Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.4.24.17 (MMP-3)
 3,419 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A one-step sandwich enzyme immunoassay (EIA) for matrix metalloproteinase 3 (MMP-3; stromelysin-1) was developed. The assay system used two simultaneous immunoreactions using a solid phase monoclonal antibody and a horseradish peroxidase-labeled monoclonal antibody (Fab'). The sensitivity of the assay system was 20 micrograms/l and linearity was obtained between 31 and 500 micrograms/l. The EIA system was capable of measuring both precursor and active forms of MMP-3 as well as the forms of MMP-3 complexed with tissue inhibitors of metalloproteinases. MMP-3 levels as measured by this assay are significantly higher in the sera of patients with rheumatoid arthritis as compared to those of healthy subjects and patients with osteoarthritis. Immunoblot analyses showed that in the sera and synovial fluids of patients with rheumatoid arthritis, MMP-3 is present in the 59- and 57-kDa precursor forms.
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PMID:A one-step sandwich enzyme immunoassay for human matrix metalloproteinase 3 (stromelysin-1) using monoclonal antibodies. 128 63

Eight adult periodontitis (AP) patients were studied immunohistochemically to determine the presence of matrix metalloproteinases (MMPs) MMP-1, MMP-3, and MMP-8 in the marginal gingival and gingival granulation tissue specimens obtained from periodontal flap surgery after scaling and root planing. Clinically healthy gingival tissue specimens obtained from impacted third-molar extraction operations served as controls. MMP-type-specific antisera were applied by the avidin-biotin-peroxidase complex staining method. Moderate immunoreactivity for neutrophil collagenase (MMP-8) was found both in the AP patients' marginal gingival connective tissue and in gingival granulation tissue specimens. Immunoreactivity for fibroblast-type collagenase (MMP-1) and stromelysin-1 (MMP-3) was detected only in the AP patients' gingival granulation tissue specimens. In the control specimens, no immunoreactivity for the MMPs could be detected. For the first time, this finding demonstrates immunohistochemically the presence of MMP-8 in human inflamed gingiva in situ, and further highlights the importance of MMP-8 in periodontal tissue destruction, evidently during the acute phase(s) of the disease. However, our results confirm and extend previous studies indicating that other types of MMPs from resident gingival cell sources also seem to participate in the chronic and destructive course of periodontal inflammation.
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PMID:Immunohistochemical study of neutrophil- and fibroblast-type collagenases and stromelysin-1 in adult periodontitis. 787 57

We have explored the tissue localization of extracellular matrix metalloproteinases MMP-1 (fibroblast collagenase), MMP-2 (72-kDa gelatinase/Type IV collagenase), MMP-3 (stromelysin), MMP-8 (polymorphonuclear leukocyte collagenase) and MMP-9 (92-kDa gelatinase/Type IV collagenase) in the tissues around loose hip prostheses. The findings were compared with those in synovial tissues obtained from patients with a fractured femoral neck. MMP-type specific antisera were applied in the sensitive avidin-biotin-peroxidase complex methods. MMP-1 was found in monocyte/macrophages, fibroblasts, and vascular endothelial cells in both interface tissues between bone and acetabular components and the pseudocapsular tissues obtained from loosening of hip prostheses. In these tissues, MMP-8 was occasionally found, but only in polymorphonuclear leukocytes. Cells showing immunoreactivity to 72- and 92-kDa gelatinase/Type IV collagenase, MMP-2 and MMP-9, respectively, and stromelysin, MMP-3, were abundant in both interface and pseudocapsular tissues in loose hip prostheses. In contrast, in hip fractures, immunoreactivity to MMP-1, 2, 3, and 9 was weak and only observed in synovial tissues. Immunoreactivity to MMP-8 was confined to polymorphonuclear leukocytes attached to the synovial membrane or in the infiltrate around blood vessels in the subsynovial connective tissues. The finding of MMP-1, 2, 3, and 9 in the tissues around loose hip prostheses suggests that they play a role in the weakening of connective tissues, and this leads to loosening.
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PMID:Extracellular matrix metalloproteinases around loose total hip prostheses. 804 79

