ArticleCalcified tissue international1996
Collagen type I of rat cortical and trabecular bone differs in the extent of posttranslational modifications.
Article in Calcified tissue international, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 34 citations in OpenAlex.
- Multiscale molecular profiling of pathological bone resolves sexually dimorphic control of extracellular matrix composition.Disease models & mechanisms · 2021Article
- Hierarchical analysis and multi-scale modelling of rat cortical and trabecular bone.Journal of the Royal Society, Interface · 2015Article
- Glycosylation and cross-linking in bone type I collagen.The Journal of biological chemistry · 2014Article
- Distinct characteristics of mandibular bone collagen relative to long bone collagen: relevance to clinical dentistry.BioMed research international · 2014Review
- Infrared spectroscopic assessment of the inflammation-mediated osteoporosis (IMO) model applied to rabbit bone.Journal of biological physics · 2012Article
- Lysyl hydroxylase 3-mediated glucosylation in type I collagen: molecular loci and biological significance.The Journal of biological chemistry · 2012Article
- Bone architecture: collagen structure and calcium/phosphorus maps.Journal of biological physics · 2008Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
This study sought to evaluate whether the architecture of the matrix of cortical and trabecular bone is exactly the same. For this purpose we analyzed the extent of some posttranslational modifications of type I collagen, which is the major component of bone matrix. Ten female and 10 male 100-day-old rats were sacrificed and the content of hydroxylysine, glycosylated hydroxylysine, and pyridinium cross-links of collagen from cortical and trabecular bone was determined. The amount of each compound was expressed as a molar ratio with hydroxyproline. The collagen posttranslational modification pattern appears to be the same in both sexes but with a higher extent of differences in females compared with males. Comparing cortical and trabecular bone, the former contains a higher amount of hydroxylysine residues whereas in the latter, glycosylation of hydroxylysine is higher and pyridinium cross-link concentration is lower. Moreover, an inverse linear relationship between glycosylated hydroxylysine and pyridinium cross-links concentration was established, both for female (r = -0.455, P = 0.04) and male rats (r = -0.426; P = 0.06). This paper discusses what these findings may mean in functional terms.
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