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Research Article Free access | 10.1172/JCI105524
Department of Medicine, Washington University School of Medicine and the Jewish Hospital of St. Louis, St. Louis, Mo.
Department of Medicine, University of Pennsylvania and the Philadelphia General Hospital, Philadelphia, Pa.
Department of Biochemistry, University of Pennsylvania and the Philadelphia General Hospital, Philadelphia, Pa.
†Career Research Development awardee of the National Institute of General Medical Sciences (6-K3-GM-22, 676-O1A1).
Address requests for reprints to Dr. Louis V. Avioli, Jewish Hospital, 216 S. Kingshighway, St. Louis, Mo. 63110.
*Submitted for publication June 30, 1966; accepted October 20, 1966.
Supported in part by U. S. Public Health Service grants 06404 and FR-00107 from the National Institutes of Health and by Atomic Energy Commission contract AT(30-1)-3174. A preliminary report of this work has been presented (1).
Find articles by Avioli, L. in: JCI | PubMed | Google Scholar
Department of Medicine, Washington University School of Medicine and the Jewish Hospital of St. Louis, St. Louis, Mo.
Department of Medicine, University of Pennsylvania and the Philadelphia General Hospital, Philadelphia, Pa.
Department of Biochemistry, University of Pennsylvania and the Philadelphia General Hospital, Philadelphia, Pa.
†Career Research Development awardee of the National Institute of General Medical Sciences (6-K3-GM-22, 676-O1A1).
Address requests for reprints to Dr. Louis V. Avioli, Jewish Hospital, 216 S. Kingshighway, St. Louis, Mo. 63110.
*Submitted for publication June 30, 1966; accepted October 20, 1966.
Supported in part by U. S. Public Health Service grants 06404 and FR-00107 from the National Institutes of Health and by Atomic Energy Commission contract AT(30-1)-3174. A preliminary report of this work has been presented (1).
Find articles by Prockop, D. in: JCI | PubMed | Google Scholar
Published February 1, 1967 - More info
Proline-14C was administered to five adult rhesus monkeys, and the degradation of collagen was followed by the excretion of hydroxyproline-14C. The results suggested the presence of at least three separate pools of collagen with half-lives of 1 to 2, 2 to 3, and 50 to 70 days. The monkeys were killed after 44 days; at that time the specific activity of the hydroxyproline-14C in urine was found to be four to five times that of the hydroxyproline in soluble collagen and 81 to 93% that of hydroxyproline in insoluble collagen. The relationships between urinary hydroxyproline and the degradation of collagen were similar to those previously demonstrated in rats.
Parathyroid hormone was administered daily to two of the monkeys from the 27th to the 44th day of the study. The parathyroid hormone increased the amount of hydroxyproline-14C excreted, but there was no significant change in the specific activity of the urinary hydroxyproline-14C. Since under the conditions of the experiment insoluble collagen was the only possible source of hydroxyproline-14C of relatively high specific activity, the results indicated that parathyroid hormone directly or indirectly increased the degradation of insoluble collagen. The results also suggested that parathyroid hormone increased the degradation of soluble collagen, but the relative magnitude of this effect was not clearly established.