Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:3.4.24.3 (collagenase)
18,340 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Osteoarthritis is characterized by a loss of articular cartilage due at least in part to the action of degradative enzymes secreted by chondrocytes. We have investigated the effect of type II collagen from cartilage and interleukin 1 on collagenase production in cultures of rabbit articular chondrocytes. Interleukin 1 alone stimulated the chondrocytes to secrete collagenase but this response was increased as much as fivefold by the addition of rabbit type II collagen. Bovine type II and chick type I collagens were also stimulatory. The native form of the collagens was not required since denatured collagens and purified chick type II alpha chains were effective. The observed effects of collagens and interleukin 1 may contribute to the progressive nature of osteoarthritis.
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PMID:The stimulation of collagenase production in rabbit articular chondrocytes by interleukin-1 is increased by collagens. 282 8

This study was undertaken to examine and quantitate the chemical injury and repair of the dog nucleus pulposus in collagenase-induced chemonucleolysis. Thirty three adult mongrel dogs were used into which the purified collagenase was injected at a rate of 200 units. The dogs were sacrificed after roentgenography. Disc specimens were stained primarily with safranin-O for microscopic study, and fresh tissues were used for electron microscopic study. For immunohistochemical analysis, paraffin sections were reacted with anti-bovine types I, II and III collagen antibodies. Two weeks after the injection, the height of the injected disc was reduced by about 50% and there was no sign of recovery for 52 weeks. There was a profound loss of safranin-O stainability in the nucleus pulposus, annulus fibrosus and cartilagenous endplate. By 8 weeks, regeneration of the nucleus pulposus began and chondrocytes appeared from the junctional area. The regenerated nucleus pulposus was stained well with safranin-O and consisting largely of type II collagen immunohistochemically. In the regenerated nucleus pulposus, collagen fibers and proteoglycans were reconstructed in a net-work with hyaluronic acids.
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PMID:A pathological study of experimental chemonucleolysis with collagenase. 283 93

The action of purified rheumatoid synovial collagenase and human neutrophil elastase on the cartilage collagen types II, IX, X and XI was examined. At 25 degrees C, collagenase attacked type II and type X (45-kDa pepsin-solubilized) collagens to produce specific products reflecting one and at least two cleavages respectively. At 35 degrees C, collagenase completely degraded the type II collagen molecule to small peptides whereas a large fragment of the type X molecule was resistant to further degradation. In contrast, collagen type IX (native, intact and pepsin-solubilized type M) and collagen type XI were resistant to collagenase attack at both 25 degrees C and 35 degrees C even in the presence of excess enzyme. Mixtures of type II collagen with equimolar amounts of either type IX or XI did not affect the rate at which the former was degraded by collagenase at 25 degrees C. Purified neutrophil elastase, shown to be functionally active against soluble type III collagen, had no effect on collagen type II at 25 degrees C or 35 degrees C. At 25 degrees C collagen types IX (pepsin-solubilized type M) and XI were also resistant to elastase, but at 35 degrees C both were susceptible to degradation with type IX being reduced to very small peptides. Collagen type X (45-kDa pepsin-solubilized) was susceptible to elastase attack at 25 degrees C and 35 degrees C as judged by the production of specific products that corresponded closely with those produced by collagenase. Although synovial collagenase failed to degrade collagen types IX and XI, all the cartilage collagen species examined were degraded at 35 degrees C by conditioned culture medium from IL1-activated human articular chondrocytes. Thus chondrocytes have the potential to catabolise each cartilage collagen species, but the specificity and number of the chondrocyte-derived collagenase(s) has yet to be resolved.
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PMID:Susceptibility of cartilage collagens type II, IX, X, and XI to human synovial collagenase and neutrophil elastase. 284 Nov 21

