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)

Degradation of type II and III collagens by tadpole collagenase in a mixture of both substrates was monitored by SDS-polyacrylamide gel electrophoresis in 3 M urea, followed by densitometric quantiation. The degradation rates of type II and III collagens were increased and decreased, respectively, by the mutual prsence, compared with those of type II and III collagens alone. The results suggest that the degradation of type II collagen in vivo may be regulated by the presence of other type(s) of collagen, particularly in such a case as resorption of cartilage in the region of newly forming osteoid tissue.
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PMID:Degradation rates of type II and III collagens by tadpole collagenase are modulated by mutual presence. 624 1

Mice infected with Schistosoma mansoni develop hepatic fibrosis associated with enhanced collagen synthesis that out-paces induced collagenase activity. Administration of one dose of concanavalin A [Con A (200 micrograms)] by i.p. injection to mice at 5 or 6 weeks after infection with 50 S. mansoni cercariae decreased liver collagen content by 50% compared to levels in control-infected mice injected with either homologous immunoglobulin (200 micrograms) or phosphate-buffered saline; additional doses of Con A had no further effect. The decrease in collagen content could not be attributed to either decreased egg deposition in the liver or inhibition of liver collagen synthesis, but was coincident with a greater solubility of granulomas. Collagen contents of skin and tail were unaffected. The relative solubilities of liver collagen in 8 M urea: 10 mM dithiothreitol were greater in treated animals as compared to controls. However, the amounts of collagen solubilized were similar in both sets of animals, since the total collagen content of treated mice was 50% of the controls. A possible explanation for these results is that much of the synthesized collagen does not accumulate in treated animals, whereas it does accumulate in controls. Peak collagenase and neutral protease activities occurred at 7 weeks postinfection in treated animals, and were 2-fold greater than in controls. Similar effects were observed when succinylated Con A was administered. The results suggest that Con A may modulate host-immune responses influencing fibrogenesis in hepatic murine schistosomiasis.
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PMID:Concanavalin A reduces liver collagen accumulation in murine schistosomiasis. 627 83

A skeletal growth factor was isolated and purified from demineralized human bone matrix. A dose of 6 micrograms/mL of the purified factor significantly increased the proliferation rate of embryonic chick bone cells in serum-free culture (292% of controls, p less than 0.0001) but had no effect on embryonic chick skin cells plated at the same initial density. The factor is sensitive to inactivation by trypsin and urea, but not by collagenase, 20% butanol, or 1% mercaptoethanol. It is also resistant to inactivation by heat (stable for 15 min at 75 degrees C) and extremes of pH (stable for 30 min at 4 degrees C from pH 2.5 to 10.0). Purification of the active factor by selective heat and acid precipitations, molecular sieve column chromatography, and preparative polyacrylamide gel electrophoresis provided a material that was homogeneous by the criteria of high-pressure liquid chromatography, polyacrylamide gel electrophoresis, and isoelectric focusing. The apparent molecular weight is 83 000. The purified factor increases bone cell proliferation at doses comparable to other mitogens: 0.3 microgram/mL (3.6 nM) significantly increases DNA synthesis to 231% of controls (p less than 0.001). The purified factor was also active on cultured embryonic chick bones, enhancing the growth rate of tibiae and femurs, as measured by increased dry weight (185% of controls, p less than 0.025) and [3H]proline incorporation (164% of control, p less than 0.001), respectively.
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PMID:Purification of a skeletal growth factor from human bone. 628 76

A freeze-etch replica method combined with biochemical analyses was used to investigate the ultrastructural organization of the bovine Descemet's membrane. The freeze-etch replica observations revealed that the intact Descemet's membranes were composed of stacks of two-dimensionally arranged hexagonal lattices, in which four components were resolved; (1) round densities as nodes, (2) rod-like structures connecting the densities, (3) randomly oriented fine filaments within the lattices, and (4) amorphous materials covering the lattices. When the membranes were treated with sodium dodecyl sulfate (SDS) and mercaptoethanol, only the amorphous materials were solubilized. However, both the amorphous materials and rod-like structures disappeared in SDS-mercaptoethanol-urea-treated membranes. When the membranes were treated with a very low concentration (0.0005%) of collagenase, rod-like structures and round densities remained insoluble. If the concentration was raised to 0.01%, only the round densities persisted. Comparing these data with the amino acid analysis of each fraction, the following conclusions may be drawn: rod-like structures and fine filaments contain collagenous proteins of different solubility, while round densities and amorphous materials are non-collagenous in nature.
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PMID:The fine structure of the bovine Descemet's membrane with special reference to biochemical nature. 629 70

