{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,29]],"date-time":"2026-07-29T03:12:24Z","timestamp":1785294744022,"version":"3.55.0"},"reference-count":220,"publisher":"MDPI AG","issue":"4","license":[{"start":{"date-parts":[[2026,2,20]],"date-time":"2026-02-20T00:00:00Z","timestamp":1771545600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"crossref","award":["EY10101"],"award-info":[{"award-number":["EY10101"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"crossref","award":["EY033758"],"award-info":[{"award-number":["EY033758"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"crossref","award":["EY01792"],"award-info":[{"award-number":["EY01792"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"crossref","award":["EY035681"],"award-info":[{"award-number":["EY035681"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/100000738","name":"Department of Veterans Affairs","doi-asserted-by":"crossref","award":["I01 BX004234"],"award-info":[{"award-number":["I01 BX004234"]}],"id":[{"id":"10.13039\/100000738","id-type":"DOI","asserted-by":"crossref"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>Corneal neovascularization (CoNV) disrupts the natural avascularity of the cornea, leading to loss of transparency and visual impairment. Among matrix metalloproteinases (MMP), MMP-14, a membrane-bound MMP, plays a central role in CoNV through matrix remodeling, activation of pro-MMP-2, modulation of growth factors-induced signaling, and regulation of vascular endothelial cell behavior. Under pathogenic conditions, MMP-14 promotes angiogenesis by degrading stromal collagen, enhancing vascular endothelial growth factor (VEGF) signaling, and stimulating vascular endothelial cell migration. However, MMP-14 can also exert anti-angiogenic effects by generating endostatin-like fragments such as neostatin-14. MMP-14 also participates in corneal wound healing and lymphangiogenesis, making it a promising therapeutic target for CoNV. Standard therapies for CoNV, such as corticosteroids, immunosuppressants, and anti-VEGF agents, remain partially effective. Novel strategies targeting MMP-14, including small-molecule inhibitors, selective use of TIMP-2, and recombinant antibodies, are being explored. A deeper understanding of how membrane-bound MMP-14 is regulated and functions in different contexts may allow better modulation of angiogenesis, ultimately preserving corneal clarity and visual function after injury or inflammation.<\/jats:p>","DOI":"10.3390\/ijms27042027","type":"journal-article","created":{"date-parts":[[2026,2,20]],"date-time":"2026-02-20T15:57:11Z","timestamp":1771603031000},"page":"2027","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":2,"title":["Matrix Metalloproteinase 14 in Corneal Neovascularization"],"prefix":"10.3390","volume":"27","author":[{"ORCID":"https:\/\/orcid.org\/0009-0008-4206-6768","authenticated-orcid":false,"given":"Kaley","family":"Qin","sequence":"first","affiliation":[{"name":"Department of Ophthalmology and Visual Sciences, Illinois Eye and Ear Infirmary, College of Medicine, University of Illinois Chicago, Chicago, IL 60612, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8619-4154","authenticated-orcid":false,"given":"Nicholas W.","family":"Setter","sequence":"additional","affiliation":[{"name":"Department of Ophthalmology and Visual Sciences, Illinois Eye and Ear Infirmary, College of Medicine, University of Illinois Chicago, Chicago, IL 60612, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lily","family":"Yu","sequence":"additional","affiliation":[{"name":"Department of Ophthalmology and Visual Sciences, Illinois Eye and Ear Infirmary, College of Medicine, University of Illinois Chicago, Chicago, IL 60612, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Zahra","family":"Vasi","sequence":"additional","affiliation":[{"name":"Department of Ophthalmology and Visual Sciences, Illinois Eye and Ear Infirmary, College of Medicine, University of Illinois Chicago, Chicago, IL 60612, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Weiyu","family":"Wu","sequence":"additional","affiliation":[{"name":"Department of Ophthalmology and Visual Sciences, Illinois Eye and Ear Infirmary, College of Medicine, University of Illinois Chicago, Chicago, IL 60612, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yunjeong","family":"Hwang","sequence":"additional","affiliation":[{"name":"Department of Ophthalmology and Visual Sciences, Illinois Eye and Ear Infirmary, College of Medicine, University of Illinois Chicago, Chicago, IL 60612, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2570-8120","authenticated-orcid":false,"given":"Hyun","family":"Lee","sequence":"additional","affiliation":[{"name":"Department of Pharmaceutical Sciences, College of Pharmacy and Biophysics Core, the Research Resource Center, University of Illinois at Chicago, Chicago, IL 60607, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-7993-1144","authenticated-orcid":false,"given":"Jin-Hong","family":"Chang","sequence":"additional","affiliation":[{"name":"Department of Ophthalmology and Visual Sciences, Illinois Eye and Ear Infirmary, College of Medicine, University of Illinois Chicago, Chicago, IL 60612, USA"},{"name":"Jesse Brown Veterans Affairs Medical Center, Chicago, IL 60612, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mark I.","family":"Rosenblatt","sequence":"additional","affiliation":[{"name":"Department of Ophthalmology and Visual Sciences, Illinois Eye and Ear Infirmary, College of Medicine, University of Illinois Chicago, Chicago, IL 60612, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2561-8187","authenticated-orcid":false,"given":"Kyuyeon","family":"Han","sequence":"additional","affiliation":[{"name":"Department of Ophthalmology and Visual Sciences, Illinois Eye and Ear Infirmary, College of Medicine, University of Illinois Chicago, Chicago, IL 60612, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Dimitri T.","family":"Azar","sequence":"additional","affiliation":[{"name":"Department of Ophthalmology and Visual Sciences, Illinois Eye and Ear Infirmary, College of Medicine, University of Illinois Chicago, Chicago, IL 60612, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2026,2,20]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/bs.pmbts.2017.02.005","article-title":"Biochemical and Biological Attributes of Matrix Metalloproteinases","volume":"Volume 147","author":"Cui","year":"2017","journal-title":"Progress in Molecular Biology and Translational Science"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"4141","DOI":"10.1158\/0008-5472.CAN-09-4466","article-title":"Matrix metalloproteinase-14 (MT1-MMP)-mediated endoglin shedding inhibits tumor angiogenesis","volume":"70","author":"Hawinkels","year":"2010","journal-title":"Cancer Res."},{"key":"ref_3","first-page":"555","article-title":"MT1-MMP expression promotes tumor growth and angiogenesis through an up-regulation of vascular endothelial growth factor expression","volume":"16","author":"Sounni","year":"2002","journal-title":"FASEB J. Off. Publ. Fed. Am. Soc. Exp. Biol."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"2446","DOI":"10.1074\/jbc.272.4.2446","article-title":"Membrane type 1 matrix metalloproteinase digests interstitial collagens and other extracellular matrix macromolecules","volume":"272","author":"Ohuchi","year":"1997","journal-title":"J. Biol. Chem."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"757","DOI":"10.1083\/jcb.200405001","article-title":"MT1-MMP\u2013dependent neovessel formation within the confines of the three-dimensional extracellular matrix","volume":"167","author":"Chun","year":"2004","journal-title":"J. Cell Biol."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"77","DOI":"10.1007\/s10555-006-7891-z","article-title":"MT1-MMP: Universal or particular player in angiogenesis?","volume":"25","author":"Genis","year":"2006","journal-title":"Cancer Metastasis Rev."},{"key":"ref_7","first-page":"264","article-title":"Corneal Angiogenic Privilege: Angiogenic and Antiangiogenic Factors in Corneal Avascularity, Vasculogenesis, and Wound Healing (an American Ophthalmological Society Thesis)","volume":"104","author":"Azar","year":"2006","journal-title":"Trans. Am. Ophthalmol. Soc."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"108457","DOI":"10.1016\/j.exer.2021.108457","article-title":"Corneal angiogenic privilege and its failure","volume":"204","author":"Gaudenzi","year":"2021","journal-title":"Exp. Eye Res."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"507","DOI":"10.1016\/S0008-6363(00)00281-9","article-title":"Molecular mechanisms of blood vessel growth","volume":"49","author":"Conway","year":"2001","journal-title":"Cardiovasc. Res."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"108363","DOI":"10.1016\/j.exer.2020.108363","article-title":"Corneal neovascularization","volume":"202","author":"Nicholas","year":"2021","journal-title":"Exp. Eye Res."