Hydroxylation of collagen by lungs of rats administered bleomycin.

Jerold A Last; J. E. Gerriets; L. C. Armstrong; T. R. Gelzleichter; K. M. Reiser

Hydroxylation of collagen by lungs of rats administered bleomycin.

Jerold A Last, J. E. Gerriets, L. C. Armstrong, T. R. Gelzleichter, K. M. Reiser

Pulmonary, Critical Care, and Sleep Medicine

Research output: Contribution to journal › Article › peer-review

8 Scopus citations

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

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title = "Hydroxylation of collagen by lungs of rats administered bleomycin.",

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.",

author = "Last, {Jerold A} and Gerriets, {J. E.} and Armstrong, {L. C.} and Gelzleichter, {T. R.} and Reiser, {K. M.}",

year = "1990",

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journal = "American Journal of Respiratory Cell and Molecular Biology",

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T1 - Hydroxylation of collagen by lungs of rats administered bleomycin.

AU - Last, Jerold A

AU - Gerriets, J. E.

AU - Armstrong, L. C.

AU - Gelzleichter, T. R.

AU - Reiser, K. M.

PY - 1990/6

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N2 - 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.

AB - 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.

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