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)

Using collagenase digestion as an assay for collagen in partially synchronized secondary cultures of chick embryo fibroblasts, we find that the rate of collagen synthesis remains at a constant fraction of overall protein synthesis (5%) regardless of the growth rate of the cells even when the rate of protein synthesis is accelerated 5-fold by adding serum and altering the pH of the culture medium. However, in cells oncogenically transformed by Rous sarcoma virus, the relative rate of collagen synthesis was decreased by 50% 24 hours after infection and was 10% of the initial rate after 5 days. This selective decrease in rate of collagen synthesis could be reversed in cells infected with an RSV temperature-sensitive transformation-defective mutant at the non-permissive temperature, indicating that the decrease in the rate of collagen synthesis was not merely the result of viral infection but was a direct consequence of oncogenic transformation.
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PMID:Coordinate control of collagen synthesis and cell growth in chick embryo fibroblasts and the effect of viral transformation on collagen synthesis. 1 83

Transformation of the chick fibroblast surface has been studied in cells infected with Schmidt-Ruppin Rous sarcoma virus and the temperature-sensitive mutant of this virus, TS-68. Major findings following transformation induced by a shift from nonpermissive (41 C.) to permissive (36 C.) temperature in TS-68 infected cells were: (1) rapid cessation or slowing of the synthesis of a protein, M.W. 100-200,000, localization uncertain; (2) cessation or slowing of the synthesis of a plasma membrane protein, M.W. 45,000, within 2-4 hours; (3) cessation or slowing of the synthesis of a large trypsin- and collagenase- sensitive protein (M.W. greater than 200,000) only after an extended period of morphologic transformation. In addition, increased quantities of type-specific viral antigen in the membranes of infected cells were observed in TS-68-infected cells at 41 compared with 36 C.
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PMID:Comparisons of major cell-surface proteins of normal and transformed cells. 16 7

Antibodies to fibronectin and to distinct types of procollagens and collagens were used in immunofluorescent staining to localize these proteins in cell cultures. Normal human skin or lung fibroblasts produced a fibrillar pericellular matrix in which fibronectin and procollagen (types I and III) showed extensive codistribution. Fibronectin and procollagen were synthesized by the same cells as judged by double-stain immunofluorescence. Pericellular procollagen was specifically digested with collagenase without an effect on the fibrillar distribution of matrix fibronectin. Brief treatment with trypsin removed both matrix proteins. The human tumor cell lines HT-1080 (fibrosarcoma) and RD (rhabdomyosarcoma) produced little or no matrix fibronectin or procollagen. At sites of cell contact, simian virus 40-transformed lung fibroblasts (VA13) produced small amounts of pericellular fibrillar matrix fibronectin that codistributed with procollagen type I. Intracellular fibronectin and procollagen were visualized in all of these human sarcoma cell lines. When chicken embryo fibroblasts infected with a T class mutant (NY68) of Rous sarcoma virus temperature-sensitive for transformation were maintained at the nonpermissive temperature (41 degrees ) the cells had normal phenotype and a fibrillar matrix containing fibronectin and procollagen was present. At the permissive temperature (35 degrees ), the cells showed transformed phenotype and the matrix was lost. The failure to produce a pericellular fibronectin/collagen matrix may account for several phenotypic characteristics of transformed cultured fibroblasts.
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PMID:Codistribution of pericellular matrix proteins in cultured fibroblasts and loss in transformation: fibronectin and procollagen. 21 6

The effect of the potent tumor promoter phorbol 12-myristate 13-acetate (PMA) on collagen synthesis, a differentiated property of chick embryo fibroblasts, was examined. Collagen synthesis, as measured by the rate of formation of [3H]hydroxyproline from [3H]proline, was found to be decreased in cells treated with PMA but not in cells treated with the parent alcohol phorbol. The decrease in collagenase-sensitive proteins was confirmed by polyacrylamide gel electrophoresis of cell lysates, indicating that the decrease could not be ascribed simply to an effect on prolyl hydroxylase. Although a decrease in collagen synthesis was observed after one day, five days were required for a maximal reduction to 20% of that of dimethyl sulfoxide-treated controls. The effect of PMA on collagen synthesis was reversible. It was therefore not the result of a permanent transformation of the cells or of the selection of a population of cells with a reduced capacity for collagen synthesis. Collagen synthesis was decreased in chick embryo fibroblasts transformed by Rous sarcoma virus. Treatment of these cells with PMA for 5 days brought about a further decrease to 50% of the level in dimethyl sulfoxide-treated transformed controls.
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PMID:Decrease in collagen production in normal and Rous sarcoma virus-transformed chick embryo fibroblasts induced by phorbol myristate acetate. 21 32

Chick cells infected with Rous sarcoma virus are characterized by a wide variety of changes known collectively as transformation. Among these are decreases in the level of procollagen biosynthesis and in the level of procollagen mRNA. In this communication, we examine the time course of the decrease in procollagen biosynthesis, as measured by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and collagenase assay, and compare it with the decrease in procollagen mRNA sequences measured by hybridization to a complementary DNA. Procollagen biosynthesis and procollagen mRNA sequences decrease simultaneously after infection. Even the initial decrease in procollagen biosynthesis, therefore, is due to a decline in the level of procollagen mRNA.
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PMID:Declining procollagen mRNA sequences in chick embryo fibroblasts infected with rous sarcoma virus. Correlation with procollagen synthesis. 22 54