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"230","DOI":"10.1177\/10454411950060030501","article-title":"The Pathophysiology of Angiogenesis","volume":"6","author":"Polverini","year":"1995","journal-title":"Crit. Rev. Oral Biol. Med."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"1519","DOI":"10.1242\/dev.124.8.1519","article-title":"Matrix metalloproteinases regulate morphogenesis, migration and remodeling of epithelium, tongue skeletal muscle and cartilage in the mandibular arch","volume":"124","author":"Chin","year":"1997","journal-title":"Development"},{"key":"ref_13","doi-asserted-by":"crossref","unstructured":"Edwards, D., H\u00f8yer-Hansen, G., Blasi, F., and Sloane, B.F. (2008). Cytokine Substrates: MMP Regulation of Inflammatory Signaling Molecules. The Cancer Degradome, Springer.","DOI":"10.1007\/978-0-387-69057-5"},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"1014","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. USA"},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"H919","DOI":"10.1152\/ajpheart.00577.2012","article-title":"The history of matrix metalloproteinases: Milestones, myths, and misperceptions","volume":"303","author":"Iyer","year":"2012","journal-title":"Am. J. Physiol. Heart Circ. Physiol."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"714","DOI":"10.1124\/pharmrev.121.000349","article-title":"Matrix Metalloproteinases: From Molecular Mechanisms to Physiology, Pathophysiology, and Pharmacology","volume":"74","author":"Thode","year":"2022","journal-title":"Pharmacol. Rev."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"32","DOI":"10.1016\/j.biochi.2019.07.001","article-title":"MMP-14 degrades tropoelastin and elastin","volume":"165","author":"Miekus","year":"2019","journal-title":"Biochimie"},{"key":"ref_18","doi-asserted-by":"crossref","unstructured":"Caban, M., Owczarek, K., and Lewandowska, U. (2022). The Role of Metalloproteinases and Their Tissue Inhibitors on Ocular Diseases: Focusing on Potential Mechanisms. Int. J. Mol. Sci., 23.","DOI":"10.3390\/ijms23084256"},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"226","DOI":"10.1186\/s12967-019-1975-3","article-title":"Clinicohistopathological implications of MMP\/VEGF expression in retinoblastoma: A combined meta-analysis and bioinformatics analysis","volume":"17","author":"Zhu","year":"2019","journal-title":"J. Transl. Med."},{"key":"ref_20","doi-asserted-by":"crossref","unstructured":"Kim, M.H., and Lim, S.H. (2022). Matrix Metalloproteinases and Glaucoma. Biomolecules, 12.","DOI":"10.3390\/biom12101368"},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"18","DOI":"10.1167\/iovs.62.3.18","article-title":"A Porcine Organ-Culture Glaucoma Model Mimicking Trabecular Meshwork Damage Using Oxidative Stress","volume":"62","author":"Snider","year":"2021","journal-title":"Investig. Ophthalmol. Vis. Sci."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"597","DOI":"10.1038\/labinvest.3700251","article-title":"Matrix metalloproteinases in early diabetic retinopathy and their role in alteration of the blood-retinal barrier","volume":"85","author":"Giebel","year":"2005","journal-title":"Lab. Investig. J. Tech. Methods Pathol."},{"key":"ref_23","doi-asserted-by":"crossref","unstructured":"Garc\u00eda-Onrubia, L., Valent\u00edn-Bravo, F.J., Coco-Martin, R.M., Gonz\u00e1lez-Sarmiento, R., Pastor, J.C., Usategui-Mart\u00edn, R., and Pastor-Idoate, S. (2020). Matrix Metalloproteinases in Age-Related Macular Degeneration (AMD). Int. J. Mol. Sci., 21.","DOI":"10.3390\/ijms21165934"},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"108523","DOI":"10.1016\/j.exer.2021.108523","article-title":"Inhibition of matrix metalloproteinase-9 for the treatment of dry eye syndrome; a review study","volume":"205","author":"Shoari","year":"2021","journal-title":"Exp. Eye Res."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"1376","DOI":"10.1111\/j.1523-1755.2004.00900.x","article-title":"TNF-alpha and IL-1beta-mediated regulation of MMP-9 and TIMP-1 in renal proximal tubular cells","volume":"66","author":"Nee","year":"2004","journal-title":"Kidney Int."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"14351","DOI":"10.1038\/s41598-023-41514-6","article-title":"TNFalpha induces matrix metalloproteinase-9 expression in monocytic cells through ACSL1\/JNK\/ERK\/NF-kB signaling pathways","volume":"13","author":"Akhter","year":"2023","journal-title":"Sci. Rep."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"61","DOI":"10.1016\/S0002-9440(10)62232-8","article-title":"Matrix metalloproteinase-9 knockout confers resistance to corneal epithelial barrier disruption in experimental dry eye","volume":"166","author":"Pflugfelder","year":"2005","journal-title":"Am. J. Pathol."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"189","DOI":"10.1016\/j.jtos.2015.10.004","article-title":"The Matrix Metalloproteinase 9 Point-of-Care Test in Dry Eye","volume":"14","author":"Lanza","year":"2016","journal-title":"Ocul. Surf."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"387","DOI":"10.1016\/j.ajo.2025.05.033","article-title":"TFOS DEWS III: Diagnostic Methodology","volume":"279","author":"Wolffsohn","year":"2025","journal-title":"Am. J. Ophthalmol."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"S59","DOI":"10.1097\/ICO.0000000000000995","article-title":"Regulatory Mechanism of Collagen Degradation by Keratocytes and Corneal Inflammation: The Role of Urokinase-Type Plasminogen Activator","volume":"35","author":"Sugioka","year":"2016","journal-title":"Cornea"},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"929","DOI":"10.1016\/j.survophthal.2023.06.007","article-title":"The role of matrix metalloproteinases in infectious corneal ulcers","volume":"68","author":"Borroni","year":"2023","journal-title":"Surv. Ophthalmol."},{"key":"ref_32","doi-asserted-by":"crossref","unstructured":"Park, J.Y., Choi, Y., Kim, H.D., Kuo, H.H., Chang, Y.C., and Kim, C.H. (2025). Matrix Metalloproteinases and Their Inhibitors in the Pathogenesis of Epithelial Differentiation, Vascular Disease, Endometriosis, and Ocular Fibrotic Pterygium. Int. J. Mol. Sci., 26.","DOI":"10.3390\/ijms26125553"},{"key":"ref_33","first-page":"71","article-title":"Overexpression of collagenase (MMP-1) and stromelysin (MMP-3) by pterygium head fibroblasts","volume":"119","author":"Li","year":"2001","journal-title":"Arch. Ophthalmol."},{"key":"ref_34","first-page":"1963","article-title":"Active matrilysin (MMP-7) in human pterygia: Potential role in angiogenesis","volume":"42","author":"Coroneo","year":"2001","journal-title":"Investig. Ophthalmol. Vis. Sci."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"4588","DOI":"10.1167\/iovs.08-3147","article-title":"Increased expression of gelatinase (MMP-2 and MMP-9) in pterygia and pterygium fibroblasts with disease progression and activation of protein kinase C","volume":"50","author":"Yang","year":"2009","journal-title":"Investig. Ophthalmol. Vis. Sci."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"1156","DOI":"10.1167\/iovs.18-24743","article-title":"Bromfenac Inhibits TGF-beta1-Induced Fibrotic Effects in Human Pterygium and Conjunctival Fibroblasts","volume":"60","author":"Chen","year":"2019","journal-title":"Investig. Ophthalmol. Vis. Sci."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"493","DOI":"10.1083\/jcb.200109100","article-title":"The integrin alpha(v)beta8 mediates epithelial homeostasis through MT1-MMP-dependent activation of TGF-beta1","volume":"157","author":"Mu","year":"2002","journal-title":"J. Cell Biol."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"61","DOI":"10.1038\/370061a0","article-title":"A matrix metalloproteinase expressed on the surface of invasive tumour cells","volume":"370","author":"Sato","year":"1994","journal-title":"Nature"},{"key":"ref_39","doi-asserted-by":"crossref","unstructured":"Lv, X., Lai, L., Xu, Y., Sun, M., Li, Y., Song, Y., Wang, N., and Zhang, F. (2023). Effects of riboflavin\/ultraviolet-A scleral collagen cross-linking on regional scleral thickness and expression of MMP-2 and MT1-MMP in myopic guinea pigs. PLoS ONE, 18.","DOI":"10.1371\/journal.pone.0279111"},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"16098","DOI":"10.1074\/jbc.273.26.16098","article-title":"TIMP-2 promotes activation of progelatinase A by membrane-type 1 matrix metalloproteinase immobilized on agarose beads","volume":"273","author":"Kinoshita","year":"1998","journal-title":"J. Biol. Chem."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"13053","DOI":"10.1074\/jbc.M709327200","article-title":"The second dimer interface of MT1-MMP, the transmembrane domain, is essential for ProMMP-2 activation on the cell surface","volume":"283","author":"Itoh","year":"2008","journal-title":"J. Biol. Chem."