All of the collagenase activity extracted from cultured bovine dental pulp tissue with NaCl or urea solutions was due to enzyme in a latent form and identified as a typical animal collagenase. Isotonic sucrose solution solubilized no detectable collagenase activity from cultured dental pulps. Also, no collagenase activity was extracted from either fresh bovine dental pulps or those cultured in Tyrode's solution containing 50 micrograms/ml cycloheximide. A two-day difference was observed between the appearance of collagenase activity in the cultured pulps and in the culture medium. The activity profiles in the culture media showed essentially no difference with or without the addition of cyclohexamide on and after the 10th day of culture, indicating that the biosynthesis of collagenase in the cultured pulp might have terminated around that time. About 80% of the total pulp collagenase activity was extracted by a bacterial collagenase procedure. Nearly half (43.5%) of the collagenase activity extracted from the cultured pulps with NaCl or urea solution was precipitated with collagen molecules in the presence NaCl, and most of the precipitated activity retained in the precipitate even after washing it with NaCl-buffer solution. These facts suggest a close association of collagenase with the collagen in cultured dental pulp tissue.
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PMID:Extraction of latent-type collagenase from cultured bovine dental pulps with NaCl or urea or by collagen degradation. 629 Jan 34

The extracellular matrix, prepared by extraction of confluent cultures of human lung WI-38 fibroblasts with a dipolar tonic detergent, contains four major glycoproteins: fibronectin, GP250, GP170, and GP140. All the glycoproteins can be surface-labeled; however, only fibronectin and GP170 can be readily removed by digestion with trypsin (Carter, W. G., and Hakomori, S. (1981) J. Biol. Chem. 256, 6953-6960). Most of the noncovalently bound GP250, GP170, and GP190, an additional minor glycoprotein, can be dissociated from the matrix by extraction with 8 M urea. The remaining insoluble matrix is stabilized by extensive intermolecular disulfide bonds and contains primarily GP140 and fibronectin (Carter, W. G. (1982) J. Biol. Chem. 257, 3249-3257). Affinity-purified, monospecific antibodies were prepared against GP[140 and fibronectin and utilized for detection of GP140 and fibronectin in extracts and conditioned media of WI-38, WI-38 VA13, WI-26, WI-26 VA4, and HT-1080 cells. Additional affinity-purified, polyspecific antibodies that react with GP250, GP190 GP170, and GP140 were also utilized. Fibronectin, GP250, GP190, GP170, and GP140 were all absent from transformed cells. With the exception of GP140, the absence of these glycoproteins from the matrix of transformed cells was paralleled by their accumulation in the conditioned culture media. Incubation of conditioned culture media with collagenase indicated that GP190, GP170, and GP140, as well as other glycoproteins, were digested. Antibodies to GP140 did not react with any other cellular component indicating that it is not a processing product of other matrix glycoproteins. GP140 has characteristics unlike all reported collagen types and appears to be a new collagen-like glycoprotein. In contrast, neither Gp250 nor fibronectin were sensitive to digestion with collagenase. Antibodies that react with GP250 did not react with fibronectin and vice versa, suggesting that GP250 and fibronectin do not share antigenic determinants. The interaction of labeled fibronectin and the labeled, gelatin-binding domain of fibronectin with cells after fractionation on polyacrylamide gels indicated that GP170 is the primary procollagen receptor for fibronectin in the extracellular matrix. GP140 also bound fibronectin but to a lesser degree. Soluble GP170 and GP190 present in the conditioned medium of cultured cells also bound to insolubilized fronectin, confirming the association of GP170 and GP190 with fibronectin. The interaction of the glycoprotein components in the matrix are discussed in relation to their potential cooperative function in cell attachment and their failure to adhere to the surface of transformed cells.
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PMID:Transformation-dependent alterations is glycoproteins of extracellular matrix of human fibroblasts. Characterization of GP250 and the collagen-like GP140. 629 8

