Metalloproteinases in Inflammatory Bowel Diseases

References

• Seyedian SS, Nokhostin F, Malamir MD. A review of the diagnosis, prevention, and treatment methods of inflammatory bowel disease. J Med Life. 2019;12(2):113–122. doi:10.25122/jml-2018-0075
   PubMedGoogle Scholar
• MacDonald TT, Monteleone G. Immunity, inflammation, and allergy in the gut. Science. 2005;307(5717):1920–1925. doi:10.1126/science.1106442
   PubMed Web of Science ®Google Scholar
• Yang C, Singh P, Singh H, Le M-L, El-Matary W. Systematic review: thalidomide and thalidomide analogues for treatment of inflammatory bowel disease. Aliment Pharmacol Ther. 2015;41(11):1079–1093. doi:10.1111/apt.13181
   PubMed Web of Science ®Google Scholar
• Baldassano RN, Piccoli DA. Inflammatory bowel disease in pediatric and adolescent patients. Gastroenterol Clin North Am. 1999;28(2):445–458. doi:10.1016/S0889-8553(05)70064-9
   PubMed Web of Science ®Google Scholar
• Dalal SR, Cohen RD. What to Do When Biologic Agents Are Not Working in Inflammatory Bowel Disease Patients. Gastroenterol Hepatol. 2015;11(10):657–665.
   PubMedGoogle Scholar
• Biancheri P, Di Sabatino A, Corazza GR, MacDonald TT. Proteases and the gut barrier. Cell Tissue Res. 2013;351(2):269–280. doi:10.1007/s00441-012-1390-z
   PubMed Web of Science ®Google Scholar
• Kucukguven A, Khalil R. Matrix metalloproteinases as potential targets in the venous dilation associated with varicose veins. Curr Drug Targets. 2013;14(3):287–324.
   PubMed Web of Science ®Google Scholar
• Gomis-Rüth FX, Maskos K, Betz M, et al. Mechanism of inhibition of the human matrix metalloproteinase stromelysin-1 by TIMP-1. Nature. 1997;389(6646):77–81. doi:10.1038/37995
   PubMed Web of Science ®Google Scholar
• Nagase H, Visse R, Murphy G. Structure and function of matrix metalloproteinases and TIMPs. Cardiovasc Res. 2006;69(3):562–573. doi:10.1016/j.cardiores.2005.12.002
   PubMed Web of Science ®Google Scholar
• Strongin AY, Collier I, Bannikov G, Marmer BL, Grant GA, Goldberg GI. Mechanism of cell surface activation of 72-kDa type IV collagenase. Isolation of the activated form of the membrane metalloprotease. J Biol Chem. 1995;270(10):5331–5338. doi:10.1074/jbc.270.10.5331
   PubMed Web of Science ®Google Scholar
• Gomez D, Alonso D, Yoshiji H, Thorgeirsson U. Tissue inhibitors of metalloproteinases: structure, regulation and biological functions. Eur J Cell Biol. 1997;74(2):111–122.
   PubMed Web of Science ®Google Scholar
• Murphy G, Willenbrock F. Tissue inhibitors of matrix metalloendopeptidases. Methods Enzymol. 1995;248(C):496–510. doi:10.1016/0076-6879(95)48032-3
   PubMedGoogle Scholar
• Saarialho-Kere U, Vaalamo M, Puolakkainen P, Airola K, Parks WC, Karjalainen-Lindsberg ML. Enhanced expression of matrilysin, collagenase, and stromelysin-1 in gastrointestinal ulcers. Am J Pathol. 1996;148(2):519–526.
   PubMed Web of Science ®Google Scholar
• Vaalamo M, Karjalainen-Lindsberg ML, Puolakkainen P, Kere J, Saarialho-Kere U. Distinct expression profiles of stromelysin-2 (MMP-10), collagenase-3 (MMP-13), macrophage metalloelastase (MMP-12), and tissue inhibitor of metalloproteinases-3 (TIMP-3) in intestinal ulcerations. Am J Pathol. 1998;152(4):1005–1014.
