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Research Article Free access | 10.1172/JCI105957

The quantitative relationship of urinary peptide hydroxyproline excretion to collagen degradation

Phillip H. Weiss and LeRoy Klein

1Division of Orthopaedic Surgery, Department of Surgery, Case Western Reserve University School of Medicine, Cleveland, Ohio 44106

*

This work was done in partial fulfillment of the requirement for the degree of Doctor of Medicine, Case Western Reserve University School of Medicine, Cleveland, Ohio 44106.

Find articles by Weiss, P. in: PubMed | Google Scholar

1Division of Orthopaedic Surgery, Department of Surgery, Case Western Reserve University School of Medicine, Cleveland, Ohio 44106

*

This work was done in partial fulfillment of the requirement for the degree of Doctor of Medicine, Case Western Reserve University School of Medicine, Cleveland, Ohio 44106.

Find articles by Klein, L. in: PubMed | Google Scholar

Published January 1, 1969 - More info

Published in Volume 48, Issue 1 on January 1, 1969
J Clin Invest. 1969;48(1):1–10. https://doi.org/10.1172/JCI105957.
© 1969 The American Society for Clinical Investigation
Published January 1, 1969 - Version history
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Abstract

To determine the quantitative relationship of urinary hydroxyproline peptide excretion to collagen breakdown, known quantities of radioactive hydroxyproline peptides were administered to unlabeled animals and excertion of radioactivity in respiratory carbon dioxide, urine, and feces was measured. The major routes of excretion of collagen peptide metabolites were respiratory carbon dioxide (75%) and urine, as hydroxyproline-containing peptides (25%).

Since the predominant urine hydroxyproline peptide linkage is proly-hydroxyproline, L-prolyl-L-hydroxyproline-3H was administered to unlabeled animals. Greater than 80% of the administered dipeptide was excreted in urine, suggesting that this peptide linkage is not hydrolyzed to a significant extent in vivo.

These data suggest that urinary hydroxyproline excretion is a “fairly” sensitive indicator of collagen breakdown and can be used at the clinical level to quantitate changes in collagen breakdown.

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