Interstitial collagenase (EC 3.4.24.7, matrix metalloproteinase-1, MMP-1) is synthesized and secreted by many cells, and plays an important role in a wide variety of pathophysiological degradation processes of extracellular matrices. The activity of MMP-1 is regulated by tissue inhibitors of metalloproteinases, TIMP-1 or TIMP-2, which form a non-covalent complex with the active enzyme. We raised monoclonal antibodies against zymogen of MMP-1, proMMP-1 purified from human skin fibroblasts. The antibodies recognized both precursor and active forms of MMP-1, but did not cross-react with 72-kDa and 92-kDa gelatinase/type IV collagenases or stromelysin-1. A specific and sensitive one-step sandwich enzyme immunoassay for human MMP-1 was developed using a solid phase monoclonal antibody and a horseradish peroxidase-labeled monoclonal antibody (Fab'). The assay can be completed within 1 h (30 min for immunoreaction and 15 min for color development) and the sensitivity is 0.12 microgram/l with the linearity between 0.12 and 10 micrograms/l. Active MMP-1 shows 1.3-fold higher absorption at 492 nm than proMMP-1. However, the recognition rate of MMP-1 is decreased to approximately 50% and < 3% for the MMP-1-TIMP-1 and MMP-1-TIMP-2 complex forms, respectively. The MMP-1 levels in human sera from 120 healthy subjects are shown to be in the range of 8.5 +/- 5.2 micrograms/l (mean +/- S.D.) and the levels of 95% of the samples range from 0 to 20 micrograms/l.
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PMID:A one-step sandwich enzyme immunoassay for human matrix metalloproteinase 1 (interstitial collagenase) using monoclonal antibodies. 830 49

Six patients with recurrent aphthous ulcers were studied for the presence of matrix metalloproteinases (MMP) 1, 3, and 8 in the lesions and in the clinically unaffected control mucosa obtained from the opposite side. MMP-type specific antisera were applied in the avidin-biotin-peroxidase complex staining method. Neutrophil-type collagenase (MMP-8) was found intracellularly in the connective tissue under the necrotized epithelium, and also laterally to the ulcer in association with the basement membrane. Fibroblast-type collagenase (MMP-1) and stromelysin (MMP-3) were found in the epithelial cells adjacent to the ulcerous lesion. They were found also in the endothelium of capillary blood vessels and postcapillary venules and also in some macrophage- and fibroblast-like mononuclear cells in the lamina propria laterally to the ulcer. A small number of MMP-1 and MMP-3 positive cells were noted in the control biopsies obtained from the clinically uninvolved control mucosa. These findings suggest regional differences in the distribution of the two main collagenases, implying distinct roles in tissue destruction and remodeling.
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PMID:Collagenase and stromelysin in recurrent aphthous ulcers (RAU). 845 24

Fibroblast-type interstitial collagenase (E.C. 3.4.24.7) was associated with loosening of total hip prostheses in eight patients: there were four cemented stems and one cementless stem with the common type of loosening and two cemented stems and one cementless acetabular component with aggressive granulomatous lesions. The authors used a specific, well-characterized, heterologous, affinity-purified, polyclonal rabbit anti-human fibroblast collagenase antiserum applied in avidin-biotin-peroxidase-complex (ABC) staining. In the aggressive granulomatous type of loosening, collagenase was found in most of the fibroblast- and macrophagelike cells, including multinuclear giant cells and epithelioid cells in periprosthetic tissue. Collagenase-positive cells also were found in the periprosthetic tissue associated with common loosening. Collagenase was also found in capillary and postcapillary venule endothelial cells in the richly vascularized aggressive granulomatous tissue. Collagenase was extracted directly from the tissue samples and incubated with soluble Type I collagen. Collagen degradation products then were analyzed by sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis, and the three-fourths length degradation product quantitated by gel scanning densitometry. In both aggressive granulomatosis and the common type of loosening, extractable collagenase was found in tissue. No significant differences between the sample groups were detected in respect to total measurable collagenase, however. The extractable collagenase was present in a latent form that could be activated by the organomercurial procollagenase activator, phenylmercuric chloride (PMC). It is likely that interstitial collagenase contributes to rapid growth of reactive infiltrative tissue, loosening of the prosthesis associated with aggressive granulomatosis, and the periprosthetic lytic process associated with the common type of hip prosthesis loosening.
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PMID:Role of mesenchymal collagenase in the loosening of total hip prosthesis. 847 51

