Collagen synthesis regulation by the aminopropeptide of procollagen I in normal and scleroderma fibroblasts.
The effect of the aminopropeptide of type I procollagen, Col 1(I), on collagen synthesis by normal and scleroderma fibroblasts was investigated. Collagen synthesis was inhibited by about 42% when normal fibroblasts were labeled with 3H-proline in the presence of 4 microM Col 1(I). In contrast, collagen synthesis by scleroderma fibroblasts was inhibited to a lesser degree, about 19%. Furthermore, scleroderma fibroblasts with elevated rates of collagen synthesis (2.5-5 times normal) were inhibited by only about 10%. The data suggest that the increased accumulation of collagen in the skin of scleroderma patients may be related to a defect in the regulation of collagen synthesis by the aminopropeptide.
D000328:Adult; D000368:Aged; D002478:Cells, Cultured; D005260:Female; D005347:Fibroblasts / Q000378:metabolism; D006801:Humans; D008875:Middle Aged; D010446:Peptide Fragments / Q000502:physiology*; D011347:Procollagen / Q000096:biosynthesis* / Q000502:physiology*; D012595:Scleroderma, Systemic / Q000378:metabolism*
D010446:Peptide Fragments; D011347:Procollagen; C041876:procollagen Type III-N-terminal peptide