C-telopeptide

Refer ence values of bone turnover markers (BTMs) are determined by factors that are country-specific. In Sri Lanka, unavailability of BTM reference data has led to their non-use in management of osteoporosis. The results of this study can be used as reference data for women in Sri Lanka.Introduction:This study was performed to establish age-related reference intervals for bone resorption marker; cross-linked C-telopeptide of type I collagen (CTX) and bone formation marker; procollagen type I N-propeptide (PINP) in a group of Sri Lankan adult women.Methods:Adult women (n = 347) aged 20-70 years were recruited using age-stratified random sampling technique and categorized into age groups by decades. Serum CTX and PINP concentration were measured using enzyme-linked immunosorbent assay (ELISA). The geometric mean (95% confidence interval) and 2.5th and 97.5th percentiles were calculated. ANOVA was used to compare the means between groups.Results:Mean CTX levels were relatively low and remained unchanged between 20 and 49 years. After the age of 49 years, mean CTXconcentration elevated significantly until the age of 70 years (43%, p < 0.001). Mean PINP concentrations were not significantly different between age categories (p > 0.05). Reference intervals of CTX and PINP were based on 2.5th and 97.5th percentile values. Reference intervals of CTX for the age groups of 20-29, 30-39, 40-49, 50-59, and 60-70 years were 0.19-0.97 ng/mL, 0.18-0.95 ng/mL, 0.20-1.29 ng/mL, 0.17-2.20 ng/mL, and 0.17-2.85 ng/mL respectively. Reference intervals of PINP for the same age groups were 118-810 pg/mL, 119-772 pg/mL, 116-645 pg/mL, 108-684 pg/mL, and 108-715 pg/mL respectively.Conclusion:In Sri Lanka, bone turnover markers are not used in evaluating patients mainly due to lack of normative data. These values can be used as reference data for women in this age group.

Introduction:Investigations in rodents as well as in vitro experiments have suggested an anabolic influence of specific collagen peptides (SCP) on bone formation and bone mineral density (BMD). The goal of the study was to investigate the effect of 12-month daily oral administration of 5 g SCP vs. placebo (CG: control group) on BMD in postmenopausal women with primary, age-related reduction in BMD.Methods:131 women were enrolled in this randomized, placebo-controlled double-blinded investigation. The primary endpoint was the change in BMD of the femoral neck and the spine after 12 months. In addition, plasma levels of bone markers-amino-terminal propeptide of type I collagen (P1NP) and C-telopeptide of type I collagen (CTX 1)-were analysed.Results:A total of 102 women completed the study, but all subjects were included in the intention-to-treat (ITT) analysis (age 64.3 ± 7.2 years; Body Mass Index, BMI 23.6 ± 3.6 kg/m²; T-score spine -2.4 ± 0.6; T-score femoral neck -1.4 ± 0.5). In the SCP group (n= 66), BMD of the spine and of the femoral neck increased significantly compared to the control group (n= 65) (T-score spine: SCP +0.1 ± 0.26; CG -0.03 ± 0.18; ANCOVAp= 0.030; T-score femoral neck: SCP +0.09 ± 0.24; CG -0.01 ± 0.19; ANCOVAp= 0.003). P1NP increased significantly in the SCP group (p= 0.007), whereas CTX 1 increased significantly in the control group (p= 0.011).Conclusions:These data demonstrate that the intake of SCP increased BMD in postmenopausal women with primary, age-related reduction of BMD. In addition, SCP supplementation was associated with a favorable shift in bone markers, indicating increased bone formation and reduced bone degradation.

The amino (N-telo) and carboxyl (C-telo) telopeptides of type I collagen play crucial roles, in vivo and in vitro, in the assembly of collagen fibrils, regulating the axial alignment of the molecules within a fibril, azimuthal orientations of neighboring molecules, and cross-link formation. High-resolution structures of the telopeptides are not available from X-ray diffraction studies, but computational methods permitted prediction of the N-telo structure within a fibril. Here, using a suite of molecular modeling software, the more complex heterotrimeric C-telo of human type I collagen has been built from the correct sequences and energy minimized and the energy minimum confirmed by molecular dynamics. The receptor triple helix was modeled on the basis of the Protein Data Bank coordinates of a collagen-like sequence. Docking of the heterotrimeric C-telopeptide to its receptor showed that hydrophobic interactions involving the short alpha2 C-telopeptide are crucial determinants of its azimuthal orientation within the docked structure. A docked C-telo can interact with only one neighboring helix. The two alpha1(I) C-telo chains in the alpha1(Alpha)-alpha2-alpha1(B) chain stagger do not have identical docked conformations, and one of the alpha1(I) C-telo chains appears to be favored for formation of a cross-link between its K(16C) and a helix K87. Prior studies showed that a docked N-telopeptide can interact with two adjacent collagen monomers, forming a tightly packed region. A recent X-ray analysis showed the N- and C-telo regions pack differently, with the C-telo region being less densely packed than N-telo regions. This difference between N- and C-telopeptide docked structures demonstrates how unique and specific packing can occur in the fibril at each boundary of the type I collagen gap region.