   PubMed Web of Science ®Google Scholar
• Dobre M, Milanesi E, Mănuc TE, et al. Differential intestinal mucosa transcriptomic biomarkers for Crohn’s disease and ulcerative colitis. J Immunol Res. 2018;2018:9208274. doi:10.1155/2018/9208274
   PubMed Web of Science ®Google Scholar
• Altadill A, Eiró N, González LO, et al. Comparative analysis of the expression of metalloproteases and their inhibitors in resected crohn’s disease and complicated diverticular disease. Inflamm Bowel Dis. 2012;18(1):120–130. doi:10.1002/ibd.21682
   PubMed Web of Science ®Google Scholar
• Mäkitalo L, Kolho KL, Karikoski R, Anthoni H, Saarialho-Kere U. Expression profiles of matrix metalloproteinases and their inhibitors in colonic inflammation related to pediatric inflammatory bowel disease. Scand J Gastroenterol. 2010;45(7–8):862–871. doi:10.3109/00365520903583863
   PubMed Web of Science ®Google Scholar
• Mäkitalo L, Piekkala M, Ashorn M, et al. Matrix metalloproteinases in the restorative proctocolectomy pouch of pediatric ulcerative colitis. World J Gastroenterol. 2012;18(30):4028–4036. doi:10.3748/wjg.v18.i30.4028
   PubMed Web of Science ®Google Scholar
• Jimbo K, Ohtsuka Y, Kojima Y, et al. Increased expression of CXCR3 axis components and matrix metalloproteinase in pediatric inflammatory bowel disease patients. Pediatr Int. 2014;56(6):873–883. doi:10.1111/ped.12362
   PubMed Web of Science ®Google Scholar
• Manuc M, Ionescu EM, Milanesi E, et al. Molecular signature of persistent histological inflammation in ulcerative colitis with mucosal healing. J Gastrointest Liver Dis. 2020;29(2):159–166. doi:10.15403/jgld-576
   PubMed Web of Science ®Google Scholar
• Salmela MT, MacDonald TT, Black D, et al. Upregulation of matrix metalloproteinases in a model of T cell mediated tissue injury in the gut: analysis by gene array and in situ hybridisation. Gut. 2002;51(4):540–547. doi:10.1136/gut.51.4.540
   PubMed Web of Science ®Google Scholar
• Pender SLF, Li CKF, Sabatino ADI, Macdonald TT, Buckley MG. Role of macrophage metalloelastase in gut inflammation. In: Annals of the New York Academy of Sciences. Vol. 1072. Blackwell Publishing Inc;2006:386–388. doi:10.1196/annals.1326.019
   Google Scholar
• Schuppan D, Freitag T. Fistulising Crohn’s disease: MMPs gone awry. Gut. 2004;53(5):622–624. doi:10.1136/gut.2003.034207
   PubMed Web of Science ®Google Scholar
• Kirkegaard T, Hansen A, Bruun E, Brynskov J. Expression and localisation of matrix metalloproteinases and their natural inhibitors in fistulae of patients with Crohn’s disease. Gut. 2004;53(5):701–709. doi:10.1136/gut.2003.017442
   PubMed Web of Science ®Google Scholar
• Baugh MD, Perry MJ, Hollander AP, et al. Matrix metalloproteinase levels are elevated in inflammatory bowel disease. Gastroenterology. 1999;117(4):814–822. doi:10.1016/S0016-5085(99)70339-2
   PubMed Web of Science ®Google Scholar
• Matsuno K, Adachi Y, Yamamoto H, et al. The expression of matrix metalloproteinase matrilysin indicates the degree of inflammation in ulcerative colitis. J Gastroenterol. 2003;38(4):348–354. doi:10.1007/s005350300062
   PubMed Web of Science ®Google Scholar
• Rath T, Roderfeld M, Halwe JM, Tschuschner A, Roeb E, Graf J. Cellular sources of MMP-7, MMP-13 and MMP-28 in ulcerative colitis. Scand J Gastroenterol. 2010;45(10):1186–1196. doi:10.3109/00365521.2010.499961
   PubMed Web of Science ®Google Scholar
• Dunsmore SE, Saarialho-Kere UK, Roby JD, et al. Matrilysin expression and function in airway epithelium. J Clin Invest. 1998;102(7):1321–1331. doi:10.1172/JCI1516
   PubMed Web of Science ®Google Scholar
