6533b860fe1ef96bd12c3a4c

RESEARCH PRODUCT

Hydroxylation of collagen type I: evidence that both lysyl and prolyl residues are overhydroxylated in osteogenesis imperfecta

Peter K. MüllerRolf E. BrennerD. RimekH. LehmannM. BodoU. VetterO. WörsdorferA. Karbowski

subject

AdultMaleAdolescentProlineClinical BiochemistryAlpha (ethology)Fibroblast culturesHydroxylationHydroxylysineBiochemistryHydroxylationFractures Bonechemistry.chemical_compoundHydroxyprolinePregnancymedicineHumansChildCells CulturedCollagen typeGrowth retardationLysineInfantGeneral MedicineFibroblastsMiddle AgedOsteogenesis Imperfectamedicine.diseaseMolecular biologyBody HeightHydroxyprolineHydroxylysinePhenotypechemistryBiochemistryOsteogenesis imperfectaChild PreschoolFemaleCollagen

description

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 alpha 1(I) 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.

yearjournalcountryeditionlanguage
1995-05-01European Journal of Clinical Investigation
https://doi.org/10.1111/j.1365-2362.1995.tb01706.x