Hydroxylation of collagen by lungs of rats administered bleomycin.
Collagen synthesized by tissue minces from lungs of rats administered 1 unit of bleomycin by intratracheal instillation 1 or 2 wk earlier contained relatively more hydroxylysine than did collagen made by lungs from saline-instilled control animals. Most, if not all, of the relative increase in lysine hydroxylation could be localized to the alpha 1 (I) chain of type I collagen. Lung homogenates from bleomycin-treated rats showed increased activity of lysyl hydroxylase (EC 1.14.11.4), the enzyme catalyzing the conversion of collagen-bound lysine to hydroxylysine. Thus, the increased hydroxylation of lysine and of lysine-derived cross-links previously observed in collagen of diseased human lungs and in animal models of lung fibrosis is reflected in an in vitro system.
Last
J A
JA
Department of Internal Medicine, School of Medicine, University of California, Davis.
Gerriets
J E
JE
Armstrong
L C
LC
Gelzleichter
T R
TR
Reiser
K M
KM
D000818:Animals; D001761:Bleomycin; D003094:Collagen / Q000378:metabolism*; D004305:Dose-Response Relationship, Drug; D006900:Hydroxylation; D006901:Hydroxylysine / Q000378:metabolism; D008168:Lung / Q000378:metabolism*; D008914:Minoxidil / Q000494:pharmacology; D006899:Mixed Function Oxygenases / Q000378:metabolism*; D008240:Procollagen-Lysine, 2-Oxoglutarate 5-Dioxygenase / Q000378:metabolism*; D011658:Pulmonary Fibrosis / Q000139:chemically induced / Q000378:metabolism*; D051381:Rats
D001761:Bleomycin; D006901:Hydroxylysine; D008914:Minoxidil; D003094:Collagen; D006899:Mixed Function Oxygenases; D008240:Procollagen-Lysine, 2-Oxoglutarate 5-Dioxygenase