Measurements of urinary nonisomerized form of type I collagen degradation products (α-CTx) in aging, menopause, and osteoporosis with fractures

1999 ◽  
Vol 279 (1-2) ◽  
pp. 69-76 ◽  
Author(s):  
Masaaki Takahashi ◽  
Hironobu Hoshino ◽  
Kazuhiro Kushida
1994 ◽  
Vol 40 (11) ◽  
pp. 2022-2025 ◽  
Author(s):  
M Bonde ◽  
P Qvist ◽  
C Fledelius ◽  
B J Riis ◽  
C Christiansen

Abstract An enzyme-linked immunosorbent assay (ELISA) for measuring type I collagen degradation products in urine < 3 h was evaluated. The measuring range was 0.5-10.5 mg/L with a detection limit of 0.2 mg/L. Within-run and total CVs were 5.3% and 6.6%, respectively. Analytical recovery averaged 100%. The mean (+/- SD) concentrations in urine samples from a healthy premenopausal population (n = 102) were 250 +/- 110 mg/mol creatinine (Cr). A group of healthy postmenopausal women (n = 410) gave a mean value of 416 +/- 189 mg/mol Cr. Values obtained in the ELISA correlated well (r = 0.83) to HPLC values for the established bone resorption marker deoxypyridinoline (n = 214), slightly better than the correlation to hydroxyproline measurements (r = 0.78, n = 421). We conclude that the assay described here presents a useful tool for further elucidating the importance of type I collagen degradation products in urine.


2005 ◽  
Vol 24 (1) ◽  
pp. 63-70 ◽  
Author(s):  
M. Fichter ◽  
U. Körner ◽  
J. Schömburg ◽  
L. Jennings ◽  
A. A. Cole ◽  
...  

1973 ◽  
Vol 12 (1) ◽  
pp. 303-312 ◽  
Author(s):  
Yoshinori Kuboki ◽  
Hitoyata Shimokawa ◽  
Toshio Ono ◽  
Satoshi Sasaki

Bone ◽  
1989 ◽  
Vol 10 (6) ◽  
pp. 471 ◽  
Author(s):  
BM Thomson ◽  
SJ Atkinson ◽  
AM McGarrity ◽  
RM Hembry ◽  
JJ Reynolds ◽  
...  

1987 ◽  
Vol 87 (2) ◽  
pp. 357-362
Author(s):  
J. Gavrilovic ◽  
R.M. Hembry ◽  
J.J. Reynolds ◽  
G. Murphy

A specific antiserum to purified rabbit tissue inhibitor of metalloproteinases (TIMP) was raised in sheep, characterized and used to investigate the role of TIMP in a model system. Chondrocytes and endothelial cells cultured on 14C-labelled type I collagen films and stimulated to produce collagenase were unable to degrade the films unless the anti-TIMP antibody was added. The degradation induced was inhibited by a specific anti-rabbit collagenase antibody. It was concluded that TIMP is a major regulatory factor in cell-mediated collagen degradation.


2003 ◽  
Vol 77 (2) ◽  
pp. 197-203 ◽  
Author(s):  
A. Liesegang ◽  
M.-L. Sassi ◽  
J. Risteli

AbstractTwelve 6-month-old growing female goats and sheep were used in this study. Blood samples were obtained in the morning before goats and sheep were given food and then at 2-h intervals for 24 h (part I). This procedure was repeated 2 weeks later (part II). Concentrations of osteocalcin (OC), activities of total (tAP) and bone-specific alkaline phosphatase (bAP), degradation products of C-terminal telopeptide of type-I collagen (CrossLaps™ CL), and carboxyterminal telopeptide of type-I collagen (ICTP) were measured in serum.In both parts of the study, all bone marker concentrations were significantly higher in goats than in sheep. The OC concentrations in goats increased in the late afternoon/evening and decreased thereafter to reach values similar to those obtained at the beginning. The ICTP concentrations in goats slowly decreased until 14:00 h, increased, and decreased again. The concentrations in sheep decreased continuously but not significantly, towards the morning sampling. The CL concentrations increased in both sheep and goats during the night but at 06:00 h started to decrease to levels found at the beginning of testing. The bAP activities decreased in goats from 20:00 to 22:00 h. Changes in the concentrations of bone markers were mainly observed in goats of this study. As documented for bone resorption and formation in other species, circadian rhythms were evident for concentrations of ICTP, CL, bAP and OC. The present study indicates that growing goats may have a physiologically higher bone turn-over than growing sheep, because the bone marker concentrations were always higher.


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