Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.4.24.3 (collagenase)
 18,340 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A number of soluble proteins contained in human aortic intimal tissue was extracted into buffered saline (pH 7.4) and identified and quantitated by immunoelectrophoresis and immunodiffusion. The proteins included IgA, IgG, IgM, B1C (C3), alpha 1-antitrypsin, alpha 2-macroglobulin, fibrinogen, albumin, LDL, HDL, alpha 1-acid glycoprotein, beta 2-glycoprotein, transferrin and ceruloplasmin. The concentration of soluble proteins was significantly higher in the atherosclerotic intima than in the normal intima. The diseased intima also contained a small amount of tissue-bound IgG, IgA and B1C which was extractable with citrate buffer at pH 3.2. The vascular band IgG, and B1C were shown by enzymatic and immunohistochemical studies to be closely associated with the collagenous tissue of the plaque. The Ig contained in the atherosclerotic plaque may be derived in part from the biosynthesis of Ig by the artery, since the incorporation of 14C-labeled leucine into IgG by the atheromatous plaque was demonstrable by radioimmunoelectrophoresis. In contrast to the diseased artery, the normal artery did not synthesize IgG and did not contain vascular bound IgG or complement. However, the normal artery was capable of fixing IgG and B1C eluted from the diseased artery. The present studies suggested that the IgG contained and synthesized by the plaque might represent an immune response to an endogenous or exogenous antigen closely associated with plaque collagen. IgG and B1C either alone or in the form of an immune complex also may play an important role in phagocytosis in the plaque and thereby influence the course of atherosclerosis. The proteolytic inhibitors, alpha 1-antitrypsin and alpha 2-macroglobulin, found in relatively high concentrations in the plaque, could enhance fibrosis of the lesion because of thier known inhibitory effects on collagenase and elastase.
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PMID:Soluble proteins in the human atherosclerotic plaque. With spectral reference to immunoglobulins, C3-complement component, alpha 1-antitrypsin and alpha 2-macroglobulin. 9 93

The bone cells and fibroblasts from fetal rat calvaria can be isolated by collagenase digestion of the collagen matrix and separated into specific cell types by free-flow electrophoresis. The method involves injection of a specially prepared suspension of cells into a stream of buffer across which is maintained an electric field of 60 V/cm. The fetal bone cell types are differentially deflected toward the anode where they can be collected. Free-flow electrophoresis of this heterogenous cell preparation yields three distinguishable peaks which can be identified by morphologic, morphometric, and enzymatic characteristics. All three cell peaks have greater than 95% viability as judged by trypan blue exclusion and will grow to confluent monolayers in culture. The data indicate that these cell peaks may be comprised of osteoclasts and/or preosteoclasts, osteoblasts and/or preosteoblasts, and fibroblasts.
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PMID:Isolation of specific bone cell types by free-flow electrophoresis. 11 88

An analog of bobine PTH [nle-8, nle-18, tyr-34 bPTH-(1-34) amide, (PTH-Ana)] which is a potent stimulator of renal adenylate cyclase has been compared with the native hormone bPTH-(1-84) and the biologically active amino terminal portion, bPTH-(1-34), for its effects on bone resorption and bone collagen synthesis in organ culture. All three compounds stimulated the release of previously incorporated 45Ca from cultured fetal rat long bone shafts with similar dose-response curves at 10(-9) to 3 X 10(-8) M. All three compounds inhibited bone collagen synthesis as measured by incorporation of proline into collagenase digestible protein, whereas incorporation into noncollagen protein was not inhibited. The effects were dose related and decreases in percent collagen synthesis were significant at 10(-9) M. Thus PTH-Ana appears to have the same effects on bone resorption and collagen synthesis as bPTH-(1-84) and (1-34) and is likely to be a valid probe for investigating PTH receptors in bone as well as in kidney.
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PMID:Comparison of the effects of a potent synthetic analog of bovine parathyroid hormone with native bPTH-(1-84) and synthetic bPTH-(1-34) on bone resorption and collagen synthesis. 11 85

Adult rat heart was dissociated into a single cell suspension by a perfusion technique which used 0.05% collagenase and 0.1% hyaluronidase in Krebs-Ringer phosphate buffer (KRP). The non-muscle cells of the suspension were separated from the myocytes by centrifugation through 3% Ficoll solution in KRP with 0.01 mM Ca2+. An approximately 90% pure suspension of isolated single muscle cells was obtained with this method. The effects of the successive steps in the dissociation procedure on the ultrastructure of the heart were studied by scanning and transmission electron microscopy. After 30 minutes of enzyme digestion, dissociation of the inner endothelial lining of the ventricle into single cells or small groups of cells became apparent. In addition, the underlying cardiac skeleton began to disintegrate and linear arrays of cardiac muscle cells were observed. After 45 minutes of enzyme digestion the number of released single cells was higher because of the separation of intercalated discs. The majority of non-muscle cells were by now dissociated from the surfaces of muscle cells. Widening of the lateral intercellular spaces between the myocardial cells was associated with separation of desmosomes. In some regions of the heart, intact desmosomes, fasciae adherentes and gap junctions were observed even though lateral intercellular spaces had widened greatly. The majority of myocardial cells had become separated from one another after 60 minutes of enzyme digestion. Separation of gap junctional sites took place in two ways: (1) by 'unzipping' them through enzyme action; (2) by tearing them mechanically. Gap junction remnants were sometimes observed in a vesiculated state within the cell. The dissociation of the heart was ineffective when perfused with media containing 1.0 or 2 mM Ca2+. Alcian blue treatment after 60 minutes of enzyme digestion revealed that the basement membrane, and its accompanying collagen fibrils, was still present on the plasma membrane of dissociated single cells. The isolated myocardial cells retained their normal morphological characteristics. This study has enabled us to understand in detail how dismantlement of highly ordered adult cardiac tissue into a single cell suspension takes place. Cell suspensions of this type should be invaluable in the study of metabolic and synthetic activities in adult myocardial cells.
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PMID:Dissociation of adult mammalian heart into single cell suspension: an ultrastructural study. 12 Mar 52