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"2878","DOI":"10.1096\/fj.201700919RRR","article-title":"MMP14 is a novel target of PTH signaling in osteocytes that controls resorption by regulating soluble RANKL production","volume":"32","author":"Hancock","year":"2018","journal-title":"FASEB J."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"3167","DOI":"10.1007\/s00018-019-03178-2","article-title":"Metalloproteinases and their tissue inhibitors in Alzheimer\u2019s disease and other neurodegenerative disorders","volume":"76","author":"Rivera","year":"2019","journal-title":"Cell. Mol. Life Sci."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1186\/s13048-021-00852-7","article-title":"The role of MMP-14 in ovarian cancer: A systematic review","volume":"14","author":"Vos","year":"2021","journal-title":"J. Ovarian Res."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"207","DOI":"10.1016\/j.matbio.2015.03.004","article-title":"Membrane-type matrix metalloproteinases: Their functions and regulations","volume":"44\u201346","author":"Itoh","year":"2015","journal-title":"Matrix Biol."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"4782","DOI":"10.1093\/emboj\/20.17.4782","article-title":"Homophilic complex formation of MT1-MMP facilitates proMMP-2 activation on the cell surface and promotes tumor cell invasion","volume":"20","author":"Itoh","year":"2001","journal-title":"EMBO J."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"319","DOI":"10.1042\/BJ20110424","article-title":"Dimerization of MT1-MMP during cellular invasion detected by fluorescence resonance energy transfer","volume":"440","author":"Itoh","year":"2011","journal-title":"Biochem. J."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"6244","DOI":"10.1038\/onc.2017.219","article-title":"The interactome of metabolic enzyme carbonic anhydrase IX reveals novel roles in tumor cell migration and invadopodia\/MMP14-mediated invasion","volume":"36","author":"Swayampakula","year":"2017","journal-title":"Oncogene"},{"key":"ref_49","first-page":"10","article-title":"Matrix Metalloproteinases -14, -9 and -2 are Localized to the Podosome and Involved in Podosome Development in the A7r5 Smooth Muscle Cell","volume":"5","author":"Thatcher","year":"2017","journal-title":"J. Cardiobiol."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"3949","DOI":"10.1093\/emboj\/cdf411","article-title":"CD44 directs membrane-type 1 matrix metalloproteinase to lamellipodia by associating with its hemopexin-like domain","volume":"21","author":"Mori","year":"2002","journal-title":"EMBO J."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"35126","DOI":"10.1074\/jbc.M113.496067","article-title":"MT-LOOP-dependent Localization of Membrane Type I Matrix Metalloproteinase (MT1-MMP) to the Cell Adhesion Complexes Promotes Cancer Cell Invasion","volume":"288","author":"Woskowicz","year":"2013","journal-title":"J. Biol. Chem."},{"key":"ref_52","doi-asserted-by":"crossref","unstructured":"Maybee, D.V., Ink, N.L., and Ali, M.A.M. (2022). Novel Roles of MT1-MMP and MMP-2: Beyond the Extracellular Milieu. Int. J. Mol. Sci., 23.","DOI":"10.20944\/preprints202206.0305.v1"},{"key":"ref_53","doi-asserted-by":"crossref","unstructured":"Tanaka, N., and Sakamoto, T. (2023). MT1-MMP as a Key Regulator of Metastasis. Cells, 12.","DOI":"10.3390\/cells12172187"},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1016\/S0378-1119(99)00549-1","article-title":"Structural analysis and promoter characterization of the human membrane-type matrix metalloproteinase-1 (MT1-MMP) gene","volume":"242","author":"Lohi","year":"2000","journal-title":"Gene"},{"key":"ref_55","doi-asserted-by":"crossref","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":"ref_56","doi-asserted-by":"crossref","first-page":"22679","DOI":"10.1074\/jbc.274.32.22679","article-title":"Egr-1 mediates extracellular matrix-driven transcription of membrane type 1 matrix metalloproteinase in endothelium","volume":"274","author":"Haas","year":"1999","journal-title":"J. Biol. Chem."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"45","DOI":"10.1007\/s10585-015-9756-8","article-title":"Tip60 regulates MT1-MMP transcription and invasion of glioblastoma cells through NF-kappaB pathway","volume":"33","author":"Takino","year":"2016","journal-title":"Clin. Exp. Metastasis"},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"735","DOI":"10.1093\/ndt\/gfn576","article-title":"Characterization of the transcriptional regulation of the human MT1-MMP gene and association of risk reduction for focal-segmental glomerulosclerosis with two functional promoter SNPs","volume":"24","author":"Munkert","year":"2009","journal-title":"Nephrol. Dial. Transplant."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"61107","DOI":"10.18632\/oncotarget.11243","article-title":"Interleukin-6 increases matrix metalloproteinase-14 (MMP-14) levels via down-regulation of p53 to drive cancer progression","volume":"7","author":"Cathcart","year":"2016","journal-title":"Oncotarget"},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"12727","DOI":"10.1074\/jbc.M900273200","article-title":"Epigenetic control of the invasion-promoting MT1-MMP\/MMP-2\/TIMP-2 axis in cancer cells","volume":"284","author":"Chernov","year":"2009","journal-title":"J. Biol. Chem."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"9531","DOI":"10.1038\/s41598-018-27739-w","article-title":"PROX1 is a transcriptional regulator of MMP14","volume":"8","author":"Gramolelli","year":"2018","journal-title":"Sci. Rep."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"460","DOI":"10.1007\/s12272-022-01396-0","article-title":"STAT3 mediates RCP-induced cancer cell invasion through the NF-kappaB\/Slug\/MT1-MMP signaling cascade","volume":"45","author":"Cho","year":"2022","journal-title":"Arch. Pharmacal Res."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"1996","DOI":"10.1007\/s11427-024-2884-2","article-title":"VPS35\/Retromer-dependent MT1-MMP regulation confers melanoma metastasis","volume":"68","author":"Hao","year":"2025","journal-title":"Sci. China Life Sci."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"39042","DOI":"10.1074\/jbc.M404958200","article-title":"Differential regulation of membrane type 1-matrix metalloproteinase activity by ERK 1\/2- and p38 MAPK-modulated tissue inhibitor of metalloproteinases 2 expression controls transforming growth factor-beta1-induced pericellular collagenolysis","volume":"279","author":"Munshi","year":"2004","journal-title":"J. Biol. Chem."},{"key":"ref_65","doi-asserted-by":"crossref","unstructured":"Gonzalez-Avila, G., Sommer, B., Flores-Soto, E., and Aquino-Galvez, A. (2023). Hypoxic Effects on Matrix Metalloproteinases\u2019 Expression in the Tumor Microenvironment and Therapeutic Perspectives. Int. J. Mol. Sci., 24.","DOI":"10.3390\/ijms242316887"},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"186","DOI":"10.1186\/s13148-019-0786-y","article-title":"DNMT1 recruited by EZH2-mediated silencing of miR-484 contributes to the malignancy of cervical cancer cells through MMP14 and HNF1A","volume":"11","author":"Hu","year":"2019","journal-title":"Clin. Epigenet."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"787","DOI":"10.1016\/j.omtn.2021.08.022","article-title":"lncRNA MELTF-AS1 facilitates osteosarcoma metastasis by modulating MMP14 expression","volume":"26","author":"Ding","year":"2021","journal-title":"Mol. Ther. Nucleic Acids"},{"key":"ref_68","first-page":"10313","article-title":"LncRNA BLACAT1 regulates the viability, migration and invasion of oral squamous cell carcinoma cells by targeting miR-142-5p","volume":"23","author":"Dai","year":"2019","journal-title":"Eur. Rev. Med. Pharmacol. Sci."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"811","DOI":"10.1042\/BST20180363","article-title":"MT1-MMP-dependent cell migration: Proteolytic and non-proteolytic mechanisms","volume":"47","author":"Gifford","year":"2019","journal-title":"Biochem. Soc. Trans."},{"key":"ref_70","first-page":"2820","article-title":"A specific subset of RabGTPases controls cell surface exposure of MT1-MMP, extracellular matrix degradation and three-dimensional invasion of macrophages","volume":"126","author":"Wiesner","year":"2013","journal-title":"J. Cell Sci."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"1559","DOI":"10.1182\/blood-2009-12-257089","article-title":"KIF5B and KIF3A\/KIF3B kinesins drive MT1-MMP surface exposure, CD44 shedding, and extracellular matrix degradation in primary macrophages","volume":"116","author":"Wiesner","year":"2010","journal-title":"Blood"},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.matbio.2022.01.004","article-title":"Coordination of two kinesin superfamily motor proteins, KIF3A and KIF13A, is essential for pericellular matrix degradation by membrane-type 1 matrix metalloproteinase (MT1-MMP) in cancer cells","volume":"107","author":"Gifford","year":"2022","journal-title":"Matrix Biol."