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Marfan syndrome: Absence of type I or III collagen structural defects in 25 patients
Author(s) -
Harley V. R.,
Chan D.,
Rogers J. G.,
Cole W. G.
Publication year - 1990
Publication title -
journal of inherited metabolic disease
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.462
H-Index - 102
eISSN - 1573-2665
pISSN - 0141-8955
DOI - 10.1007/bf01799689
Subject(s) - cyanogen bromide , dermis , fibroblast , lysine , marfan syndrome , type i collagen , collagen, type i, alpha 1 , chemistry , biochemistry , biology , pathology , medicine , extracellular matrix , peptide sequence , amino acid , in vitro , gene
Summary The structure and metabolism of type I and III collagens were studied in fibroblast cultures and dermis from 25 unrelated patients including 23 with typical Marfan syndrome and two infants with a very severe clinical form of this syndrome. Electrophoretic analysis of collagen α‐chains, as well as one‐ and two‐dimensional electrophoresis of collagen cyanogen bromide peptides, failed to show any evidence of primary structure defects or overmodification of lysine residues in these collagens. The proportion of hydroxylated prolyl residues in isolated α1(I) chains was also normal. There was a minimal increase in the proportion of type III collagen produced by nine cultures. The findings in this study indicate that the underlying molecular defects in the patients studied are unlikely to involve the structure of the main fibrillar type I and III collagens.