Effect of streptococcal lipoteichoic acid on prolyl hydroxylase activity as related to collagen formation in mouse fibroblast monolayers

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Effect of streptococcal lipoteichoic acid on prolyl hydroxylase activity as related to collagen formation in mouse fibroblast monolayers.

Dried and wet mouse fibroblast monolayers with labeled collagenous substrate were used to study the effects of lipoteichoic acid (LTA) on cellular prolyl hydroxylase activity. LTA is a scavenger of cations, and Fe2+ is essential for prolyl hydroxylase activity. Surprisingly, addition of LTA to dried monolayers resulted in increased prolyl hydroxylase activity, whereas preincubation of Fe2+ with...

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Selective Inhibition of Collagen Prolyl 4-Hydroxylase in Human Cells.

Collagen is the most abundant protein in animals. Its overproduction is associated with fibrosis and cancer metastasis. The stability of collagen relies on post-translational modifications, the most prevalent being the hydroxylation of collagen strands by collagen prolyl 4-hydroxylases (CP4Hs). Catalysis by CP4Hs enlists an iron cofactor to convert proline residues to 4-hydroxyproline residues,...

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Reduction of collagen production in keloid fibroblast cultures by ethyl-3,4-dihydroxybenzoate. Inhibition of prolyl hydroxylase activity as a mechanism of action.

Excessive accumulation of collagen is the hallmark of several clinical conditions characterized by tissue fibrosis. Previously, 3,4-dihydroxybenzoic acid, a structural analog of alpha-ketoglutarate and ascorbate, has been shown to inhibit the activity of purified prolyl 4-hydroxylase, the enzyme catalyzing the synthesis of 4-hydroxyproline during intracellular biosynthesis of procollagen. In th...

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Binding of streptococcal lipoteichoic acid to the fatty acid binding sites on serum albumin.

The ability of the fatty acid binding sites of serum albumin to bind lipoteichoic acid of Streptococcus pyogenes was investigated. Initial studies indicated that lipoteichoic acid, but not its deacylated deprivative, protected albumin from being denatured by heat (80C for 1 h) and changed its mobility in an electrical field. Albumin covalently linked to agarose beads bound radiolabeled lipoteic...

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ژورنال

عنوان ژورنال: Infection and Immunity

سال: 1985

ISSN: 0019-9567,1098-5522

DOI: 10.1128/iai.50.3.745-752.1985