• Lin X, Li J, Zhao Q, Feng J-R, Gao Q, Nie J-Y. WGCNA Reveals Key Roles of IL8 and MMP-9 in Progression of Involvement Area in Colon of Patients with Ulcerative Colitis. Curr Med Sci. 2018;38(2):252–258. doi:10.1007/s11596-018-1873-6
   PubMed Web of Science ®Google Scholar
• Wiercinska-Drapalo A, Jaroszewicz J, Flisiak R, Prokopowicz D. Plasma matrix metalloproteinase-1 and tissue inhibitor of metalloproteinase-1 as biomarkers of ulcerative colitis activity. World J Gastroenterol. 2003;9(12):2843–2845. doi:10.3748/wjg.v9.i12.2843
   PubMed Web of Science ®Google Scholar
• De WY, Tan XY, Zhang K. Correlation of plasma MMP-1 and TIMP-1 levels and the colonic mucosa expressions in patients with ulcerative colitis. Mediators Inflamm. 2009;2009:275072. doi:10.1155/2009/275072
   PubMed Web of Science ®Google Scholar
• Arihiro S, Ohtani H, Hiwatashi N, Torii A, Sorsa T, Nagura H. Vascular smooth muscle cells and pericytes express MMP-1, MMP-9, TIMP-1 and type I procollagen in inflammatory bowel disease. Histopathology. 2001;39(1):50–59. doi:10.1046/j.1365-2559.2001.01142.x
   PubMed Web of Science ®Google Scholar
• Louis E, Ribbens C, Godon A, et al. Increased production of matrix metalloproteinase-3 and tissue inhibitor of metalloproteinase-1 by inflamed mucosa in inflammatory bowel disease. Clin Exp Immunol. 2000;120(2):241–246. doi:10.1046/j.1365-2249.2000.01227.x
   PubMed Web of Science ®Google Scholar
• Meijer MJW, Mieremet-Ooms MAC, van der Zon AM, et al. Increased mucosal matrix metalloproteinase-1, −2, −3 and −9 activity in patients with inflammatory bowel disease and the relation with Crohn’s disease phenotype. Dig Liver Dis. 2007;39(8):733–739. doi:10.1016/j.dld.2007.05.010
   PubMedGoogle Scholar
• Von Lampe B, Barthel B, Coupland SE, Riecken EO, Rosewicz S. Differential expression of matrix metalloproteinases and their tissue inhibitors in colon mucosa of patients with inflammatory bowel disease. Gut. 2000;47(1):63–73. doi:10.1136/gut.47.1.63
   PubMed Web of Science ®Google Scholar
• Heuschkel RB, MacDonald TT, Monteleone G, Bajaj-Elliott M, Smith JAW, Pender SLF. Imbalance of stromelysin-1 and TIMP-1 in the mucosal lesions of children with inflammatory bowel disease. Gut. 2000;47(1):57–62. doi:10.1136/gut.47.1.57
   PubMed Web of Science ®Google Scholar
• Gordon JN, Pickard KM, Disabatino A, et al. Matrix metalloproteinase-3 production by gut IgG plasma cells in chronic inflammatory bowel disease. Inflamm Bowel Dis. 2008;14(2):195–203. doi:10.1002/ibd.20302
   PubMed Web of Science ®Google Scholar
• Pender S, Tickle S, Docherty A, Howie D, Wathen N, MacDonald T. A major role for matrix metalloproteinases in T cell injury in the gut. J Immunol. 1997;158(4):1582–1590.
   PubMed Web of Science ®Google Scholar
• Pender SLF, Braegger C, Günther U, et al. Matrix metalloproteinases in necrotising enterocolitis. Pediatr Res. 2003;54(2):160–164. doi:10.1203/01.PDR.0000072326.23442.C3
   PubMed Web of Science ®Google Scholar
• Lakatos G, Hritz I, Varga MZ, et al. The impact of matrix metalloproteinases and their tissue inhibitors in inflammatory bowel diseases. Dig Dis. 2012;30(3):289–295. doi:10.1159/000336995
   PubMed Web of Science ®Google Scholar
• Salmela MT, Karjalainen-Lindsberg ML, Jeskanen L, Saarialho-Kere U. Overexpression of tissue inhibitor of metalloproteinases-3 in intestinal and cutaneous lesions of graft-versus-host disease. Mod Pathol. 2003;16(2):108–114. doi:10.1097/01.MP.0000051681.43441.82
   PubMed Web of Science ®Google Scholar
• Pender SLF, Fell J, Chamow S, Ashkenazi A, MacDonald T. A p55 TNF receptor immunoadhesin prevents T cell-mediated intestinal injury by inhibiting matrix metalloproteinase production. J Immunol. 1998;160(8):4098–4103.
