Abstract
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.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 543-548 |
| Number of pages | 6 |
| Journal | American Journal of Respiratory Cell and Molecular Biology |
| Volume | 2 |
| Issue number | 6 |
| State | Published - Jun 1990 |
ASJC Scopus subject areas
- Cell Biology