},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"3158","DOI":"10.1111\/j.1742-4658.2010.07723.x","article-title":"Golgi reassembly stacking protein 55 interacts with membrane-type (MT) 1-matrix metalloprotease (MMP) and furin and plays a role in the activation of the MT1-MMP zymogen","volume":"277","author":"Roghi","year":"2010","journal-title":"FEBS J."},{"key":"ref_74","first-page":"4707","article-title":"ADAM12 redistributes and activates MMP-14, resulting in gelatin degradation, reduced apoptosis and increased tumor growth","volume":"126","author":"Albrechtsen","year":"2013","journal-title":"J. Cell Sci."},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1111\/febs.16586","article-title":"MT1-MMP and ADAM10\/17 exhibit a remarkable overlap of shedding properties","volume":"290","author":"Werny","year":"2023","journal-title":"FEBS J."},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"1176","DOI":"10.1016\/j.devcel.2012.04.014","article-title":"MT1-MMP inactivates ADAM9 to regulate FGFR2 signaling and calvarial osteogenesis","volume":"22","author":"Chan","year":"2012","journal-title":"Dev. Cell"},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"36","DOI":"10.1016\/j.matbio.2025.01.004","article-title":"Decoding the MMP14 integrin link: Key player in the secretome landscape","volume":"136","author":"Niland","year":"2025","journal-title":"Matrix Biol."},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"jcs239152","DOI":"10.1242\/jcs.239152","article-title":"beta1 integrin-mediated signaling regulates MT1-MMP phosphorylation to promote tumor cell invasion","volume":"133","author":"Grafinger","year":"2020","journal-title":"J. Cell Sci."},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"1133","DOI":"10.1016\/j.biocel.2013.02.020","article-title":"The tetraspanin network modulates MT1-MMP cell surface trafficking","volume":"45","author":"Schroder","year":"2013","journal-title":"Int. J. Biochem. Cell Biol."},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"858","DOI":"10.5483\/BMBRep.2008.41.12.858","article-title":"Caveolin-1 inhibits membrane-type 1 matrix metalloproteinase activity","volume":"41","author":"Kim","year":"2008","journal-title":"BMB Rep."},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"8","DOI":"10.1038\/labinvest.3700003","article-title":"Upregulation of tissue inhibitor of metalloproteinases (TIMP)-2 promotes matrix metalloproteinase (MMP)-2 activation and cell invasion in a human glioblastoma cell line","volume":"84","author":"Lu","year":"2004","journal-title":"Lab. Investig."},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"478","DOI":"10.1016\/j.survophthal.2015.11.006","article-title":"Matrix metalloproteinase 14 modulates signal transduction and angiogenesis in the cornea","volume":"61","author":"Chang","year":"2016","journal-title":"Surv. Ophthalmol."},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"2339","DOI":"10.1158\/0008-5472.CAN-11-4149","article-title":"Novel MT1-MMP small-molecule inhibitors based on insights into hemopexin domain function in tumor growth","volume":"72","author":"Remacle","year":"2012","journal-title":"Cancer Res."},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"11348","DOI":"10.1074\/jbc.M116.720250","article-title":"Thermodynamic Basis of Selectivity in the Interactions of Tissue Inhibitors of Metalloproteinases N-domains with Matrix Metalloproteinases-1, -3, and -14","volume":"291","author":"Zou","year":"2016","journal-title":"J. Biol. Chem."},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"8592","DOI":"10.1074\/jbc.M308708200","article-title":"Differential inhibition of membrane type 3 (MT3)-matrix metalloproteinase (MMP) and MT1-MMP by tissue inhibitor of metalloproteinase (TIMP)-2 and TIMP-3 rgulates pro-MMP-2 activation","volume":"279","author":"Zhao","year":"2004","journal-title":"J. Biol. Chem."},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"12067","DOI":"10.1038\/s41598-020-69008-9","article-title":"TIMP-3 facilitates binding of target metalloproteinases to the endocytic receptor LRP-1 and promotes scavenging of MMP-1","volume":"10","author":"Carreca","year":"2020","journal-title":"Sci. Rep."},{"key":"ref_87","first-page":"3610","article-title":"Tissue inhibitor of metalloproteinases-4 inhibits but does not support the activation of gelatinase A via efficient inhibition of membrane type 1-matrix metalloproteinase","volume":"61","author":"Bigg","year":"2001","journal-title":"Cancer Res."},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"85","DOI":"10.1186\/1476-4598-7-85","article-title":"Tissue inhibitor of metalloproteinases-4. The road less traveled","volume":"7","author":"Ceballos","year":"2008","journal-title":"Mol. Cancer"},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"617","DOI":"10.1111\/j.1365-2443.2009.01293.x","article-title":"Cytoplasmic tail of MT1-MMP regulates macrophage motility independently from its protease activity","volume":"14","author":"Sakamoto","year":"2009","journal-title":"Genes Cells"},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"30350","DOI":"10.1074\/jbc.M109.019216","article-title":"Mint3 enhances the activity of hypoxia-inducible factor-1 (HIF-1) in macrophages by suppressing the activity of factor inhibiting HIF-1","volume":"284","author":"Sakamoto","year":"2009","journal-title":"J. Biol. Chem."},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"395","DOI":"10.1101\/gad.178749.111","article-title":"MT1-MMP regulates the PI3Kdelta.Mi-2\/NuRD-dependent control of macrophage immune function","volume":"26","author":"Xiong","year":"2012","journal-title":"Genes Dev."},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"601","DOI":"10.1007\/s00018-005-5426-3","article-title":"The role of VEGF receptors in angiogenesis; complex partnerships","volume":"63","year":"2006","journal-title":"Cell. Mol. Life Sci."},{"key":"ref_93","doi-asserted-by":"crossref","unstructured":"Wang, X., Bove, A.M., Simone, G., and Ma, B. (2020). Molecular Bases of VEGFR-2-Mediated Physiological Function and Pathological Role. Front. Cell Dev. Biol., 8.","DOI":"10.3389\/fcell.2020.599281"},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"3336","DOI":"10.1182\/blood.V87.8.3336.bloodjournal8783336","article-title":"Migration of human monocytes in response to vascular endothelial growth factor (VEGF) is mediated via the VEGF receptor flt-1","volume":"87","author":"Barleon","year":"1996","journal-title":"Blood"},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"993","DOI":"10.1038\/nature05249","article-title":"Corneal avascularity is due to soluble VEGF receptor-1","volume":"443","author":"Ambati","year":"2006","journal-title":"Nature"},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"5450","DOI":"10.1167\/iovs.14-16248","article-title":"MMP14 Cleavage of VEGFR1 in the Cornea Leads to a VEGF-Trap Antiangiogenic Effect","volume":"56","author":"Han","year":"2015","journal-title":"Investig. Ophthalmol. Vis. Sci."},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"2321","DOI":"10.1167\/iovs.18-26277","article-title":"MMP14-Containing Exosomes Cleave VEGFR1 and Promote VEGFA-Induced Migration and Proliferation of Vascular Endothelial Cells","volume":"60","author":"Han","year":"2019","journal-title":"Investig. Ophthalmol. Vis. Sci."},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"328","DOI":"10.1007\/s10792-025-03691-3","article-title":"miR-497 knockout aggravates alkali burn-induced corneal neovascularization via VEGFA and FGF2 pathways in mice models","volume":"45","author":"Guo","year":"2025","journal-title":"Int. Ophthalmol."},{"key":"ref_99","first-page":"2894","article-title":"Differential expression of MT1-MMP (MMP-14) and collagenase III (MMP-13) genes in normal and wounded rat corneas","volume":"41","author":"Ye","year":"2000","journal-title":"Investig. Ophthalmol. Vis. Sci."},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"3313","DOI":"10.1167\/iovs.16-19420","article-title":"Proangiogenic Interactions of Vascular Endothelial MMP14 With VEGF Receptor 1 in VEGFA-Mediated Corneal Angiogenesis","volume":"57","author":"Han","year":"2016","journal-title":"Investig. Ophthalmol. Vis. Sci."},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"3601","DOI":"10.1016\/j.febslet.2005.05.043","article-title":"Functional characterization of neostatins, the MMP-derived, enzymatic cleavage products of type XVIII collagen","volume":"579","author":"Chang","year":"2005","journal-title":"FEBS Lett."},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"541","DOI":"10.1159\/000226222","article-title":"MT1-MMP-mediated Cleavage of Decorin in Corneal Angiogenesis","volume":"46","author":"Mimura","year":"2009","journal-title":"J. Vasc. Res."