Basement membranes isolated from the entire neural retinae of normal cows consist of a heterogeneous mixture of polypeptides resolvable as two major populations, one collagenous and the other non-collagenous. The non-collagenous population consists of disulfide-bonded aggregates of which the major fraction is soluble in lithium dodecyl sulfate (LDS) at 4 degrees C without reducing agent, with the remainder requiring reduction for solubilization at 4 degrees C. Only the second 4 degrees C extract is contaminated with small amounts of hydroxylated amino acids. The non-collagenous population consists of up to 25 polypeptides detectable in sodium dodecyl sulfate (SDS) gels, all of which stain blue with Coomassie Blue R-250, are insensitive to bacterial collagenase and migrate on or slightly below the central diagonal in urea-SDS/SDS electrophoresis. The collagenous population is soluble in LDS at 100 degrees C under reducing conditions and has a collagenous amino acid composition, although consisting of only 272 glycine residues/1000. This fraction consists of four major and four minor polypeptides detectable in SDS gels, all of which stain red (metachromatically) with Coomassie Blue R-250, are degraded by bacterial collagenase and migrate below the central diagonal in urea-SDS/SDS electrophoresis. The four major collagenous polypeptides are larger than the alpha-chains of type I collagen. In total, the solubilized proteins account for 60% of the general protein, but only 30% of the sum of hydroxyproline and hydroxylysine. The insoluble residue has a collagenous amino acid composition similar to that of the 100 degrees C extract, but with lower 3-hydroxyproline and hydroxylysine contents.
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PMID:Selective solubilization of two populations of polypeptides from bovine retinal basement membranes. 629 40

We have isolated a major glycoprotein that appears to be associated with rat skeletal muscle basement membrane. We determined that the glycoprotein was part of the muscle cell surface complex when we found it to be enriched in preparations of muscle ghosts. We isolate the glycoprotein from homogenized muscle preextracted with 4 M and 8 M urea. It elutes as a major component in the presence of 8 M urea/50 mM 2-mercaptoethanol. Its apparent molecular weight on sodium dodecyl sulfate gels is 130,000. Amino acid analysis indicates that it is not a collagen but that it does contain small amounts of hydroxyproline and hydroxylysine. There may be collagenous domains in the glycoprotein molecule, for it is cleaved into three fragments by purified bacterial collagenase. Immunoperoxidase staining confirms that the 130,000-dalton protein is localized at the surface of adult skeletal muscle cells. It is probably a general basement membrane-associated glycoprotein because we found material immunologically cross-reactive with the muscle glycoprotein in basement membrane regions of kidney, liver, brain, and small intestine. We have shown the glycoprotein to be distinct from fibronectin, laminin, and types I, III, IV, and V collagens in enzyme-linked immunosorbent assays.
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PMID:A basement membrane-associated glycoprotein from skeletal muscle. 629 56

Human cementum was demineralized and exhaustively extracted with EDTA and then digested with collagenase. The insoluble residue after digestion was extracted successively with 8M urea and with 8M urea containing 0.1M mercaptoethanol. The non-collagenous fraction accounted for a larger proportion of the total organic matrix than previously found in bone and dentine, largely due to the presence of more collagenase-insoluble material. Fractionation of the EDTA-soluble material resulted in less-acidic fractions, showing similarities to the corresponding fractions of bone and dentine, and anionic fractions with lower levels of acidic amino acids than those from other hard tissues. Fractions obtained from the soluble collagenase-released material after ion-exchange chromatography and gel filtration, although more heterogeneous than those of bone and dentine, showed many similarities, thus confirming the close homology within this fraction from the various hard tissues. The insoluble residue after collagenase digestion appeared to be of the acid-structural protein type found also in bone, dentine and a wide range of connective tissues.
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PMID:The amino-acid composition of the non-collagenous organic matrix of human cementum. 631 8

We examined effects of osmolality or sodium concentration on vasopressin induced cyclic AMP generation in the medullary thick ascending limbs isolated from collagenase treated rat kidneys. Vasopressin-stimulated cyclic AMP generation was increased as a function of NaCl concentration of the incubation medium. Addition of sucrose was also effective in enhancing the vasopressin-stimulated cyclic AMP, whereas addition of urea was without effect. When incubation medium was made hypertonic with sodium cyclamate, vasopressin-stimulated cyclic AMP generation was also enhanced. When choline chloride was used instead of sodium cyclamate, only an insignificant increase in the hormone-stimulated cyclic AMP generation was observed. These results suggest that the responsiveness of the rat medullary thick ascending limbs to vasopressin is regulated, at least in part, by transmembrane osmotic gradient.
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PMID:Effects of solute concentration on vasopressin stimulated cyclic AMP generation in the rat medullary thick ascending limbs of Henle's loop. 632 7


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