The pathogenesis of the tissue damage and fibrosis in sarcoidosis is poorly understood. The matrix metalloproteinases (MMPs) and their tissue inhibitors (TIMPs) must be considered in this regard, because they control the lysis of connective tissue components. Immunohistochemical studies (peroxidase and dual labeling for confocal microscopy) of reactivity for MMP-1, MMP-2, MMP-3, MMP-7, MMP-9, and the 4 membrane-type-MMPs were made on tissues from patients with cardiac (n = 4) and pulmonary (n = 5) sarcoidosis. The granulomas were histochemically similar in both organs. The multinucleated giant cells (MGCs) showed moderate reactivity for MMP-1 and MMP-9 and variable reactivity for MMP-2 and MMP-3; in addition, they showed colocalization of MT-1-MMP, which activates MMP-2. The reactivity of epithelioid cells (ECs) was moderate for MMP-2 and mild for other MMPs. Macrophages showed weaker reactivity for MMPs than did MGCs and ECs. All 3 types of cells showed very low reactivity for TIMPs. Staining for type IV collagen showed focal damage to the basement membranes of cardiac myocytes and pulmonary alveoli near the granulomas. The cells in sarcoid granulomas contain an abundance of MMPs and a paucity of TIMPs. The MGCs also contain MT-1-MMP and thus can activate MMP-2 in the granulomas. The MMPs can cause damage to adjacent cardiac myocytes and pulmonary alveoli, leading to the interstitial fibrosis produced by sarcoidosis.
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PMID:Matrix metalloproteinases and their tissue inhibitors in the lesions of cardiac and pulmonary sarcoidosis: an immunohistochemical study. 1251 81

We investigated the expression of genes in response to exposure of primary human chondrocytes to extracellular catalase. The addition of catalase to culture medium caused a significant up-regulation of cyclooxygenase 2, interleukin 8, and stromelysin mRNA levels. Similar pattern of gene activation occurred in chondrocytes incubated with horseradish peroxidase. On the contrary, ebselen, a glutathione peroxidase mimetic agent, did not affect expression of catalase-inducible genes. Taken together, these observations imply that catalase action is mediated by its side peroxidase-like activity, rather than elimination of H2O2. Genistein suppressed catalase-mediated effects on gene expression. This finding implies that tyrosine kinases are implicated in underlying signaling pathway.
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PMID:Extracellular catalase induces cyclooxygenase 2, interleukin 8, and stromelysin genes in primary human chondrocytes. 1566 46

Matrix metalloproteinases (MMPs) have been implicated in the tumor invasion and growth through the degradation of extracellular matrix. In this study, we selected 46 hepatocellular carcinoma (HCC) cases, at random, and we immunohistologically examined the expression of MMP-1, MMP-2, MMP-3, MMP-7, MMP-9, tissue inhibitor of metalloproteinases (TIMP)-1, TIMP-2, in cancerous and non-cancerous areas using avidin-biotin-peroxidase complex method. In all cases, cancer cells, hepatocytes, sinusoidal lining cells, leukocytes, and bile ducts were positive for all the primary antibodies. The expressions of MMPs and TIMPs in most of the HCC tissues were equal or low compared with those in the surrounding non-tumor tissues, although mixed expression pattern were recognized in some HCC tissues. The difference of MMP and TIMP expression was not related with the histological differentiation of HCC and the condition of non-cancerous area. These findings suggested little association of the clinicopathological findings of HCC with the histological expression of MMPs and TIMPs.
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PMID:Expression of matrix metalloproiteinases (MMPs) and tissue inhibitors of metalloproteinases (TIMPs) in hepatocellular carcinoma tissue, compared with the surrounding non-tumor tissue. 1756 13

Periodontitis is commonly observed in dogs. In human medicine, it is well documented that matrix metalloproteinases (MMPs) are involved in the destruction of the periodontium. Therefore, the aim of this prospective study was to investigate the impact of MMPs and their inhibitors, the TIMPs (tissue inhibitors of metalloproteinases), on canine periodontitis. The oral cavities of 57 dogs were examined clinically and radiologically. Gingival biopsies were obtained from the examined dogs and histologically analysed via haematoxylin and eosin stained sections. Immunohistological detection of MMP-2, MMP-3, MMP-8 and MMP-9 as well as TIMP-1 and TIMP-2 was performed by the avidin-biotin peroxidase complex technique. All sections were evaluated by light microscopy. Statistically significant positive correlations were detected between the histologically verified degree of inflammation and the expression of MMP-2, MMP-3, MMP-8 and MMP-9 as well as between changes in collagen fibre content and the occurrence of MMP-2, MMP-8 and MMP-9. Concerning TIMP-1 and TIMP-2, non-significant, generally negative correlations were observed. In summary, in canine periodontitis, an increased expression of the above mentioned MMPs and a tendentially decreased expression of TIMPs are present. In conclusion, in canine periodontitis, a MMP-TIMP imbalance is suggestive of contributing to the destruction of the periodontium.
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PMID:Immunohistochemical localisation and effect of matrix metalloproteinases and their inhibitors on canine spontaneous periodontitis. 2626 63


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