Human macrophages have been implicated in connective tissue remodeling; however, little is known about their direct effects upon collagen degradation. We now report that human alveolar macrophages in culture produced both a collagenase and a collagenase inhibitor. The collagenase was secreted in latent form and could be activated by exposure to trypsin. Collagenase production could be increased three- to fourfold by incubating the cells with lipopolysaccharide, but synthesis was largely unaffected by exposure to phorbol myristate acetate. By several criteria, macrophage collagenase was the same as the collagenase secreted by human skin fibroblasts: (a) they were antigenically indistinguishable in double immunodiffusion; (b) both degraded type III collagen preferentially to type I, had little activity against type II collagen, and none against types IV and V, and (c) their affinity for susceptible collagens was equivalent, Michaelis constant = 1-2 microM. Collagenase inhibitory activity was also present in the macrophage-conditioned medium, and was accounted for by an antigen that showed immunologic and functional identity with the collagenase inhibitor secreted by human skin fibroblasts. The amount of inhibitor released by unstimulated cells, approximately 100 ng/10(6) cells per 24 h, was substantially augmented by both phorbol and lipopolysaccharide, although considerable variability in response to these agents was observed between macrophage populations derived from different subjects. As negligible quantities of collagenase or collagenase inhibitor were detectable intracellularly, it appeared that both proteins were secreted rapidly after synthesis. Thus, human macrophages have the capacity to modulate collagen degradation directly by production of collagenase and collagenase inhibitor.
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PMID:Human alveolar macrophages produce a fibroblast-like collagenase and collagenase inhibitor. 299 37

Bone resorption in the temporal bone of rats was induced by peripheral immunizations of heterogeneous type II collagen. Bone resorption was found at both the tympanic bone and the petrous bone of the otic capsule. Macrophages, fibroblasts and osteoclasts were found in the enlarged spaces of bone. Immunohistochemical studies demonstrated that macrophages, fibroblasts and osteoclasts produced collagenase and prostaglandins in the bone resorption processes, suggesting that these cells are responsible for the resorption observed.
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PMID:Type II collagen induced bone resorption in the temporal bone of rats: histological and immunohistochemical studies. 299 9

We obtained monoclonal antibodies specific for human type II collagen and characterized them using human collagen type I, II, III and V and tropocollagen A (3/4) (TCA) and tropocollagen B (1/4) (TCB) fragments of type II collagen which were obtained by digestion with tadpole collagenase. These antibodies were of the IgG2a class and specific for the conformational determinant of TCA fragment of type II collagen. When injected intravenously into DBA/1J mice, one of the monoclonal antibodies induced arthritis, which was characterized by early onset, mildness in severity and preferential localization mainly in the peripheral joints of the lower extremities. These results suggest that, at least, one of the arthritogenic determinants of type II collagen for collagen-induced arthritis of mice exists in the three quarter region from the N-terminus of type II collagen.
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PMID:Characterization of monoclonal antibody specific for human type II collagen: possible implication in collagen-induced arthritis. 299 57

Type X collagen was cleaved at two sites by a purified human skin collagenase. Two experimental approaches were used to identify the location of the cleavage sites. First, native type X collagen was digested with the enzyme, and the rotary-shadowed products were visualized in the electron microscope. The major collagenase fragment of type X contained the epitope recognized by a monoclonal antibody (X-AC9). The antibody was used as a point of reference to locate the position of the cleavage fragment within the native molecule. Second, the digestion of radiolabeled type X collagen substrates was analyzed by gel electrophoresis. The complete cleavage of type X generated three products with 32-, 18-, and 9-kDa chains. The 32-kDa peptides were present in a triple-helical conformation and demonstrated a midpoint denaturation temperature of 43 degrees C in CD experiments. The 18-kDa peptide contained the tyrosine-rich globular domain of the molecule. The 9-kDa peptide was derived from the triple-helical end of the native molecule. Type X collagen was cleaved more rapidly by the vertebrate collagenase than was type II collagen in in vitro solution studies.
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PMID:Type X collagen contains two cleavage sites for a vertebrate collagenase. 300 23