},{"key":"ref_103","doi-asserted-by":"crossref","unstructured":"M\u00e9ndez-Vald\u00e9s, G., G\u00f3mez-Hevia, F., Lillo-Moya, J., Gonz\u00e1lez-Fern\u00e1ndez, T., Abelli, J., Cereceda-Cornejo, A., Bragato, M.C., Saso, L., and Rodrigo, R. (2023). Endostatin and Cancer Therapy: A Novel Potential Alternative to Anti-VEGF Monoclonal Antibodies. Biomedicines, 11.","DOI":"10.3390\/biomedicines11030718"},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"3361","DOI":"10.3748\/wjg.v10.i22.3361","article-title":"Effects of endostatin on expression of vascular endothelial growth factor and its receptors and neovascularization in colonic carcinoma implanted in nude mice","volume":"10","author":"Jia","year":"2004","journal-title":"World J. Gastroenterol."},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"2037","DOI":"10.1242\/jcs.01061","article-title":"EphA2 receptor tyrosine kinase regulates endothelial cell migration and vascular assembly through phosphoinositide 3-kinase-mediated Rac1 GTPase activation","volume":"117","author":"Caughron","year":"2004","journal-title":"J. Cell Sci."},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"467","DOI":"10.1083\/jcb.201205176","article-title":"EphA2 cleavage by MT1-MMP triggers single cancer cell invasion via homotypic cell repulsion","volume":"201","author":"Sugiyama","year":"2013","journal-title":"J. Cell Biol."},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"3327","DOI":"10.1158\/0008-5472.CAN-14-2798","article-title":"Proteolysis of EphA2 Converts It from a Tumor Suppressor to an Oncoprotein","volume":"75","author":"Koshikawa","year":"2015","journal-title":"Cancer Res."},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"10824","DOI":"10.1038\/ncomms10824","article-title":"MT1-MMP sheds LYVE-1 on lymphatic endothelial cells and suppresses VEGF-C production to inhibit lymphangiogenesis","volume":"7","author":"Wong","year":"2016","journal-title":"Nat. Commun."},{"key":"ref_109","doi-asserted-by":"crossref","unstructured":"Wang, X., Lu, J., He, Y., Shu, Q., Lin, Y., Su, W., and Wang, P. (2025). MMP14 as a central mediator of TGF-\u03b21\u2212induced extracellular matrix remodeling in graves\u2019 orbitopathy. Front. Endocrinol., 16.","DOI":"10.3389\/fendo.2025.1623842"},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"425","DOI":"10.1016\/0012-1606(91)90300-R","article-title":"Differential roles for two gelatinolytic enzymes of the matrix metalloproteinase family in the remodelling cornea","volume":"147","author":"Matsubara","year":"1991","journal-title":"Dev. Biol."},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"462","DOI":"10.1038\/gt.2010.159","article-title":"Matrix metalloproteinase 14 overexpression reduces corneal scarring","volume":"18","author":"Galiacy","year":"2011","journal-title":"Gene Ther."},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"237","DOI":"10.1182\/blood-2008-12-196451","article-title":"Endothelial cell lumen and vascular guidance tunnel formation requires MT1-MMP\u2013dependent proteolysis in 3-dimensional collagen matrices","volume":"114","author":"Stratman","year":"2009","journal-title":"Blood"},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"1334","DOI":"10.2174\/092986612803521639","article-title":"MT1-MMP Modulates bFGF-Induced VEGF-A Expression in Corneal Fibroblasts","volume":"19","author":"Han","year":"2012","journal-title":"Protein Pept. Lett."},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"208","DOI":"10.1016\/j.preteyeres.2010.01.002","article-title":"Novel aspects of corneal angiogenic and lymphangiogenic privilege","volume":"29","author":"Ellenberg","year":"2010","journal-title":"Prog. Retin. Eye Res."},{"key":"ref_115","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/S0945-053X(98)90121-4","article-title":"Leucine-rich repeat glycoproteins of the extracellular matrix","volume":"17","author":"Hocking","year":"1998","journal-title":"Matrix Biol. J. Int. Soc. Matrix Biol."},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"27935","DOI":"10.1074\/jbc.M414320200","article-title":"Peptides derived from human decorin leucine-rich repeat 5 inhibit angiogenesis","volume":"280","author":"Sulochana","year":"2005","journal-title":"J. Biol. Chem."},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"26","DOI":"10.1006\/mvre.2001.2311","article-title":"Decorin inhibits endothelial migration and tube-like structure formation: Role of thrombospondin-1","volume":"62","author":"Davies","year":"2001","journal-title":"Microvasc. Res."},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"4052","DOI":"10.1073\/pnas.060037197","article-title":"Impaired endochondral ossification and angiogenesis in mice deficient in membrane-type matrix metalloproteinase I","volume":"97","author":"Zhou","year":"2000","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_119","doi-asserted-by":"crossref","unstructured":"Zhang, Z., Warner, K.A., Mantesso, A., and Nor, J.E. (2022). PDGF-BB signaling via PDGFR-beta regulates the maturation of blood vessels generated upon vasculogenic differentiation of dental pulp stem cells. Front. Cell Dev. Biol., 10.","DOI":"10.3389\/fcell.2022.977725"},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"979","DOI":"10.1101\/gad.1294605","article-title":"An MT1-MMP-PDGF receptor-beta axis regulates mural cell investment of the microvasculature","volume":"19","author":"Lehti","year":"2005","journal-title":"Genes Dev."},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"79","DOI":"10.1007\/s10456-008-9101-9","article-title":"Endoglin in angiogenesis and vascular diseases","volume":"11","author":"Goumans","year":"2008","journal-title":"Angiogenesis"},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"3020","DOI":"10.1182\/blood-2003-08-2968","article-title":"Membrane type 1-matrix metalloproteinase (MT1-MMP) cooperates with sphingosine 1-phosphate to induce endothelial cell migration and morphogenic differentiation","volume":"103","author":"Langlois","year":"2004","journal-title":"Blood"},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"321","DOI":"10.1097\/ICO.0b013e3181b1165d","article-title":"Corneal Epithelial MT1-MMP Inhibits Vascular Endothelial Cell Proliferation and Migration","volume":"29","author":"Azar","year":"2010","journal-title":"Cornea"},{"key":"ref_124","doi-asserted-by":"crossref","first-page":"10195","DOI":"10.1074\/jbc.M112.447169","article-title":"Targeting a Single Function of the Multifunctional Matrix Metalloprotease MT1-MMP","volume":"288","author":"Ingvarsen","year":"2013","journal-title":"J. Biol. Chem."},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"e21498","DOI":"10.1096\/fj.202002426RR","article-title":"Matrix stiffness primes lymphatic tube formation directed by vascular endothelial growth factor-C","volume":"35","author":"Alderfer","year":"2021","journal-title":"FASEB J."},{"key":"ref_126","doi-asserted-by":"crossref","unstructured":"Barry, Z., Park, B., and Corson, T.W. (2020). Pharmacological Potential of Small Molecules for Treating Corneal Neovascularization. Molecules, 25.","DOI":"10.3390\/molecules25153468"},{"key":"ref_127","doi-asserted-by":"crossref","unstructured":"Drzyzga, \u0141., \u015apiewak, D., Dorecka, M., and Wygl\u0119dowska-Promie\u0144ska, D. (2024). Available Therapeutic Options for Corneal Neovascularization: A Review. Int. J. Mol. Sci., 25.","DOI":"10.3390\/ijms25105479"},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"100592","DOI":"10.1016\/j.bj.2023.03.005","article-title":"Targeted dexamethasone nano-prodrug for corneal neovascularization management","volume":"47","author":"Yin","year":"2024","journal-title":"Biomed. J."},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"13267","DOI":"10.1038\/s41598-017-13122-8","article-title":"Non-steroidal anti-inflammatory drug delays corneal wound healing by reducing production of 12-hydroxyheptadecatrienoic acid, a ligand for leukotriene B4 receptor 2","volume":"7","author":"Iwamoto","year":"2017","journal-title":"Sci. Rep."},{"key":"ref_130","doi-asserted-by":"crossref","first-page":"140","DOI":"10.1177\/11206721231172236","article-title":"Topical tacrolimus in high-risk corneal transplants","volume":"34","author":"Bernardes","year":"2024","journal-title":"Eur. J. Ophthalmol."},{"key":"ref_131","doi-asserted-by":"crossref","first-page":"19","DOI":"10.5935\/0004-2749.20220004","article-title":"Comparison of the inhibitory effect of topical cyclosporine A 0.1% and topical anti-VEGF application in an experimental model of corneal neovascularization","volume":"85","author":"Ulusoy","year":"2022","journal-title":"Arq. Bras. Oftalmol."},{"key":"ref_132","doi-asserted-by":"crossref","first-page":"256","DOI":"10.4161\/cib.3.3.11456","article-title":"MT1-MMP: A novel component of the macrophage cell fusion machinery","volume":"3","author":"Gonzalo","year":"2010","journal-title":"Commun. Integr. Biol."},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"100492","DOI":"10.1016\/j.xops.2024.100492","article-title":"Suppression of Neovascularization by Topical and Subconjunctival Bevacizumab After High-Risk Corneal Transplantation","volume":"4","author":"Dohlman","year":"2024","journal-title":"Ophthalmol. Sci."