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Open AccessJournal ArticleDOI

The effect of ascorbic acid on the nature and production of collagen and elastin by rat smooth-muscle cells.

Y A de Clerck, +1 more
- 15 Jan 1980 - 
- Vol. 186, Iss: 1, pp 217-225
TLDR
The appearance of insoluble collagen in the extracellular matrices produced by cultured human fibroblasts and calf endothelial cells was completely dependent on the presence of ascorbic acid and had variable effects on the quantity of glycoprotein(s) present in the matrix.
Abstract
1 The effects of various concentrations of ascorbic acid on the quality and quantity of the insoluble extracellular matrices produced by two strains of cultured rat smooth-muscle cells were studied 2 Ascorbic acid was necessary for the appearance of insoluble collagen in the extracellular matrix 3 Secretion of soluble collagen continued in the absence of ascorbic acid, but this soluble collagen was markedly underhydroxylated 4 The amount of insoluble collagen present in the matrix was directly related to the ascorbic acid concentration 5 The insoluble collagen that appeared in the matrix under conditions where ascorbic acid was limiting was no more than 7% underhydroxylated 6 In contrast, the amount of insoluble elastin produced was inversely proportional to the ascorbic acid concentration 7 The elastin produced in the absence of ascorbic acid had the expected amino acid composition, but hydroxyproline was absent 8 The hydroxyproline content of elastin was also directly dependent on the ascorbic acid concentration 9 Ascorbic acid had variable effects on the quantity of glycoprotein(s) present in the matrix 10 The appearance of insoluble collagen in the extracellular matrices produced by cultured human fibroblasts and calf endothelial cells was also completely dependent on the presence of ascorbic acid

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Citations
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The Biochemical Functions of Ascorbic Acid

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Regulation of collagen synthesis by ascorbic acid.

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Differentiation of axon-related Schwann cells in vitro. I. Ascorbic acid regulates basal lamina assembly and myelin formation

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Degradation of connective tissue matrices by macrophages. I. Proteolysis of elastin, glycoproteins, and collagen by proteinases isolated from macrophages.

TL;DR: The data indicate that macrophages at inflammatory sites contain and secrete proteolytic enzymes that could degrade the extracellular matrix, and human granulocyte elastase effectively degraded the matrix glycoproteins, elastin, and, to a lesser extent, collagens.
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Destruction of Extracellular Matrices Containing Glycoproteins, Elastin, and Collagen by Metastatic Human Tumor Cells

TL;DR: These quantitative studies, in which tumor cells were grown in contact with a complex extracellular matrix possessing some of the characteristics of connective tissue, should have a bearing on tumor cell invasion.
References
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Journal ArticleDOI

Modified procedure for the assay of H3- or C14-labeled hydroxyproline

TL;DR: Although the present procedure measures total radioactive hydroxyproline rather than the specific radioactivity of hydroxy Proline, it is more readily applicable to samples from a variety of sources.
Journal ArticleDOI

Independent regulation of collagen types by chondrocytes during the loss of differentiated function in culture

TL;DR: The results suggest independent regulation of X 2 Y in this situation and suggest the loss of differentiated function by these chondrocyte progeny is indicated.
Journal ArticleDOI

The thermal transition of a non-hydroxylated form of collagen. Evidence for a role for hydroxyproline in stabilizing the triple-helix of collagen

TL;DR: The results suggest that hydroxylated proline increases the thermal stability of collagen.
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Aggregation of Cartilage Proteoglycans: III. CHARACTERISTICS OF THE PROTEINS ISOLATED FROM TRYPSIN DIGESTS OF AGGREGATES

TL;DR: Experiments with aggregate preparations reconstituted from mixtures with [3H]acetylated or unlabeled proteoglycans showed that the larger protein fraction is derived from a portion of the protein in the proteoglycan monomer molecules while the smaller isderived from one of the small molecular weight "link proteins" that are present in proteogly can aggregate preparations.
Journal ArticleDOI

Cross-linking of collagen.

TL;DR: The formation of collagen cross-links is attributable to the presence of two aldehyde-containing amino acids which react with other amino acids in collagen to generate difunctional, trifunctionals, and tetrafunctional cross- links.
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