Collagenase activity of the knee joint menisci of patients suffering from rheumatoid arthritis was approximately 3-fold higher than that found in menisci of control patients. The mean collagenase activity in the macroscopically more diseased parts of the rheumatoid menisci was significantly higher than that in the less damaged areas. The specific degradation products resulting from the cleavage of human meniscoid type II collagen by rheumatoid meniscoid collagenase were demonstrated by SDS-polyacrylamide gel electrophoresis. Addition of N-ethylmaleimide, which activates latent mammalian collagenases, did not further increase collagenase activity in rheumatoid menisci. Thus in rheumatoid meniscus, collagenase may be synthesized and then activated, probably by proteolytic enzymes involved in the inflammatory reaction.
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PMID:Increased collagenase activity in human rheumatoid meniscus. 302 34

We have shown that when chondrocytes are isolated by collagenase digestion of hyaline cartilage from growth plate, nasal, and epiphyseal cartilages of bovine fetuses they rapidly elaborate an extracellular matrix in culture. Only growth plate chondrocytes can calcify this matrix as ascertained by incorporation of 45Ca2+, detection of mineral with von Kossa's stain and electron microscopy. There is an extremely close direct correlation between 45Ca2+ incorporation in the first 24 h of culture and the content of the C-propeptide of type II collagen, measured by radioimmunoassay, at the time of isolation and during culture. Moreover, growth plate cells have an increased intracellular content of the C-propeptide per deoxyribonucleic acid and, during culture, per hydroxyproline (as a measure of helical collagen) compared with nasal and epiphyseal chondrocytes. In growth plate chondrocytes 24,25-dihydroxycholecalciferol (24,25-[OH]2D3), but not 1,25-dihydroxycholecalciferol alone, stimulates the net synthesis of the C-propeptide and calcification; proteoglycan net synthesis is unaffected. Together, these metabolites of vitamin D further stimulate C-propeptide net synthesis but do not further increase calcification stimulated by 24,25-(OH)2D3. These observations further demonstrate the close correlation between the C-propeptide of type II collagen and the calcification of cartilage matrix.
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PMID:The calcification of cartilage matrix in chondrocyte culture: studies of the C-propeptide of type II collagen (chondrocalcin). 349 35

Localized bone resorption in the otic capsules of experimental rats was induced by immunization with type II collagen. The otospongiosis-like lesion showed enlarged vascular spaces that contained many fibroblasts and macrophages as well as occasional osteoclasts. A high level of acid phosphatase activity in the sera of immunized rats suggested that this enzyme is one of the important factors causing decalcification of the bony otic capsule, the first step of bone resorption. Immunofluorescent assay showed that collagenase and cyclooxygenase (prostaglandin synthetase) appeared within macrophages, fibroblasts, and osteoclasts in the bone resorption areas. These findings suggest that the collagenase and prostaglandin synthetase being produced by macrophages, fibroblasts, and osteoclasts are also involved in the processes of bone resorption in otospongiosis. Immunolocalization assay showed deposition of immunoglobulin and fibronectin on the bone matrix and vascular wall within the otospongiotic lesions. Chemotaxis studies showed that both anti-type II collagen serum and fibronectin might play a role as chemoattractants to recruit macrophages and fibroblasts to the bone resorption sites. In vitro studies also showed anti-type II collagen serum stimulates the fusion of macrophages to become multinucleated osteoclast-like cells. The antiserum also activate these cells to produce collagenase and prostaglandin synthetase. It is concluded that the chemotactic processes of macrophages and fibroblasts, the multinucleation of macrophages, and the activation of these cells may be basic processes causing bone resorption in otosclerosis. When sodium fluoride, an inhibitor of hydrolytic and proteolytic enzymes, was given to rats immunized with type II collagen, no obvious inhibition of bone resorption was seen in histologic sections.
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PMID:Bone resorption in experimental otosclerosis in rats. 350 79


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