},{"key":"ref_134","doi-asserted-by":"crossref","unstructured":"Peng, W.Y., He, L.W., Yin, X.F., Zhou, B.B., Zhou, T., and Zhou, S.Y. (2023). Successful regression of newly formed corneal neovascularization by subconjunctival injection of bevacizumab in patients with chemical burns. Front. Med., 10.","DOI":"10.3389\/fmed.2023.1210765"},{"key":"ref_135","doi-asserted-by":"crossref","first-page":"992","DOI":"10.1097\/ICO.0b013e3182775f8d","article-title":"Topical ranibizumab as a treatment of corneal neovascularization","volume":"32","author":"Ferrari","year":"2013","journal-title":"Cornea"},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"180","DOI":"10.1097\/ICL.0000000000000709","article-title":"Subconjunctival Aflibercept for the Treatment of Formed Corneal Neovascularization","volume":"47","author":"Sella","year":"2021","journal-title":"Eye Contact Lens"},{"key":"ref_137","doi-asserted-by":"crossref","first-page":"348","DOI":"10.1208\/s12248-010-9183-3","article-title":"Ocular drug delivery","volume":"12","author":"Gaudana","year":"2010","journal-title":"AAPS J."},{"key":"ref_138","doi-asserted-by":"crossref","first-page":"120924","DOI":"10.1016\/j.ijpharm.2021.120924","article-title":"Drug delivery to the anterior segment of the eye: A review of current and future treatment strategies","volume":"607","author":"Mofidfar","year":"2021","journal-title":"Int. J. Pharm."},{"key":"ref_139","doi-asserted-by":"crossref","first-page":"7376","DOI":"10.1167\/iovs.14-15257","article-title":"Intrastromal delivery of bevacizumab using microneedles to treat corneal neovascularization","volume":"55","author":"Kim","year":"2014","journal-title":"Investig. Ophthalmol. Vis. Sci."},{"key":"ref_140","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_141","doi-asserted-by":"crossref","first-page":"1742","DOI":"10.1002\/art.11030","article-title":"Broad-spectrum matrix metalloproteinase inhibitor marimastat-induced musculoskeletal side effects in rats","volume":"48","author":"Renkiewicz","year":"2003","journal-title":"Arthritis Rheumatol."},{"key":"ref_142","doi-asserted-by":"crossref","unstructured":"Laronha, H., Carpinteiro, I., Portugal, J., Azul, A., Polido, M., Petrova, K.T., Salema-Oom, M., and Caldeira, J. (2020). Challenges in Matrix Metalloproteinases Inhibition. Biomolecules, 10.","DOI":"10.3390\/biom10050717"},{"key":"ref_143","doi-asserted-by":"crossref","first-page":"38","DOI":"10.1016\/j.drudis.2019.07.013","article-title":"Understanding the variability of the S1\u2032 pocket to improve matrix metalloproteinase inhibitor selectivity profiles","volume":"25","author":"Gimeno","year":"2020","journal-title":"Drug Discov. Today"},{"key":"ref_144","doi-asserted-by":"crossref","first-page":"107465","DOI":"10.1016\/j.pharmthera.2019.107465","article-title":"The past, present and future perspectives of matrix metalloproteinase inhibitors","volume":"207","author":"Li","year":"2020","journal-title":"Pharmacol. Ther."},{"key":"ref_145","doi-asserted-by":"crossref","first-page":"djv017","DOI":"10.1093\/jnci\/djv017","article-title":"Blockade of MMP14 activity in murine breast carcinomas: Implications for macrophages, vessels, and radiotherapy","volume":"107","author":"Ager","year":"2015","journal-title":"J. Natl. Cancer Inst."},{"key":"ref_146","doi-asserted-by":"crossref","first-page":"5238","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":"Bode","year":"1998","journal-title":"EMBO J."},{"key":"ref_147","doi-asserted-by":"crossref","first-page":"5816","DOI":"10.1021\/acs.jmedchem.7b00514","article-title":"Structure-Based Design and Synthesis of Potent and Selective Matrix Metalloproteinase 13 Inhibitors","volume":"60","author":"Choi","year":"2017","journal-title":"J. Med. Chem."},{"key":"ref_148","doi-asserted-by":"crossref","first-page":"248","DOI":"10.2353\/ajpath.2010.091176","article-title":"Matrix Metalloproteinase Inhibitor Batimastat Alleviates Pathology and Improves Skeletal Muscle Function in Dystrophin-Deficient Mice","volume":"177","author":"Kumar","year":"2010","journal-title":"Am. J. Pathol."},{"key":"ref_149","doi-asserted-by":"crossref","first-page":"193","DOI":"10.1007\/BF00210790","article-title":"Phase I trial of a novel matrix metalloproteinase inhibitor batimastat (BB-94) in patients with advanced cancer","volume":"14","author":"Low","year":"1996","journal-title":"Investig. New Drugs"},{"key":"ref_150","doi-asserted-by":"crossref","first-page":"161","DOI":"10.1038\/sj.bjc.6600446","article-title":"A double-blind placebo-controlled, randomised study comparing gemcitabine and marimastat with gemcitabine and placebo as first line therapy in patients with advanced pancreatic cancer","volume":"87","author":"Bramhall","year":"2002","journal-title":"Br. J. Cancer"},{"key":"ref_151","doi-asserted-by":"crossref","first-page":"3447","DOI":"10.1200\/JCO.2001.19.15.3447","article-title":"Marimastat as first-line therapy for patients with unresectable pancreatic cancer: A randomized trial","volume":"19","author":"Bramhall","year":"2001","journal-title":"J. Clin. Oncol."},{"key":"ref_152","doi-asserted-by":"crossref","first-page":"R109","DOI":"10.1186\/ar2315","article-title":"Development of musculoskeletal toxicity without clear benefit after administration of PG-116800, a matrix metalloproteinase inhibitor, to patients with knee osteoarthritis: A randomized, 12-month, double-blind, placebo-controlled study","volume":"9","author":"Krzeski","year":"2007","journal-title":"Arthritis Res. Ther."},{"key":"ref_153","doi-asserted-by":"crossref","first-page":"300","DOI":"10.1016\/j.ygyno.2005.12.020","article-title":"A phase III randomized trial of BAY 12-9566 (tanomastat) as maintenance therapy in patients with advanced ovarian cancer responsive to primary surgery and paclitaxel\/platinum containing chemotherapy: A National Cancer Institute of Canada Clinical Trials Group Study","volume":"102","author":"Hirte","year":"2006","journal-title":"Gynecol. Oncol."},{"key":"ref_154","doi-asserted-by":"crossref","first-page":"2831","DOI":"10.1200\/JCO.2005.04.044","article-title":"Randomized phase III study of matrix metalloproteinase inhibitor BMS-275291 in combination with paclitaxel and carboplatin in advanced non-small-cell lung cancer: National Cancer Institute of Canada-Clinical Trials Group Study BR.18","volume":"23","author":"Leighl","year":"2005","journal-title":"J. Clin. Oncol."},{"key":"ref_155","doi-asserted-by":"crossref","first-page":"178","DOI":"10.1200\/JCO.2000.18.1.178","article-title":"Phase I and pharmacologic study of the specific matrix metalloproteinase inhibitor BAY 12-9566 on a protracted oral daily dosing schedule in patients with solid malignancies","volume":"18","author":"Rowinsky","year":"2000","journal-title":"J. Clin. Oncol."},{"key":"ref_156","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1016\/j.mrrev.2013.01.002","article-title":"Matrix metalloproteinase and its drug targets therapy in solid and hematological malignancies: An overview","volume":"753","author":"Chaudhary","year":"2013","journal-title":"Mutat. Res."},{"key":"ref_157","doi-asserted-by":"crossref","first-page":"1083","DOI":"10.1002\/cncr.23108","article-title":"Phase 1\/2 trial of BMS-275291 in patients with human immunodeficiency virus-related Kaposi sarcoma: A multicenter trial of the AIDS Malignancy Consortium","volume":"112","author":"Brinker","year":"2008","journal-title":"Cancer"},{"key":"ref_158","doi-asserted-by":"crossref","first-page":"1963","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":"ref_159","first-page":"8480","article-title":"Inhibition of angiogenesis and metastasis in two murine models by the matrix metalloproteinase inhibitor, BMS-275291","volume":"61","author":"Naglich","year":"2001","journal-title":"Cancer Res."},{"key":"ref_160","doi-asserted-by":"crossref","first-page":"102","DOI":"10.1016\/j.phrs.2010.10.004","article-title":"Tetracycline compounds with non-antimicrobial organ protective properties: Possible mechanisms of action","volume":"63","author":"Griffin","year":"2011","journal-title":"Pharmacol. Res."},{"key":"ref_161","doi-asserted-by":"crossref","unstructured":"Chan, S.-M., Tseng, C.-L., Huang, W.-H., and Lin, C.-T. (2025). Therapeutic Assessment of Diverse Doxycycline-Based Formulations in Promoting Deep Corneal Wound Healing: Evidence from a Rat Model. Vet. Sci., 12.","DOI":"10.3390\/vetsci12020143"},{"key":"ref_162","doi-asserted-by":"crossref","first-page":"446","DOI":"10.1097\/ICO.0b013e3181605ff9","article-title":"Inhibition of experimental angiogenesis of cornea by various doses of doxycycline and combination of triamcinolone acetonide with low-molecular-weight heparin and doxycycline","volume":"27","author":"Aydin","year":"2008","journal-title":"Cornea"},{"key":"ref_163","doi-asserted-by":"crossref","first-page":"142","DOI":"10.3109\/02713683.2013.833246","article-title":"The Effect of Topical Doxycycline on Corneal Neovascularization","volume":"39","author":"Jovanovic","year":"2014","journal-title":"Curr. Eye Res."