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Investigation of bone disease using isomerized and racemized fragments of type I collagen.
Calcif Tissue Int. 2003 Jan; 72(1):8-17.CT

Abstract

In the collagen type I C-telopeptide an aspartyl-glycine site within the sequence AHDGGR is susceptible to molecular rearrangement. In newly synthesized collagen this site is in the native form, denoted alpha L. During aging a spontaneous reaction occurs resulting in three age-modified forms: an isomerized form (beta L) a racemized form (alpha D), and an isomerized/racemized form (beta D). In this study, we measured the urinary excretion of the four forms of C-telopeptides (CTX) in healthy adults and in patients with bone diseases. Levels of all CTX forms were higher in healthy postmenopausal women (P<0.001) compared with premenopausal controls. Levels decreased within 3 days of bisphosphonate treatment indicating that all CTX forms reflect bone resorption. In hyperthyroidism, characterized by a generalized increased bone turnover, native (alpha L) and age-modified (beta L, alpha D and beta D) forms increased to a similar extent compared to controls, resulting in normal ratios between the alpha L and age-modified forms of CTX. Conversely, in Paget's disease and prostate cancer-induced bone metastases, conditions characterized by focal increased bone turnover, alpha L CTX levels were more elevated than those of age-related CTX forms, resulting in increased ratios between native and age-modified CTX. For example, the ratio alpha L/alpha D was increased 7-fold in Paget's disease (P<0.001) and 2-fold in prostate cancer-induced bone metastases (P<0.002). In conclusion, the study suggests that in conditions with a localized alteration in bone turnover the ratio between alpha L CTX and the age-modified forms is significantly elevated. This may provide a new diagnostic and monitoring tool for diseases such as metastatic bone cancer and Paget's disease.

Authors+Show Affiliations

Nordic Bioscience A/S, Herlev Hovedgade 207, DK-2730 Herlev, Denmark. PC@nordicbioscience.comNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article

Language

eng

PubMed ID

12384813

Citation

Cloos, P A C., et al. "Investigation of Bone Disease Using Isomerized and Racemized Fragments of Type I Collagen." Calcified Tissue International, vol. 72, no. 1, 2003, pp. 8-17.
Cloos PA, Fledelius C, Christgau S, et al. Investigation of bone disease using isomerized and racemized fragments of type I collagen. Calcif Tissue Int. 2003;72(1):8-17.
Cloos, P. A., Fledelius, C., Christgau, S., Christiansen, C., Engsig, M., Delmas, P., Body, J. J., & Garnero, P. (2003). Investigation of bone disease using isomerized and racemized fragments of type I collagen. Calcified Tissue International, 72(1), 8-17.
Cloos PA, et al. Investigation of Bone Disease Using Isomerized and Racemized Fragments of Type I Collagen. Calcif Tissue Int. 2003;72(1):8-17. PubMed PMID: 12384813.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Investigation of bone disease using isomerized and racemized fragments of type I collagen. AU - Cloos,P A C, AU - Fledelius,C, AU - Christgau,S, AU - Christiansen,C, AU - Engsig,M, AU - Delmas,P, AU - Body,J-J, AU - Garnero,P, Y1 - 2002/10/21/ PY - 2002/03/06/received PY - 2002/06/27/accepted PY - 2002/10/18/pubmed PY - 2003/12/13/medline PY - 2002/10/18/entrez SP - 8 EP - 17 JF - Calcified tissue international JO - Calcif Tissue Int VL - 72 IS - 1 N2 - In the collagen type I C-telopeptide an aspartyl-glycine site within the sequence AHDGGR is susceptible to molecular rearrangement. In newly synthesized collagen this site is in the native form, denoted alpha L. During aging a spontaneous reaction occurs resulting in three age-modified forms: an isomerized form (beta L) a racemized form (alpha D), and an isomerized/racemized form (beta D). In this study, we measured the urinary excretion of the four forms of C-telopeptides (CTX) in healthy adults and in patients with bone diseases. Levels of all CTX forms were higher in healthy postmenopausal women (P<0.001) compared with premenopausal controls. Levels decreased within 3 days of bisphosphonate treatment indicating that all CTX forms reflect bone resorption. In hyperthyroidism, characterized by a generalized increased bone turnover, native (alpha L) and age-modified (beta L, alpha D and beta D) forms increased to a similar extent compared to controls, resulting in normal ratios between the alpha L and age-modified forms of CTX. Conversely, in Paget's disease and prostate cancer-induced bone metastases, conditions characterized by focal increased bone turnover, alpha L CTX levels were more elevated than those of age-related CTX forms, resulting in increased ratios between native and age-modified CTX. For example, the ratio alpha L/alpha D was increased 7-fold in Paget's disease (P<0.001) and 2-fold in prostate cancer-induced bone metastases (P<0.002). In conclusion, the study suggests that in conditions with a localized alteration in bone turnover the ratio between alpha L CTX and the age-modified forms is significantly elevated. This may provide a new diagnostic and monitoring tool for diseases such as metastatic bone cancer and Paget's disease. SN - 0171-967X UR - https://www.unboundmedicine.com/medline/citation/12384813/Investigation_of_bone_disease_using_isomerized_and_racemized_fragments_of_type_I_collagen_ L2 - https://dx.doi.org/10.1007/s00223-002-2034-1 DB - PRIME DP - Unbound Medicine ER -