Neutrophil collagenase (EC 3.4.24.34, matrix metalloproteinase 8, PMNL collagenase, MMP-8) is an enzyme. This enzyme catalyses the following chemical reaction Cleavage of interstitial collagens in the triple helical domain. Unlike EC 3.4.24.7, interstitial collagenase, this enzyme cleaves type III collagen more slowly than type I This enzyme belongs to the peptidase family M10. Collagenase Hasty, K. (1987). "A., Jeffrey, J. J., Hibbs, M. S. and Welgus, H. G. The collagen substrate specificity of human neutrophil collagenase". J. Biol. Chem. 262 (21): 10048-10052. PMID 3038863. Hasty, K. (1990). "A., Pourmotabbed, T. F., Goldberg, G. I., Thompson, J. P., Spinella, D. G., Stevens, R. M. and Mainardi, C. L. Human Neutrophil Collagenase. A distinct gene product with homology to other matrix metalloproteinases". J. Biol. Chem. 265 (20): 11421-11424. PMID 2164002. Knäuper, V.; Krämer, S.; Reinke, H.; Tschesche, H. (1990). "Characterization and activation of procollagenase from human ...
1JAQ: X-ray structures of human neutrophil collagenase complexed with peptide hydroxamate and peptide thiol inhibitors. Implications for substrate binding and rational drug design.
1A85: Structure of malonic acid-based inhibitors bound to human neutrophil collagenase. A new binding mode explains apparently anomalous data.
Full-length recombinant human neutrophil pro-collagenase (MMP-8), latent form. Matrix metalloproteinase 8 (MMP-8), or neutrophil collagenase, degrades interstitial collag
We studied the in vivo effect of long-term doxycycline treatment combined with NSAID on human interstitial collagenases, other matrix metalloproteinases, serine proteinases, tissue inhibitor of matrix metalloproteinase-l (TIMP-1) and lactoferrin from saliva and serum during the course of acute reactive arthritis (ReA). Collagenase activity and serine proteases (elastase-like, cathepsin G-like and trypsin-like activities) of saliva (n = 10) and gelatinase, lactoferrin and TIMP-1 of saliva (E = 10) and serum (n = 10) samples before and after 2 months doxycycline treatment, combined with NSAID, were studied by quantitative SDS-PAGE assay, ELISA assay and by spectrophotometric assay. The cellular source and molecular forms of salivary collagenase were characterized by immunoblotting using specific antisera. We found that activities of total and endogenously active interstitial collagenase reduced significantly. The salivary collagenase was found to originate from neutrophils. No fragmentation of ...
Neutrophil collagenase, also known as matrix metalloproteinase-8 (MMP-8) or PMNL collagenase (MNL-CL), is a collagen cleaving enzyme which is present in the connective tissue of most mammals. In humans, the MMP-8 protein is encoded by the MMP8 gene. Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMPs are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. However, the enzyme encoded by this gene is stored in secondary granules within neutrophils and is activated by autolytic cleavage. Its function is degradation of type I, II and III collagens. The gene is part of a cluster of MMP genes which localize to chromosome 11q22.3. GRCh38: Ensembl release 89: ENSG00000118113 - Ensembl, May 2017 GRCm38: Ensembl release 89: ...
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We previously advanced the hypothesis that a highly regulated balance of synthesis and degradation determines collagen content in the fibrous cap of atherosclerotic plaques.1,2 In turn, collagen levels critically influence the integrity of the plaques cap, a structure whose biomechanical failure may cause most myocardial infarctions. Earlier indirect evidence suggested that collagenases of the MMP family can regulate collagen content in the plaque.5-12 We initially demonstrated overexpression of the prototypical interstitial collagenase MMP-1 in human atheromata5 and later showed colocalization of MMP-1/collagenase-1 and MMP-13/collagenase-3 with degraded collagen in these lesions as detected by an antibody specific for the collagenase cleavage site of collagen.9 Recently, our group showed that human atheromata contain a third interstitial collagenase, MMP-8/collagenase-2,11 also present in mouse atheromata, as shown here (Figure 2C). Shah et al32 reported that conditioned media of cultured ...
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lub and colleagues in the 1980s, Golub and others further studied the influence of SDD on the host response on a molecular level.. In 1997, Golub and colleagues26 studied whether SDD administration to a population of patients with chronic periodontitis would reduce the amount of specific collagenases and bone-type collagen degradation fragments in gingival crevicular fluid (GCF). Their study design included SRP in 18 subjects with chronic periodontitis, 12 of which received an adjunctive treatment with 20mg bid doxycycline. Both groups were followed up for a period of two months. A significant reduction in neutrophil-type collagenase (MMP-8) and MMP-13, which is associated with bone resorption, as well as a significant (p,0.05) reduction in collagen degradation fragments, was observed. The authors acknowledged that for the first time, in human studies, a reduction of MMP activity was detected with concomitant reduction in levels of collagen degradation fragments.. In a more recent study Choi et ...
In rheumatoid arthritis (RA) invasive tenosynovitis is associated with an increase in tendon rupture, although little is known about the mechanisms involved. We obtained specimens of noninvasive encapsulating tenosynovium, invasive tenosynovium, and wrist joint synovium from 28 rheumatoid patients. In vitro production of the matrix metalloproteinase (MMP) enzymes, MMP-8 and -9, and total collagenase activity were measured. Invasive tenosynovium produced highest levels of the collagenase MMP-8 and displayed significantly greater ability to degrade collagen type I than encapsulating tenosynovium. Levels of the gelatinase enzyme MMP-9 were similar in all groups. These results show that invasive tenosynovium is more destructive than encapsulating tenosynovium at a molecular level, providing an explanation for the increased tendon rupture associated with invasive tenosynovitis in RA.
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Matrix metalloproteases (MMPs) are a collection of enzymes capable of cleaving extracellular matrix components, growth factors, and cell-surface receptors. MMPs modulate most aspects of tumorigenesis and are highly expressed in cancer compared with normal tissues. Preclinical studies have demonstrat …
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Metalloproteinases that degrade extracellular matrix molecules play important roles in development and progression of various diseases. Among them, collagenases are unique as they have an ability to degrade triple helical interstitial collagens into 3/4 and 1/4 fragments, a crucial step for collagenolysis in the tissue. Collagenases, consisting of a catalytic domain and a hemopexin domain, requires both domains for collagenolysis. The enzymes unwind triple helical collagen before they hydrolyze the peptide bonds. Aggrecanases are also multidomain metalloproteinases belonging to the ADAMTS family, and the noncatalytic ancillary domains also play an important role in recognition of aggrecan and their activities. Attenuation of collagenase and aggrecanase activities will be achieved by inhibitors or antibodies that interact directly with those noncatalytic ancillary domains (exosite inhibitors). Such molecules will be attractive for therapy as they will be highly selective because they are based on the
The early stages of degradation of native collagen by two bacterial collagenases were studied by electron microscopy and by automatic Edman degradation. The purified collagenase from Clostridium histolyticum was shown to cleave native collagen at several sites, but not progressively from the N-terminus, as had been previously suggested. The homogeneous collagenase from Achromobacter iophagus cleaves native collagen preferentially at two sites corresponding to the interbands 33-34 and 41-42. The latter lies within the region cleaved by the eukaryotic collagenases. ...
Objectives: The gingival crevicular blood (GCB) obtained during routine periodontal probing may be a source for blood glucose measurements. The aim of this study was to c..
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