   PubMed Web of Science ®Google Scholar
• Monteleone G, Biancone L, Marasco R, et al. Interleukin 12 is expressed and actively released by Crohn’s disease intestinal lamina propria mononuclear cells. Gastroenterology. 1997;112(4):1169–1178. doi:10.1016/S0016-5085(97)70128-8
   PubMed Web of Science ®Google Scholar
• Parrello T, Monteleone G, Cucchiara S, et al. Up-Regulation of the IL-12 Receptor β2 Chain in Crohn’s Disease. J Immunol. 2000;165(12):7234–7239. doi:10.4049/jimmunol.165.12.7234
   PubMed Web of Science ®Google Scholar
• Monteleone G, Parrello T, Luzza F, Pallone F. Response of human intestinal lamina propria T lymphocytes to interleukin 12: additive effects of interleukin 15 and 7. Gut. 1998;43(5):620–628. doi:10.1136/gut.43.5.620
   PubMed Web of Science ®Google Scholar
• Pallone F, Monteleone G. Interleukin 12 and Th1 responses in inflammatory bowel disease. Gut. 1998;43(6):735–736. doi:10.1136/gut.43.6.735
   PubMed Web of Science ®Google Scholar
• Monteleone G, MacDonald TT, Wathen NC, Pallone F, Pender SLF. Enhancing lamina propria Th1 cell responses with interleukin 12 produces severe tissue injury. Gastroenterology. 1999;117(5):1069–1077. doi:10.1016/S0016-5085(99)70391-4
   PubMed Web of Science ®Google Scholar
• Monteleone G, Monteleone I, Fina D, et al. Interleukin-21 enhances T-helper cell type I signaling and interferon-γ production in Crohn’s disease. Gastroenterology. 2005;128(3):687–694. doi:10.1053/j.gastro.2004.12.042
   PubMed Web of Science ®Google Scholar
• Sarra M, Pallone F, MacDonald TT, Monteleone G. IL-23/IL-17 axis in IBD. Inflamm Bowel Dis. 2010;16(10):1808–1813. doi:10.1002/ibd.21248
   PubMed Web of Science ®Google Scholar
• Sarra M, Monteleone I, Stolfi C, et al. Interferon-gamma-expressing cells are a major source of interleukin-21 in inflammatory bowel diseases. Inflamm Bowel Dis. 2010;16(8):1332–1339. doi:10.1002/ibd.21238
   PubMed Web of Science ®Google Scholar
• Monteleone G, Pallone F, MacDonald TT. Interleukin-21: a critical regulator of the balance between effector and regulatory T-cell responses. Trends Immunol. 2008;29(6):290–294. doi:10.1016/j.it.2008.02.008
   PubMed Web of Science ®Google Scholar
• Monteleone G, Caruso R, Fina D, et al. Control of matrix metalloproteinase production in human intestinal fibroblasts by interleukin 21. Gut. 2006;55(12):1774–1780. doi:10.1136/gut.2006.093187
   PubMed Web of Science ®Google Scholar
• Bamba S, Andoh A, Yasui H, Araki Y, Bamba T, Fujiyama Y. Matrix metalloproteinase-3 secretion from human colonic subepithelial myofibroblasts: role of interleukin-17. J Gastroenterol. 2003;38(6):548–554. doi:10.1007/s00535-002-1101-8
   PubMed Web of Science ®Google Scholar
• Sandborn WJ, Targan SR. Biologic therapy of inflammatory bowel disease. Gastroenterology. 2002;122(6):1592–1608. doi:10.1053/gast.2002.33426
   PubMed Web of Science ®Google Scholar
• Sandborn WJ, Hanauer SB, Katz S, et al. Etanercept for active Crohn’s disease: a randomized, double-blind, placebo-controlled trial. Gastroenterology. 2001;121(5):1088–1094. doi:10.1053/gast.2001.28674
   PubMed Web of Science ®Google Scholar
• Biancheri P, Brezski RJ, Di Sabatino A, et al. Proteolytic cleavage and loss of function of biologic agents that neutralize tumor necrosis factor in the mucosa of patients with inflammatory bowel disease. Gastroenterology. 2015;149(6):1564–1574.e3. doi:10.1053/j.gastro.2015.07.002
   Web of Science ®Google Scholar
• Sykes AP, Bhogal R, Brampton C, et al. The effect of an inhibitor of matrix metalloproteinases on colonic inflammation in a trinitrobenzenesulphonic acid rat model of inflammatory bowel disease. Aliment Pharmacol Ther. 1999;13(11):1535–1542. doi:10.1046/j.1365-2036.1999.00633.x
   PubMed Web of Science ®Google Scholar
• Di Sebastiano P, Di Mola FF, Artese L, et al. Beneficial effects of Batimastat (BB-94), a matrix metalloproteinase inhibitor, in rat experimental colitis. Digestion. 2001;63(4):234–239. doi:10.1159/000051895
