Hw. Lehmann et al., HYDROXYLATION OF COLLAGEN TYPE-I - EVIDENCE THAT BOTH LYSYL AND PROLYL RESIDUES ARE OVERHYDROXYLATED IN OSTEOGENESIS IMPERFECTA, European journal of clinical investigation, 25(5), 1995, pp. 306-310
Citations number
17
Categorie Soggetti
Medicine, Research & Experimental","Medicine, General & Internal
The composition of the collagens secreted into the media of fibroblast
cultures of 39 patients with osteogenesis imperfecta (OI) was the sam
e in controls and OI cultures. An abnormal migration pattern of collag
ens upon SDS-PAGE was evident in one third of the cultures investigate
d. Lysyl and prolyl hydroxylation of HPLC-purified alpha 1(I) chains w
as elevated in about 60% of cultures. The degree of hydroxylation was
highest in the lethal forms. The extent of lysyl and prolyl hydroxylat
ion showed a strong correlation (r = 0.74, P < 0.001). While high leve
ls of hydroxylation are frequently observed in OI patients, a direct c
orrelation between lysyl of prolyl hydroxylation and fracture rate or
growth retardation could not be established.