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)

The interactions of mouse murinoglobulin and alpha-macroglobulin with several proteinases were investigated by filtration and by assays of amidolytic activity towards synthetic substrates in the presence of proteinaceous enzyme inhibitors as well as assays of the inhibition of proteolytic activity. Mouse alpha-macroglobulin formed complexes with thrombin, clotting factor Xa, plasmin, pancreatic kallikrein, plasma kallikrein, submaxillary gland trypsin-like proteinase, neutrophil elastase, and pancreatic elastase. These complexes lost the proteolytic activities against high-molecular-weight substrates, but protected the active sites of the enzymes from inactivation by their proteinaceous inhibitors. Mouse murinoglobulin showed essentially the same properties except (i) that it did not form a complex with the clotting factor Xa, and (ii) that it did not protect plasma kallikrein, neutrophil elastase or submaxillary proteinase from inactivation by their proteinaceous inhibitors, although it formed complexes with these proteinases. No interaction was detected between Clostridium histolyticum collagenase and murinoglobulin or alpha-macroglobulin. These results indicate (i) that murinoglobulin has a proteinase-binding spectrum similar to that of alpha-macroglobulin, but is weaker in the ability to protect the bound proteinases from inactivation by the proteinaceous inhibitors than alpha-macroglobulin and (ii) that mouse alpha-macroglobulin has essentially the same inhibitory spectrum as the human homologue.
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PMID:Proteinase inhibitory spectrum of mouse murinoglobulin and alpha-macroglobulin. 248 76

Aneurysms of the abdominal aorta occur with atherosclerosis or connective tissue disorders. Changes of three components of aortic media, smooth muscle cells, elastin, and collagen, which could contribute to medial weakening, are discussed. Smooth muscle cells cultured from the aging abdominal aorta (normal, atherosclerotic, or aneurysmal) have limited replicative potential at five to six cell doublings, whereas cells from aneurysmal thoracic aorta undergo more than 20 cell doublings in culture. The elastin content is much reduced in aneurysms and this is associated with an increase in elastase activity of medial homogenates to 17.8 U/ng of deoxyribonucleic acid (DNA) compared with 8.3 and 4.4 U/ng of DNA in atherosclerotic and normal aorta, respectively. An elastinolytic enzyme has been purified from aneurysmal aorta and appears to have different properties from human leukocyte elastase. Ruptured aneurysms are associated with an increased total collagenase activity but the increase could be stimulated by, or result from, an influx of inflammatory cells and does not necessarily have a causal significance. In patients with a family history of aneurysm there appears to be a decreased content of type III collagen in aortic media: 24% +/- 4% compared with 32% +/- 5% in most aneurysms. Familial aneurysms are most common in women, and preliminary results suggest that a polymorphic variant of the type III collagen gene, defined by restriction enzyme digest, may be associated with aneurysmal disease in women. The genetic approach may define causal mechanisms predisposing patients to aneurysmal dilatation.
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PMID:Cellular, enzymatic, and genetic factors in the pathogenesis of abdominal aortic aneurysms. 253 34

Chick-derived native cartilage collagen type X and the pepsin-resistant 45 kDa fragment were susceptible to attack by human synovial collagenase and neutrophil elastase at 25 degrees C and 35 degrees C. Synovial collagenase cleaved type X collagen at two sites which were equally susceptible to the enzyme. In contrast, elastase produced three cleavages, but the sensitive loci showed different susceptibilities as judged by the sequential appearance of specific breakdown products. Both enzymes produced a major, enzyme-resistant fragment of approximately 32 kDa at 35 degrees C, and both of these end-products co-migrated in SDS polyacrylamide gels. Human chondrocyte-derived collagenase also degraded native, 59 kDa collagen type X in a similar manner to that shown by the synovial collagenase. From amino acid sequence data the enzyme cleavages probably occur at three regions of sequence imperfection. The specific cleavages brought about by synovial or chondrocyte collagenase, or neutrophil elastase, may have a functional catabolic role in vivo, and in vitro might provide useful tools with which to further analyse specific properties of the native collagen type X molecule.
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PMID:Cleavage of collagen type X by human synovial collagenase and neutrophil elastase. 254 40

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

Bovine vitreous body and aorta contain extractable leukocyte elastase inhibitors, which were purified by gel filtration and affinity chromatography on agarose-pancreatic elastase. The purified inhibitor preparation from aorta was resolved by polyacrylamide gel electrophoresis into a main band migrating slightly faster than commercial Trasylol and a more weakly stained band migrating close to chymotrypsinogen. The purified inhibitor preparation from both sources inhibited, in a competitive fashion, purified human leukocyte elastase and was ineffective against bovine trypsin and leukocyte cathepsin G or collagenase. These inhibitors from vitreous body and aorta were distinguishable by several criteria from serum inhibitors.
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PMID:Isolation and partial characterization of neutrophil elastase inhibitors from bovine vitreous and aorta. 337 Oct 70