Myotubes prepared from the Japanese quail embryo at 9 days gestation were cultivated in the presence of glycyl-L-glutamine (Gly-Gln, beta-endorphin C-terminal dipeptide) or glycyl-glutamic acid (Gly-Glu), and changes in the activity of acetylcholinesterase (AChE) molecular forms and binding of 125I-alpha-bungarotoxin (alpha BGT) to cell surface nicotinic acetylcholine receptors were measured. The A12 oligomer was the major form of AChE in the cultures. The activity of all molecular forms of the enzyme was increased in the presence of Gly-Gln, but Gly-Glu did not alter AChE activity. In cells infected with the temperature-sensitive mutant, La31C, of Rous sarcoma virus (ts-RSV) and transferred to the nonpermissive temperature, the A12 form of AChE was absent, but its activity could be induced following exposure of the cells to Gly-Gln. When cells treated in this way were incubated in the presence of collagenase, there was a small but significant loss of A12 AChE activity, indicating that Gly-Gln stimulated the activity of a pool of this oligomer which was mainly but not entirely intracellular. Neither Gly-Gln nor Gly-Glu influenced 125I-alpha BGT binding after exposure of the cells to the peptides for any duration. Neither Gly-Gln nor Gly-Glu influenced the accumulation of cyclic AMP in the cultures. beta-Endorphin is one of a family of peptides that coexist transiently with acetylcholine in lower motoneurones of vertebrates in the perinatal period. This report provides evidence for the selective trophic activity of one of its derivatives toward the postsynaptic cholinergic system in avian muscle cells.
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PMID:Glycyl-L-glutamine stimulates the accumulation of A12 acetylcholinesterase but not of nicotinic acetylcholine receptors in quail embryonic myotubes by a cyclic AMP-independent mechanism. 215 12

The myoepithelial-type cell line, Rama 712, derived from a normal rat mammary gland, deposits an extracellular matrix containing type-IV collagen and other basement membrane proteins round its cellular periphery. After transformation with a temperature-sensitive mutant of Rous sarcoma virus (tsRSV) the cells fail to deposit an extracellular matrix at the permissive temperature (35 degrees C), but retain the capacity to do so at the non-permissive temperature (41 degrees C). The synthesis of type-IV collagen is not affected by the temperature shift. Rama 712 cells fail to form tumours in syngeneic rats. However, Rama 712-tsRSV cells form tumours that are locally invasive but fail to metastasize. In histological sections, the tumour cells stain with an antibody to type-IV collagen, but do not deposit any extracellular type-IV collagen. Cells isolated from the tumours (Rama 712T) remain temperature-sensitive for the extracellular deposition of type-IV collagen when grown in vitro. Rama 712, Rama 712-tsRSV and Rama 712T fail to produce any detectable type-I or type-IV collagenase at either 35 degrees C or 41 degrees C. These results show that in this system extracellular deposits of basement membrane proteins are lost from invasive tumours produced by myoepithelial-type cells by mechanisms other than those due to the production of collagenolytic enzymes.
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PMID:Loss of basement membrane deposits and development of invasive potential by virally-transformed rat mammary cells are independent of collagenase production. 303 59

The extracellular matrix of cultured chicken embryo fibroblasts undergoes a number of modifications during the early stages of oncogenic transformation. One alteration is increased production of a small protein (Mr approximately 21,000) which is transiently deposited in the matrix by transforming cells infected with LA24, a temperature-sensitive mutant of Rous sarcoma virus (RSV) (Blenis, J., and Hawkes, S.P. (1983) Proc. Natl. Acad. Sci. U.S.A. 80, 770-774). This protein is a major component of substratum-associated material (material which remains attached to culture dishes after removal of cells with ethylene glycol bis(beta-aminoethyl ether)-N,N,N',N'-tetraacetic acid). Its synthesis is stimulated by transformation of cells with NY68, another ts mutant of RSV, and also by treatment of normal, uninfected cells with the tumor promoter, phorbol myristate acetate. Accessibility of the 21-kDa protein to lactoperoxidase-catalyzed iodination indicates an exposed location within the matrix. The protein binds strongly to the culture dish and/or other matrix components. This interaction can be disrupted by sodium dodecyl sulfate but not by several nonionic detergents, unless beta-mercaptoethanol or KCl (0.5 M) are also present. High concentrations of urea or guanidine hydrochloride also remove the protein from the matrix. The 21-kDa protein is resistant to trypsin, collagenase, and the hydrolytic enzymes associated with cells transformed by the wild-type Prague A RSV but not to Pronase or chymotrypsin. A 21-kDa protein with properties similar to those described above is also detected in the medium and binds to the matrix, suggesting that a potential route of deposition of the 21-kDa protein in the matrix may be via shedding and subsequent interaction with other matrix components.
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PMID:Characterization of a transformation-sensitive protein in the extracellular matrix of chicken embryo fibroblasts. 643 99

Degradation (turnover) of collagenous matrix occurs on the surface of specialized membrane extensions termed "invadopodia," which are sites of cell invasion into the extracellular matrix. Here we show the localization of the M(r) 72,000 type IV collagenase of the matrix metalloproteinase family at invadopodia. When added exogenously, latent M(r) 72,000 collagenase binds to invadopodia of chicken embryo fibroblasts transformed by Rous sarcoma virus, whereupon the bound collagenase loses its propeptide. The collagenase binds to a component contained within the detergent extract of transformed cells, and increased levels of the active M(r) 62,000 form of the collagenase are seen here. Such an association is not detected in the detergent extract derived from normal cells. Using a recently developed cell fractionation procedure to collect cell surfaces enriched in invadopodia, we show that the M(r) 72,000 collagenase associates with the invadopodial fraction and active forms of the enzyme become immobilized on the collagenous surface. Thus, invadopodia direct intense localized degradation of the extracellular matrix by concentrating active membrane-associated collagenases at sites of cellular invasion.
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PMID:Binding and localization of M(r) 72,000 matrix metalloproteinase at cell surface invadopodia. 839 88

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