Publications

Abstract BACKGROUND Bone biochemical markers have been used in dynamic studies of bone metabolism, and, for accurate interpretation of measured marker levels, it is essential to have information of extra-skeletal metabolism. Therefore, the objective of the present study was to investigate if the circulating C-telopeptides of type I collagen (CTX) was subject to hepatic extraction. […]

Abstract BACKGROUND Control of pre-analytical variables is essential for successful application of biological markers, including bone resorption markers, in clinical trials and routine use. The effect of storage temperature on stability of bone resorption markers have not been subject of systematically investigation, and therefore the present study was set out to determine the stability of […]

Abstract OBJECTIVE Glucosamine sulphate has been shown in a large double-blind, placebo-controlled clinical trial to prevent structural damage and improve clinical symptoms of osteoarthritis (OA). We investigated whether early response in a newly developed biochemical marker of collagen type II degradation (CTX-II, CartiLaps ELISA) could reflect the long-term preservation of hyaline cartilage. METHODS Study subjects […]

Abstract We have previously shown that a subcutaneous injection of glucagon-like peptide-2 (GLP-2) at 9 a.m. in fasting postmenopausal women results in a dose-dependent decrease in the serum concentration of fragments derived from the degradation of the C-terminal telopeptide region of collagen type I (s-CTX), a marker of bone resorption. In contrast, GLP-2 was found […]

Abstract UNLABELLED Collagen type I fragments, reflecting bone resorption, and release of gut hormones were investigated after a meal. Investigations led to a dose escalation study with glucagon like peptide-2 (GLP-2) in postmenopausal women. We found a dose-dependent effect of GLP-2 on the reduction of bone resorption. INTRODUCTION The C-terminal telopeptide region of type I […]

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 […]

Abstract BACKGROUND Fragments of collagen type I containing the epitope AHDGGR (CTX) are generated during bone resorption. The aspartyl-glycine (DG) site within CTX is synthesised in the L-aspartyl peptide (alphaL) form, but converts to the age-modified forms L-isoaspartyl peptide (betaL) and D-aspartyl peptide (alphaD) over time. The purpose of the present study was to test […]