Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.4.24.23 (MMP)
4,246 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Programmed expression of matrix metalloproteinases is involved in wound healing in various organs. We have previously demonstrated enhanced expression of collagenase-1, stromelysin-1, matrilysin, and tissue inhibitor of metalloproteinases (TIMP-1) in gastrointestinal ulcerations. To further define the role of matrix-degrading enzymes and their inhibitors in intestinal inflammation and ulcerations, the expression of stromelysin-2 (MMP-10), collagenase-3 (MMP-13), macrophage metalloelastase (HME, MMP-12), and TIMP-3 mRNAs was studied using in situ hybridization and immunohistochemistry in 38 samples representing ulcerative colitis, Crohn's disease, ischemic colitis, and normal intestine. As controls for normally healing intestinal wounds, 12 postoperative samples of rat experimental jejunal anastomoses were also examined. The colitis types studied did not essentially differ in their MMP expression. We found stromelysin-2 mRNA in laminin-5-positive and Ki-67-negative enterocytes bordering the ulcerations. HME was abundantly expressed by macrophages in the vicinity of shedding mucosal epithelium and beneath the necrotic surface of the ulcers. Collagenase-3 and TIMP-3 were expressed by fibroblast-like cells deeper in the remodeling intestinal wall. Expression for stromelysin-2 and collagenase-3 was observed in granulation tissue, but not the epithelium, of the rat anastomoses. Our results suggest a role for stromelysin-2 in epithelial migration and for metalloelastase in macrophage movement and epithelial cell shedding.
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PMID: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. 954 61

Ischemic colitis results from insufficient blood supply but its pathogenesis is poorly understood. The aim of this study was to determine whether the activity and expression of gelatinases (MMP-9 and MMP-2) are increased in the colonic mucosa of patients with ischemic colitis. MMP-9 and MMP-2 activity and expression were assessed in colonic mucosal specimens from 8 patients with acute ischemic colitis and in 12 controls with a normal colonoscopy. The activity and expression of MMP-9 and MMP-2 were quantified in tissue samples by zymography and western blot, respectively. Colonoscopy was repeated 12 weeks after discharge in two patients and MMP activity was assessed in the slight residual mucosal changes of ischemic colitis. In patients with ischemic colitis, a significant increase in total MMP-9 and MMP-2 activity and expression was found in ulcerated areas compared with noninvolved sites of mucosa. Following resolution of ischemic ulcers the proteolytic activity returned to baseline levels. In addition, the colonic mucosa of controls showed MMP-2 activity, whereas the MMP-9 activity was negligible or not detected. We conclude that ischemic colitis induces increased activity and expression of MMP-9 and MMP-2 in the involved colonic mucosa. These changes may contribute to tissue degradation and remodeling of the colonic mucosa in ischemic colitis.
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PMID:Increased activity and expression of gelatinases in ischemic colitis. 1708 88