Neutrophil proteases are believed to play a role in the pathogenesis of a variety of human diseases. While many studies of proteases in models of disease have focused on elastase, neutrophils contain several proteases some of which share a high degree of homology. This report describes the production and characterization of an IgG1 murine monoclonal antibody (AHN-10) that reacts with human neutrophil elastase but not with the other major neutrophil neutral proteases: cathepsin G, proteinase 3, collagenase, or the newly purified neutral protease, esterase N. AHN-10 inhibited the elastinolytic activity of purified human neutrophil elastase and could detect elastase in alcohol-fixed cytospin preparations. The epitope recognized by AHN-10 was resistant to treatment with NaIO4, suggesting that the epitope is not a carbohydrate. AHN-10 should be useful for the immunolocalization of neutrophil elastase in tissue specimens and as a stable source of characterized antibody for quantitative identification of neutrophil elastase.
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PMID:Preparation and characterization of a monoclonal antibody that inhibits human neutrophil elastase activity. 341 Dec 32

An inhibitor of serine proteinases from human articular cartilage was purified to homogeneity by sequential ultrafiltration and ion exchange chromatography on CM-Sephadex C-50. The apparent molecular weight of the cationic glycoprotein (pI greater than 10) was determined to be 16.5 X 10(3) by SDS gel electrophoresis. The inhibitor blocked the activity of leukocyte elastase, cathepsin G and trypsin but not leukocyte collagenase. In kinetic studies for the interactions with leukocyte elastase a firm enzyme-inhibitor binding was obtained. Amino acid analyses did not reveal homologies with other serine proteinase inhibitors already purified from human tissues.
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PMID:Purification and characterization of a serine proteinase inhibitor from human articular cartilage. 349 75

Leukocyte-derived proteases may contribute to the destruction of basement membranes during inflammation. We have, therefore, examined the degradation of human type IV procollagen (PC) by purified human neutrophil elastase (HLE). Native [14C]proline-labeled type IV PC was isolated from cultures of human HT-1080 cells and incubated with HLE for various times at 25 or 37 degrees C. Cleavage products were resolved by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and identified by CNBr peptide mapping. Incubation of type IV PC with HLE (less than 1:10 HLE:type IV weight ratio) resulted in cleavage of the pro alpha 1 (IV) and pro alpha 2 chains (Mr 180,000 and 175,000) to discrete components of Mr greater than 140,000. Peptide mapping indicated that the carboxy-terminal collagenase-resistant domains of both chains were rapidly and preferentially degraded. Longer incubations or incubations at higher enzyme:substrate ratios resulted in extensive and asymmetric internal cleavage with the generation of fragments similar in size distribution to the major pepsin-resistant fragments of type IV collagen. Our findings indicate that soluble, native human type IV PC is a substrate for HLE and is preferentially cleaved within the globular carboxy-terminal domains of the pro alpha 1 and pro alpha 2 chains. We suggest that even limited cleavage of type IV PC by HLE may disrupt intermolecular carboxy-terminal interactions believed to be important for basement membrane assembly and for maintaining basement membrane structure in vivo.
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PMID:Degradation of native type IV procollagen by human neutrophil elastase. Implications for leukocyte-mediated degradation of basement membranes. 367 85

The present study demonstrates that a granule fraction derived from human polymorphonuclear leukocytes possesses elastinolytic activity, and that the latter can be separated from the collagenase present in these cells. Properties of the human leukocyte elastase differ sufficiently from those of pancreatic elastases of different species as to suggest that the former enzyme is a distinct and separate entity. Thus, soybean trypsin inhibitor and salivary kallikrein inhibitor (Trasylol) fail to inhibit elastolysis by the pancreatic enzyme, but do inhibit the leukocyte elastinolytic agent. Elastolysis by human leukocyte granule extract does not show significant salt inhibition, whereas that catalyzed by pancreatic elastase is markedly reduced when ionic strength is increased to physiological levels. The leukocyte granule extract is at least 10 times more resistant to serum elastase inhibitor than is the purified pancreatic enzyme. Both enzymes show optimal elastolysis above pH 8.5, but the leukocyte factor still retains 50% of its maximal elastolytic activity at pH 6-7; whereas the activity of the pancreatic enzyme falls to 10% or less of its maximal value under the same conditions. The foregoing characteristics of the human leukocyte elastase suggest that it, rather than pancreatic (serum) elastase, may mediate pathological elastolysis during acute arteritis in man. In keeping with this suggestion, the present experiments also show that elastica staining of human arterial vessels is reduced by incubation of tissues with human leukocyte granule extracts in vitro.
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PMID:Mediators of inflammation in leukocyte lysosomes. IX. Elastinolytic activity in granules of human polymorphonuclear leukocytes. 530 65

Purified polymorphonuclear leukocyte elastase degraded native human liver type III collagen at 27 degrees C by making a cleavage through the triple helix. The enzyme had no effect on human type I collagen. The reaction was inhibited by phenylmethanesulfonyl fluoride (PhCH2SO2F) but not by EDTA. The collagen reaction products were identical with those generated by human rheumatoid synovial collagenase when analyzed by polyacrylamide gel electrophoresis and gel filtration. NH2-trminal sequence analysis indicated that the enzyme cleaved at an isoleucyl-threonyl bond located 4 residues on the carboxyl side of the established cleavage site for animal collagenases. Therefore, it is likely that in pathologic states, type III collagen can be selectively depleted from the matrix by this enzyme.
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PMID:Specific cleavage of human type III collagen by human polymorphonuclear leukocyte elastase. 625 89


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