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Studies on collagen metabolism in the Marfan syndrome
Author(s) -
MÜLLER K. P.,
NERLICH A. G.,
KUNZE D.,
MÜLLER P. K.
Publication year - 1987
Publication title -
european journal of clinical investigation
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.164
H-Index - 107
eISSN - 1365-2362
pISSN - 0014-2972
DOI - 10.1111/j.1365-2362.1987.tb01239.x
Subject(s) - hydroxylation , marfan syndrome , metabolism , chemistry , biochemistry , fibroblast , medicine , enzyme , in vitro
. The pattern of collagen metabolism was studied in nine fibroblast cultures from Marfan patients. The cellular synthesis of collagen and non‐collageneous 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), a2(I) and al(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.