Five green monkeys were used in this study. Three animals were fed a scorbutigenic diet and the remaining two served as controls. Biopsies were dissected from the vestivular gingiva and dorsal skin and polyvinyl sponges were implanted subcutaneously during 4 week periods throughout the experimental period. The animals were sacrificed after 12 weeks and the periodontal ligament was removed. Collagen extracts were prepared from the gingival and granulation tissues and treated with bacterial collagenase. Following acid hydrolysis the total amount of proline and hydroxyproline was determined in various tissue preparations. In the tissues examined, the content of hydroxyproline decreased in the scorbutic animals throughout the experimental period. The decrease in the hydroxyproline content of the gingiva started within the first 4 weeks and was faster than that of the skin, indicating that the extent of decrease is dependent of the turnover rate of the collagen in the tissues. The synthesis of hydroxyproline was almost totally impaired in the granulation tissue formed in the sponges implanted after the 8th week of experimentation. Collagenase treatment of collagen extracts resulted in a release of proline and hydroxyproline in a higher ratio in extracts from the experimental animals than in extracts from the controls. It is concluded that ascorbic acid is a prerequisite for the maintenance of the collagen pool in the tissues and that lack of this vitamin results in the formation of a collagenase degradable protein fraction with a low hydroxyproline content.
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PMID:The collagen content of skin and gingival tissues in ascorbic acid-deficient monkeys. 12 36

A study of RNA synthesis in the legs and wings of chick embryos suggests synthesis of specific RNA's as a function of development. An increase in RNA at day 10 was followed by an increase in collagen synthesis. That RNA had a sedimentation coefficient of 23S and several of the characteristics of mRNA. Thus it appeared to contain a poly A sequence since it was retained on poly U coated-filters, it was not methylated, and its synthesis was not inhibited by low doses of actinomycin D. That RNA was found able to direct protein synthesis in a cell-free system derived from wheat germ. In the presence of that RNA, a small amount of protein was synthesized that migrated in acrylamide gel electrophoresis with the alpha chains of collagen and was partially digested by bacterial collagenase.
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PMID:RNA biosynthesis in the chick embryo during development and its relation to collagen synthesis. 13 68

A small molecular weight structural glycopeptide was solubilized after collagenase digestion of the connective tissue capsule surrounding the 5-day sponge-implant of the rat. The major amino acids are one residue each of aspartic and glutamic acids, proline, hydroxyproline and alanine and two residues of glycine, and the carbohydrates are one residue each of glucose, xylose and hexosamine and two residues of mannose. The sum of the amino acid and carbohydrate residues gives a molecular weight of 1635. Dansylation of the glycopeptide produces a single strongly fluorescent yellow-orange amino-terminal spot, not positively identified. The solubilization of the granuloma glycopeptide by collagenase and its composition are suggestive of its association with an immature form of collagen in early granulation tissue.
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PMID:Isolation and purification of a small molecular weight hydroxyproline-containing structural glycopeptide from early mammalian granulation tissue. 14 81

Macrophages incubated with products (lymphokines) secreted by stimulated spleen cells produced collagenase. Active lymphokines were obtained both from mitogen- and antigen-stimulated lymphocytes. These observations suggest that the degradation of collagen in chronic inflammatory lesions may be caused by macrophage collagenase.
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PMID:Collagenase production by lymphokine-activated macrophages. 16 38

Human lung tissues were exposed to proteolytic enzymes to determine the effects on tensile strength and to clarify the relationship between tensile strength and the amounts of collagen and elastin in the tissue. Elastase and papain depleted the tissue of elastin but failed to alter tensile strength. Trypsin had no effect on tensile strength, or on collagen and elastin content. collagenase lowered tensile strength and reduced the amount of collagen in the tissue. The findings with collagenase were in agreement with measurements in control tissues that showed a direct relationship between tensile strength and collagen content. These results confirm collagen as the principal determinant of the tensile strength of human lung.
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PMID:The effects of proteolytic enzymes on the tensile strength of human lung. 16 67

Two insoluble non-collagenous glycoprotein fractions (A and G) have been separated from puppy rib cartilage, following extraction of most of the proteoglycan and digestion of the insoluble residue with purified collagenase. After reduction, alkylation and extraction with sodium dodecylsulfate most of each protein is solubilized. Gel electrophoresis of solubilized A or G shows the presence of either one or two bands and gel chromatography shows both high and low molecular weight peaks. The production of a low molecular weight electrophoresis band from the high molecular weight Sephadex fraction indicates that there is aggregation and disaggregation of sub-units in sodium dodecylsulfate. Both A and G are high in aspartate plus glutamate and have a low hydroxyproline content. The insoluble A and G both contain hexose, uronic acid, galactosamine, glucosamine and a small amount of sialic acid, but they differ in their contents of hexose and six amino acids. They both form single bands in CsCl gradients but they differ in density. Electron microscopy shows that both insoluble glycoprotein fractions stain with lead, ruthenium red, or alcian blue plus phosphotungstate and that G contains many fine filaments. Material with the same appearance and staining properties was found to occur on the surface of collagen fibres in the undigested cartilage residue.
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PMID:Insoluble non-collagenous cartilage glycoproteins with aggregating sub-units. 16 54


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