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Technical Briefs |
a address correspondence to this author at: Fundación Jiménez Díaz, Laboratorio de Bioquímica, Sección Metabolismo Mineral y Óseo, Avda Reyes Católicos 2, 28040 Madrid, Spain
Many fragments derived from collagen I degradation come to serum
during bone resorption. The characterization of these fragments and the
development of assays that can measure them are the basis of most of
the biochemical markers of bone resorption. One of these fragments
consists of two cross-linked amino acid sequences derived from the
C-terminal telopeptide region of type I collagen
1 chains. Fragments containing the sequence
EKAH-DGGR (CTX), with a DG site being either nonisomerized (
-CTX) or
ß-isomerized (ß-CTX) were identified. Pyridinoline,
deoxypyridinoline, and other cross-links linked both telopeptides (Fig. 1
) (1). Recent reports have suggested that the
proportions of nonisomerized and ß-isomerized fragments depend on
bone age (1).
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There are two available assays that can measure the ß-isomer form of
the CTX epitope: urinary CrossLapsTM ELISA
(2), and Serum CrossLaps One Step ELISA (3), both
from
Acknowledgments
Footnotes
References
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