152","DOI":"10.1186\/s12943-015-0417-y","article-title":"A critical role of Oct4A in mediating metastasis and disease-free survival in a mouse model of ovarian cancer","volume":"14","author":"Samardzija","year":"2015","journal-title":"Mol. Cancer"},{"key":"ref_239","doi-asserted-by":"crossref","first-page":"79","DOI":"10.1042\/BJ20100649","article-title":"Selective inhibition of ADAM12 catalytic activity through engineering of tissue inhibitor of metalloproteinase 2 (TIMP-2)","volume":"430","author":"Kveiborg","year":"2010","journal-title":"Biochem. J."},{"key":"ref_240","doi-asserted-by":"crossref","first-page":"114","DOI":"10.1016\/j.canlet.2009.08.029","article-title":"The activity of a designer tissue inhibitor of metalloproteinases (TIMP)-1 against native membrane type 1 matrix metalloproteinase (MT1-MMP) in a cell-based environment","volume":"290","author":"Lee","year":"2010","journal-title":"Cancer Lett."},{"key":"ref_241","doi-asserted-by":"crossref","unstructured":"Duan, J.X., Rapti, M., Tsigkou, A., and Lee, M.H. (2015). Expanding the Activity of Tissue Inhibitors of Metalloproteinase (TIMP)-1 against Surface-Anchored Metalloproteinases by the Replacement of Its C-Terminal Domain: Implications for Anti-Cancer Effects. PLoS ONE, 10.","DOI":"10.1371\/journal.pone.0136384"},{"key":"ref_242","doi-asserted-by":"crossref","first-page":"54","DOI":"10.1159\/000324436","article-title":"Proteolytic matrix metallopeptidases and inhibitors in BCR-ABL1-negative myeloproliferative neoplasms: Correlation with JAK2 mutation status","volume":"126","author":"Vadikolia","year":"2011","journal-title":"Acta Haematol."},{"key":"ref_243","doi-asserted-by":"crossref","first-page":"1583","DOI":"10.1002\/ijc.28487","article-title":"Epigenetic reprogramming reverses the malignant epigenotype of the MMP\/TIMP axis genes in tumor cells","volume":"134","author":"Zhang","year":"2014","journal-title":"Int. J. Cancer"},{"key":"ref_244","doi-asserted-by":"crossref","first-page":"584","DOI":"10.1016\/j.urolonc.2014.01.016","article-title":"Significance of circulating matrix metalloproteinase-9 to tissue inhibitor of metalloproteinases-2 ratio as a predictor of disease progression in patients with metastatic renal cell carcinoma receiving sunitinib","volume":"32","author":"Miyake","year":"2014","journal-title":"Urol. Oncol."},{"key":"ref_245","doi-asserted-by":"crossref","first-page":"3203","DOI":"10.1074\/jbc.M008157200","article-title":"Tissue inhibitor of metalloproteinases-2 (TIMP-2) suppresses TKR-growth factor signaling independent of metalloproteinase inhibition","volume":"276","author":"Hoegy","year":"2001","journal-title":"J. Biol. Chem."},{"key":"ref_246","doi-asserted-by":"crossref","first-page":"4892","DOI":"10.1182\/blood-2012-05-428243","article-title":"Antagonism of VEGF-A-induced increase in vascular permeability by an integrin \u03b13\u03b21-Shp-1-cAMP\/PKA pathway","volume":"120","author":"Kim","year":"2012","journal-title":"Blood"},{"key":"ref_247","doi-asserted-by":"crossref","first-page":"374","DOI":"10.1038\/labinvest.2009.136","article-title":"TIMP-2 modulates VEGFR-2 phosphorylation and enhances phosphodiesterase activity in endothelial cells","volume":"90","author":"Lee","year":"2010","journal-title":"Lab. Investig."},{"key":"ref_248","doi-asserted-by":"crossref","first-page":"2589","DOI":"10.1016\/j.ajpath.2011.07.035","article-title":"Endogenous angiogenesis inhibitor blocks tumor growth via direct and indirect effects on tumor microenvironment","volume":"179","author":"Bourboulia","year":"2011","journal-title":"Am. J. Pathol."},{"key":"ref_249","doi-asserted-by":"crossref","first-page":"271","DOI":"10.1016\/S0168-3659(99)00248-5","article-title":"Tumor vascular permeability and the EPR effect in macromolecular therapeutics: A review","volume":"65","author":"Maeda","year":"2000","journal-title":"J. Control. Release"},{"key":"ref_250","doi-asserted-by":"crossref","unstructured":"Batra, J., Robinson, J., Mehner, C., Hockla, A., Miller, E., Radisky, D.C., and Radisky, E.S. (2012). PEGylation extends circulation half-life while preserving in vitro and in vivo activity of tissue inhibitor of metalloproteinases-1 (TIMP-1). PLoS ONE, 7.","DOI":"10.1371\/journal.pone.0050028"},{"key":"ref_251","doi-asserted-by":"crossref","unstructured":"Yang, S.W., Chanda, D., Cody, J.J., Rivera, A.A., Waehler, R., Siegal, G.P., Douglas, J.T., and Ponnazhagan, S. (2011). Conditionally replicating adenovirus expressing TIMP2 increases survival in a mouse model of disseminated ovarian cancer. PLoS ONE, 6.","DOI":"10.1371\/journal.pone.0025131"},{"key":"ref_252","doi-asserted-by":"crossref","first-page":"538","DOI":"10.1158\/1078-0432.CCR-10-1628","article-title":"Conditionally replicating adenovirus expressing TIMP2 for ovarian cancer therapy","volume":"17","author":"Yang","year":"2011","journal-title":"Clin. Cancer Res."}],"container-title":["International Journal of Molecular Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1422-0067\/19\/2\/450\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T14:53:36Z","timestamp":1760194416000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1422-0067\/19\/2\/450"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2018,2,2]]},"references-count":252,"journal-issue":{"issue":"2","published-online":{"date-parts":[[2018,2]]}},"alternative-id":["ijms19020450"],"URL":"https:\/\/doi.org\/10.3390\/ijms19020450","relation":{},"ISSN":["1422-0067"],"issn-type":[{"type":"electronic","value":"1422-0067"}],"subject":[],"published":{"date-parts":[[2018,2,2]]}}}