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Volume 272, Number 15, Issue of April 11, 1997 pp. 9755-9763
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

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Characterization of Urinary Degradation Products Derived from Type I Collagen
IDENTIFICATION OF A -ISOMERIZED ASP-GLY SEQUENCE WITHIN THE C-TERMINAL TELOPEPTIDE (1) REGION

(Received for publication, May 23, 1996, and in revised form, January 28, 1997)

Christian Fledelius , Anders H. Johnsen ^¶ , Paul A. C. Cloos , Martin Bonde and Per Qvist

From the  Osteometer BioTech A/S, Herlev Hovedgade 207, DK-2730 Herlev, Denmark and the ^¶ Department of Clinical Biochemistry, Rigshospitalet, University of Copenhagen, Blegdamsvej 9, DK-2100, Copenhagen, Denmark

The heterogeneity of urinary degradation products of C-terminal telopeptides derived from the 1 chain of human type I collagen was investigated and characterized. The urinary fragments characterized in this study consisted of two cross-linked (X) amino acid sequences derived from the C-terminal telopeptide (1) of type I collagen. Fragments containing the sequence EXAHDGGR, with a DG site being either nonisomerized (Asp-Gly) or -isomerized (Asp-Gly), were identified. Pyridinoline was detected among the pyridinium cross-links, but there was a dominance of deoxypyridinoline and a cross-link containing pyridinoline having a molecular weight identical with that of galactosyl pyridinoline. A nonfluorescent cross-link was also found. The concentration of fragments derived from the C-terminal telopeptide region of type I collagen containing the sequence Asp-Gly (CTX) and/or Asp-Gly (CTX) was measured by enzyme-linked immunosorbent assays in urine and in collagenase digests of trabecular and cortical bone of young and old origin. It was shown that the urinary ratio between such fragments, CTX/CTX, was higher in children compared with adults and that the ratio decreased with increasing age of bone. The results indicated that the C-terminal telopeptide fragments derived from type I collagen excreted into urine originated mainly from bone. In conclusion, it is demonstrated for the first time that the C-terminal telopeptide 1 chain of type I collagen contains an Asp-Gly site prone to undergo -isomerization and that the degree of -isomerization of this linkage apparently increases with increasing age of bone. These findings indicate that the ratio CTX/CTX might be clinically important in diagnosing metabolic bone diseases.

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