},{"key":"ref_164","doi-asserted-by":"crossref","first-page":"297","DOI":"10.1002\/ijc.10168","article-title":"Inhibition of cell proliferation, invasion, tumor growth and metastasis by an oral non-antimicrobial tetracycline analog (COL-3) in a metastatic prostate cancer model","volume":"98","author":"Lokeshwar","year":"2002","journal-title":"Int. J. Cancer"},{"key":"ref_165","doi-asserted-by":"crossref","first-page":"2087","DOI":"10.2174\/138161207781039706","article-title":"Matrix metalloproteinase inhibitors: New challenges in the era of post broad-spectrum inhibitors","volume":"13","author":"Nuti","year":"2007","journal-title":"Curr. Pharm. Des."},{"key":"ref_166","doi-asserted-by":"crossref","unstructured":"Lee, H., Ibrahimi, L., Azar, D.T., and Han, K.-Y. (2023). The Role of Membrane-Type 1 Matrix Metalloproteinase\u2013Substrate Interactions in Pathogenesis. Int. J. Mol. Sci., 24.","DOI":"10.3390\/ijms24032183"},{"key":"ref_167","doi-asserted-by":"crossref","first-page":"72","DOI":"10.1016\/j.bbamcr.2009.08.006","article-title":"To bind zinc or not to bind zinc: An examination of innovative approaches to improved metalloproteinase inhibition","volume":"1803","author":"Jacobsen","year":"2010","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_168","doi-asserted-by":"crossref","first-page":"555","DOI":"10.1021\/acsptsci.2c00125","article-title":"Matrix Metalloproteinase-14 as an Instigator of Fibrosis in Human Pterygium and Its Pharmacological Intervention","volume":"5","author":"Masitas","year":"2022","journal-title":"ACS Pharmacol. Transl. Sci."},{"key":"ref_169","doi-asserted-by":"crossref","first-page":"1573","DOI":"10.1007\/s00417-017-3651-8","article-title":"Blockade of MMP-2 and MMP-9 inhibits corneal lymphangiogenesis","volume":"255","author":"Du","year":"2017","journal-title":"Graefe\u2019s Arch. Clin. Exp. Ophthalmol."},{"key":"ref_170","doi-asserted-by":"crossref","first-page":"2001","DOI":"10.1016\/j.bbamcr.2017.04.011","article-title":"Selective small-molecule inhibitors as chemical tools to define the roles of matrix metalloproteinases in disease","volume":"1864","author":"Meisel","year":"2017","journal-title":"Biochim. Biophys. Acta Mol. Cell Res."},{"key":"ref_171","doi-asserted-by":"crossref","first-page":"168095","DOI":"10.1016\/j.jmb.2023.168095","article-title":"Designed Loop Extension Followed by Combinatorial Screening Confers High Specificity to a Broad Matrix Metalloproteinase Inhibitor","volume":"435","author":"Bonadio","year":"2023","journal-title":"J. Mol. Biol."},{"key":"ref_172","doi-asserted-by":"crossref","first-page":"29431","DOI":"10.18632\/oncotarget.25654","article-title":"Use of a novel camelid-inspired human antibody demonstrates the importance of MMP-14 to cancer stem cell function in the metastatic process","volume":"9","author":"Chen","year":"2018","journal-title":"Oncotarget"},{"key":"ref_173","doi-asserted-by":"crossref","first-page":"1517","DOI":"10.1158\/0008-5472.CAN-08-3255","article-title":"Selective inhibition of matrix metalloproteinase-14 blocks tumor growth, invasion, and angiogenesis","volume":"69","author":"Devy","year":"2009","journal-title":"Cancer Res."},{"key":"ref_174","doi-asserted-by":"crossref","first-page":"58372","DOI":"10.18632\/oncotarget.17702","article-title":"A novel immunotherapy targeting MMP-14 limits hypoxia, immune suppression and metastasis in triple-negative breast cancer models","volume":"8","author":"Ling","year":"2017","journal-title":"Oncotarget"},{"key":"ref_175","doi-asserted-by":"crossref","first-page":"1140","DOI":"10.1002\/bit.26248","article-title":"Identification of highly selective MMP-14 inhibitory Fabs by deep sequencing","volume":"114","author":"Lopez","year":"2017","journal-title":"Biotechnol. Bioeng."},{"key":"ref_176","doi-asserted-by":"crossref","first-page":"104","DOI":"10.1016\/j.str.2014.10.012","article-title":"Inhibition mechanism of membrane metalloprotease by an exosite-swiveling conformational antibody","volume":"23","author":"Udi","year":"2015","journal-title":"Structure"},{"key":"ref_177","doi-asserted-by":"crossref","unstructured":"Vieira, D., Barralet, J., Harvey, E.J., and Merle, G. (2022). Detecting the PEX Like Domain of Matrix Metalloproteinase-14 (MMP-14) with Therapeutic Conjugated CNTs. Biosensors, 12.","DOI":"10.3390\/bios12100884"},{"key":"ref_178","doi-asserted-by":"crossref","first-page":"114990","DOI":"10.1016\/j.biopha.2023.114990","article-title":"Naringenin: A flavanone with anti-inflammatory and anti-infective properties","volume":"164","author":"Cai","year":"2023","journal-title":"Biomed. Pharmacother."},{"key":"ref_179","doi-asserted-by":"crossref","first-page":"5764","DOI":"10.1167\/iovs.16-19702","article-title":"Naringenin Eye Drops Inhibit Corneal Neovascularization by Anti-Inflammatory and Antioxidant Mechanisms","volume":"58","author":"Oguido","year":"2017","journal-title":"Investig. Ophthalmol. Vis. Sci."},{"key":"ref_180","doi-asserted-by":"crossref","first-page":"71","DOI":"10.24976\/Discov.Med.202436180.6","article-title":"Curcumin Inhibits Bladder Cancer by Inhibiting Invasion via AKT\/MMP14 Pathway","volume":"36","author":"Wang","year":"2024","journal-title":"Discov. Med."},{"key":"ref_181","doi-asserted-by":"crossref","first-page":"1220","DOI":"10.1183\/09031936.02.00022302","article-title":"Matrix metalloproteinases and tissue inhibitor of metalloproteinase-1 in sarcoidosis and IPF","volume":"20","author":"Henry","year":"2002","journal-title":"Eur. Respir. J."},{"key":"ref_182","first-page":"100090","article-title":"The role of inflammatory mediators and matrix metalloproteinases (MMPs) in the progression of osteoarthritis","volume":"13","author":"Mukherjee","year":"2024","journal-title":"Biomater. Biosyst."},{"key":"ref_183","doi-asserted-by":"crossref","first-page":"189","DOI":"10.1006\/jsre.1998.5495","article-title":"MMP-8 is the predominant collagenase in healing wounds and nonhealing ulcers","volume":"81","author":"Nwomeh","year":"1999","journal-title":"J. Surg. Res."},{"key":"ref_184","doi-asserted-by":"crossref","first-page":"2580","DOI":"10.1096\/fj.06-7860com","article-title":"Increased inflammation delays wound healing in mice deficient in collagenase-2 (MMP-8)","volume":"21","author":"Inada","year":"2007","journal-title":"FASEB J."},{"key":"ref_185","doi-asserted-by":"crossref","first-page":"235","DOI":"10.1161\/01.STR.0000196986.50059.e0","article-title":"Matrix metalloproteinase 2 is associated with stable and matrix metalloproteinases 8 and 9 with vulnerable carotid atherosclerotic lesions: A study in human endarterectomy specimen pointing to a role for different extracellular matrix metalloproteinase inducer glycosylation forms","volume":"37","author":"Sluijter","year":"2006","journal-title":"Stroke"},{"key":"ref_186","doi-asserted-by":"crossref","first-page":"L961","DOI":"10.1152\/ajplung.00455.2017","article-title":"Delayed resolution of bleomycin-induced pulmonary fibrosis in absence of MMP13 (collagenase 3)","volume":"316","author":"Cabrera","year":"2019","journal-title":"Am. J. Physiol. Lung Cell Mol. Physiol."},{"key":"ref_187","doi-asserted-by":"crossref","first-page":"2603","DOI":"10.31557\/APJCP.2021.22.8.2603","article-title":"Tumor-Derived Matrix Metalloproteinase-13 (MMP-13) Expression in Benign and Malignant Breast Lesions","volume":"22","author":"Ameli","year":"2021","journal-title":"Asian Pac. J. Cancer Prev."},{"key":"ref_188","doi-asserted-by":"crossref","first-page":"494","DOI":"10.1006\/bbrc.1996.1688","article-title":"Identification of MMP-18, a putative novel human matrix metalloproteinase","volume":"228","author":"Cossins","year":"1996","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_189","doi-asserted-by":"crossref","first-page":"267","DOI":"10.1016\/bs.pmbts.2017.02.003","article-title":"Matrix Metalloproteinases in Remodeling of Lower Extremity Veins and Chronic Venous Disease","volume":"147","author":"Chen","year":"2017","journal-title":"Prog. Mol. Biol. Transl. Sci."},{"key":"ref_190","doi-asserted-by":"crossref","first-page":"135","DOI":"10.1515\/bmc.2011.017","article-title":"Epigenetic regulation of matrix metalloproteinases and their collagen substrates in cancer","volume":"2","author":"Chernov","year":"2011","journal-title":"Biomol. Concepts"},{"key":"ref_191","doi-asserted-by":"crossref","first-page":"102","DOI":"10.1016\/j.matbio.2017.11.007","article-title":"The gelatinases, MMP-2 and MMP-9, as fine tuners of neuroinflammatory processes","volume":"75\u201376","author":"Hannocks","year":"2019","journal-title":"Matrix Biol."},{"key":"ref_192","doi-asserted-by":"crossref","first-page":"812","DOI":"10.1016\/S0008-6363(03)00516-9","article-title":"Matrix metalloproteinases: A review of their structure and role in acute coronary syndrome","volume":"59","author":"Jones","year":"2003","journal-title":"Cardiovasc. Res."