   PubMed Web of Science ®Google Scholar
• O’Sullivan S, Wang J, Radomski MW, Gilmer JF, Medina C. Novel barbiturate-nitrate compounds inhibit the upregulation of matrix metalloproteinase-9 gene expression in intestinal inflammation through a CGMP-mediated pathway. Biomolecules. 2020;10(5):808. doi:10.3390/biom10050808
   PubMed Web of Science ®Google Scholar
• Sandborn WJ, Bhandari BR, Fogel R, et al. Randomised clinical trial: a phase 1, dose-ranging study of the anti-matrix metalloproteinase-9 monoclonal antibody GS-5745 versus placebo for ulcerative colitis. Aliment Pharmacol Ther. 2016;44(2):157–169. doi:10.1111/apt.13653
   PubMed Web of Science ®Google Scholar
• Sandborn WJ, Bhandari BR, Randall C, et al. Andecaliximab [Anti-matrix Metalloproteinase-9] induction therapy for ulcerative colitis: a randomised, double-blind, placebo-controlled, phase 2/3 study in patients with moderate to severe disease. J Crohn Colitis. 2018;12(9):1021–1029. doi:10.1093/ecco-jcc/jjy049
   PubMed Web of Science ®Google Scholar
• Schreiber S, Siegel CA, Friedenberg KA, et al. A phase 2, randomized, placebo-controlled study evaluating matrix metalloproteinase-9 inhibitor, andecaliximab, in patients with moderately to severely active Crohn’s disease. J Crohn Colitis. 2018;12(9):1014–1020. doi:10.1093/ecco-jcc/jjy070
   PubMed Web of Science ®Google Scholar
• Appleby TC, Greenstein AE, Hung M, et al. Biochemical characterization and structure determination of a potent, selective antibody inhibitor of human MMP9. J Biol Chem. 2017;292(16):6810–6820. doi:10.1074/jbc.M116.760579
   PubMed Web of Science ®Google Scholar
• De WY, Yan PY. Expression of matrix metalloproteinase-1 and tissue inhibitor of metalloproteinase-1 in ulcerative colitis. World J Gastroenterol. 2006;12(37):6050–6053. doi:10.3748/wjg.v12.i37.6050
   PubMed Web of Science ®Google Scholar
• Newell KJ, Matrisian LM, Driman DK. Matrilysin (matrix metalloproteinase-7) expression in ulcerative colitis-related tumorigenesis. Mol Carcinog. 2002;34(2):59–63. doi:10.1002/mc.10049
   PubMed Web of Science ®Google Scholar
• Rath T, Roderfeld M, Graf J, et al. Enhanced expression of MMP-7 and MMP-13 in inflammatory bowel disease: a precancerous potential? Inflamm Bowel Dis. 2006;12(11):1025–1035. doi:10.1097/01.mib.0000234133.97594.04
   PubMed Web of Science ®Google Scholar
• Baugh MD, Hollander AP, Evans GS. The regulation of matrix metalloproteinase production in human colonic fibroblasts. In: Annals of the New York Academy of Sciences. Vol. 859. New York Academy of Sciences; 1998:175–179. doi:10.1111/j.1749-6632.1998.tb11121.x
   Google Scholar
• Salmela MT, Pender SLF, Karjalainen-Lindsberg ML, Puolakkainen P, MacDonald TT, Saarialho-Kere U. Collagenase-1 (MMP-1), matrilysin-1 (MMP-7), and stromelysin-2 (MMP-10) are expressed by migrating enterocytes during intestinal wound healing. Scand J Gastroenterol. 2004;39(11):1095–1104. doi:10.1080/00365520410003470
   PubMed Web of Science ®Google Scholar
• Vizoso FJ, González LO, Corte MD, et al. Collagenase-3 (MMP-13) expression by inflamed mucosa in inflammatory bowel disease. Scand J Gastroenterol. 2006;41(9):1050–1055. doi:10.1080/00365520600554667
   PubMed Web of Science ®Google Scholar
• Bister VO, Salmela MT, Karjalainen-Lendsberg ML, et al. Differential expression of three matrix metalloproteinases, MMP-19, MMP-26, and MMP-28, in normal and inflamed intestine and colon cancer. Dig Dis Sci. 2004;49(4):653–661. doi:10.1023/B:DDAS.0000026314.12474.17
   PubMed Web of Science ®Google Scholar
• Fonseca-Camarillo G, Furuzawa-Carballeda J, Martínez-Benitez B, Barreto-Zuñiga R, Yamamoto-Furusho JK. Increased expression of extracellular matrix metalloproteinase inducer (EMMPRIN) and MMP10, MMP23 in inflammatory bowel disease: cross-sectional study. Scand J Immunol. 2021;93(1):e12962. doi:10.1111/sji.12962
   PubMed Web of Science ®Google Scholar