Studies on collagen metabolism in the Marfan syndrome.
The pattern of collagen metabolism was studied in nine fibroblast cultures from Marfan patients. The cellular synthesis of collagen and non-collagenous proteins was significantly increased, whereas secretion and degradation remained unchanged. Other steps of post-translational processing such as hydroxylation of prolyl or lysyl residues, affecting triple helix stability, were found to be normal. Furthermore, peptide mapping of isolated a 1(I), a 2(I) and a 1(III) gave no evidence for structural defects. Hence, our study would support the notion that defects other than those affecting collagen type I or III metabolism must represent the molecular basis of the Marfan syndrome.
D000293:Adolescent; D000328:Adult; D000596:Amino Acids / Q000032:analysis; D002478:Cells, Cultured; D002648:Child; D003094:Collagen / Q000302:isolation & purification / Q000378:metabolism*; D005260:Female; D005347:Fibroblasts / Q000378:metabolism; D006801:Humans; D006909:Hydroxyproline / Q000378:metabolism; D008297:Male; D008382:Marfan Syndrome / Q000378:metabolism*; D010446:Peptide Fragments / Q000302:isolation & purification; D011392:Proline / Q000378:metabolism; D011487:Protein Conformation; D011499:Protein Processing, Post-Translational
D000596:Amino Acids; D010446:Peptide Fragments; D003094:Collagen; D011392:Proline; D006909:Hydroxyproline