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Hydroxylation of collagen type I: evidence that both lysyl and prolyl residues are overhydroxylated in osteogenesis imperfecta
Author(s) -
LEHMANN H. W.,
RIMEK D.,
BODO M.,
BRENNER R. E.,
VETTER U.,
WÖRSDÖRFER O.,
KARBOWSKI A.,
MÜLLER P. K.
Publication year - 1995
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.1365-2362.1995.tb01706.x
Subject(s) - hydroxylation , osteogenesis imperfecta , chemistry , type i collagen , hydroxyproline , biochemistry , lysine , endocrinology , medicine , biology , enzyme , amino acid , anatomy
. The composition of the collagens secreted into the media of fibroblast cultures of 39 patients with osteogenesis imperfecta (OI) was the same in controls and OI cultures. An abnormal migration pattern of collagens upon SDS‐PAGE was evident in one third of the cultures investigated. Lysyl and prolyl hydroxylation of HPLC‐purified α 1(1) chains was elevated in about 60% of cultures. The degree of hydroxylation was highest in the lethal forms. The extent of lysyl and prolyl hydroxylation showed a strong correlation ( r = 0.74, P < 0.001). While high levels of hydroxylation are frequently observed in OI patients, a direct correlation between lysyl or prolyl hydroxylation and fracture rate or growth retardation could not be established.