},{"key":"ref_193","first-page":"4257","article-title":"Tissue distribution of major matrix metalloproteinases and their transcripts in human breast carcinomas","volume":"19","author":"Lebeau","year":"1999","journal-title":"Anticancer. Res."},{"key":"ref_194","doi-asserted-by":"crossref","first-page":"4281","DOI":"10.1074\/jbc.272.7.4281","article-title":"Identification and characterization of a novel human matrix metalloproteinase with unique structural characteristics, chromosomal location, and tissue distribution","volume":"272","author":"Pendas","year":"1997","journal-title":"J. Biol. Chem."},{"key":"ref_195","first-page":"e257","article-title":"Matrix metalloproteinase-10 expression is induced during hepatic injury and plays a fundamental role in liver tissue repair","volume":"34","author":"Carotti","year":"2014","journal-title":"Liver Int."},{"key":"ref_196","doi-asserted-by":"crossref","first-page":"26806","DOI":"10.18632\/oncotarget.8645","article-title":"Matrix metalloproteinase-10 regulates stemness of ovarian cancer stem-like cells by activation of canonical Wnt signaling and can be a target of chemotherapy-resistant ovarian cancer","volume":"7","author":"Mariya","year":"2016","journal-title":"Oncotarget"},{"key":"ref_197","doi-asserted-by":"crossref","first-page":"259","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. Card. Fail."},{"key":"ref_198","doi-asserted-by":"crossref","first-page":"283","DOI":"10.1002\/ijc.34289","article-title":"Germline gain-of-function MMP11 variant results in an aggressive form of colorectal cancer","volume":"152","author":"Manzano","year":"2023","journal-title":"Int. J. Cancer"},{"key":"ref_199","doi-asserted-by":"crossref","first-page":"376","DOI":"10.1038\/s41374-021-00699-y","article-title":"Matrix metalloproteinase 11 (MMP11) in macrophages promotes the migration of HER2-positive breast cancer cells and monocyte recruitment through CCL2-CCR2 signaling","volume":"102","author":"Kang","year":"2022","journal-title":"Lab. Invest."},{"key":"ref_200","doi-asserted-by":"crossref","first-page":"332","DOI":"10.1038\/pr.2012.185","article-title":"Integrins alpha4 and alphaM, collagen1A1, and matrix metalloproteinase 7 are upregulated in acute Kawasaki disease vasculopathy","volume":"73","author":"Reindel","year":"2013","journal-title":"Pediatr. Res."},{"key":"ref_201","doi-asserted-by":"crossref","first-page":"10613","DOI":"10.1002\/jcb.28351","article-title":"The prognostic value of matrix metalloproteinase-7 and matrix metalloproteinase-15 in acute myeloid leukemia","volume":"120","author":"Wu","year":"2019","journal-title":"J. Cell Biochem."},{"key":"ref_202","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1159\/000092774","article-title":"Matrix metalloproteinases 21 and 26 are differentially expressed in esophageal squamous cell cancer","volume":"27","author":"Ahokas","year":"2006","journal-title":"Tumour Biol."},{"key":"ref_203","doi-asserted-by":"crossref","first-page":"3","DOI":"10.3109\/13506129.2010.541960","article-title":"Matrix metalloproteinase-beta19 expressed in cerebral amyloid angiopathy","volume":"18","author":"Tanskanen","year":"2011","journal-title":"Amyloid"},{"key":"ref_204","first-page":"260","article-title":"Matrix metalloproteinases 15 and 19 are stromal regulators of colorectal cancer development from the early stages","volume":"41","author":"Sena","year":"2012","journal-title":"Int. J. Oncol."},{"key":"ref_205","first-page":"15","article-title":"Expression of MMP-15 and MMP-24 in atherosclerotic and nonatherosclerotic coronary arteries","volume":"1","author":"Horozoglu","year":"2014","journal-title":"Met. Med."},{"key":"ref_206","doi-asserted-by":"crossref","first-page":"46531","DOI":"10.1038\/srep46531","article-title":"High expression of matrix metalloproteinases 16 is associated with the aggressive malignant behavior and poor survival outcome in colorectal carcinoma","volume":"7","author":"Wu","year":"2017","journal-title":"Sci. Rep."},{"key":"ref_207","doi-asserted-by":"crossref","first-page":"3096","DOI":"10.3892\/ol.2017.6536","article-title":"Membranous type matrix metalloproteinase 16 induces human prostate cancer metastasis","volume":"14","author":"Jiang","year":"2017","journal-title":"Oncol. Lett."},{"key":"ref_208","first-page":"e13","article-title":"Deficiency of MMP17\/MT4-MMP proteolytic activity predisposes to aortic aneurysm in mice","volume":"117","author":"Guo","year":"2015","journal-title":"Circ. Res."},{"key":"ref_209","doi-asserted-by":"crossref","first-page":"e30279","DOI":"10.1097\/MD.0000000000030279","article-title":"Increased expression of MMP17 predicts poor clinical outcomes in epithelial ovarian cancer patients","volume":"101","author":"Xiao","year":"2022","journal-title":"Medicine"},{"key":"ref_210","doi-asserted-by":"crossref","first-page":"35023","DOI":"10.1074\/jbc.M806553200","article-title":"Identification and role of the homodimerization interface of the glycosylphosphatidylinositol-anchored membrane type 6 matrix metalloproteinase (MMP25)","volume":"283","author":"Zhao","year":"2008","journal-title":"J. Biol. Chem."},{"key":"ref_211","doi-asserted-by":"crossref","first-page":"29492","DOI":"10.1038\/srep29492","article-title":"Murine matrix metalloproteinase-20 overexpression stimulates cell invasion into the enamel layer via enhanced Wnt signaling","volume":"6","author":"Shin","year":"2016","journal-title":"Sci. Rep."},{"key":"ref_212","doi-asserted-by":"crossref","unstructured":"Mok, P.L., Anandasayanam, A.N.K., Oscar David, H.M., Tong, J., Farhana, A., Khan, M.S.A., Sivaprakasam, G., Koh, A.E., and Alzahrani, B. (2021). Lung development, repair and cancer: A study on the role of MMP20 gene in adenocarcinoma. PLoS ONE, 16.","DOI":"10.1371\/journal.pone.0250552"},{"key":"ref_213","doi-asserted-by":"crossref","first-page":"1887","DOI":"10.1097\/01.LAB.0000106721.86126.39","article-title":"Matrix metalloproteinase-21 is expressed epithelially during development and in cancer and is up-regulated by transforming growth factor-beta1 in keratinocytes","volume":"83","author":"Ahokas","year":"2003","journal-title":"Lab. Invest."},{"key":"ref_214","doi-asserted-by":"crossref","first-page":"503","DOI":"10.1042\/bj20030174","article-title":"The structure and regulation of the human and mouse matrix metalloproteinase-21 gene and protein","volume":"372","author":"Marchenko","year":"2003","journal-title":"Biochem. J."},{"key":"ref_215","unstructured":"Barrett, A.J., Rawlings, N.D., and Woessner, J.F. (2004). Chicken matrix metalloproteinase 22. Handbook of Proteolytic Enzymes (Second Edition), Elsevier."},{"key":"ref_216","doi-asserted-by":"crossref","first-page":"4570","DOI":"10.1074\/jbc.274.8.4570","article-title":"Cloning and characterization of human MMP-23, a new matrix metalloproteinase predominantly expressed in reproductive tissues and lacking conserved domains in other family members","volume":"274","author":"Velasco","year":"1999","journal-title":"J. Biol. Chem."},{"key":"ref_217","doi-asserted-by":"crossref","first-page":"767","DOI":"10.1093\/molehr\/gau034","article-title":"Matrix metalloproteinase-27 is expressed in CD163+\/CD206+ M2 macrophages in the cycling human endometrium and in superficial endometriotic lesions","volume":"20","author":"Cominelli","year":"2014","journal-title":"Mol. Hum. Reprod."},{"key":"ref_218","doi-asserted-by":"crossref","first-page":"77","DOI":"10.1165\/rcmb.2017-0223OC","article-title":"Upregulation and Nuclear Location of MMP28 in Alveolar Epithelium of Idiopathic Pulmonary Fibrosis","volume":"59","author":"Maldonado","year":"2018","journal-title":"Am. J. Respir. Cell Mol. Biol."},{"key":"ref_219","doi-asserted-by":"crossref","first-page":"812","DOI":"10.7150\/ijbs.31335","article-title":"Upregulated MMP28 in Hepatocellular Carcinoma Promotes Metastasis via Notch3 Signaling and Predicts Unfavorable Prognosis","volume":"15","author":"Zhou","year":"2019","journal-title":"Int. J. Biol. Sci."},{"key":"ref_220","doi-asserted-by":"crossref","first-page":"263","DOI":"10.1016\/j.matbio.2009.04.006","article-title":"Expression and function of matrix metalloproteinase (MMP)-28","volume":"28","author":"Rodgers","year":"2009","journal-title":"Matrix Biol."}],"container-title":["International Journal of Molecular Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1422-0067\/27\/4\/2027\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,2,25]],"date-time":"2026-02-25T08:53:40Z","timestamp":1772009620000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1422-0067\/27\/4\/2027"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,2,20]]},"references-count":220,"journal-issue":{"issue":"4","published-online":{"date-parts":[[2026,2]]}},"alternative-id":["ijms27042027"],"URL":"https:\/\/doi.org\/10.3390\/ijms27042027","relation":{},"ISSN":["1422-0067"],"issn-type":[{"value":"1422-0067","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,2,20]]}}}