ArticleThe Journal of biological chemistry2016
Developmental Stage-dependent Regulation of Prolyl 3-Hydroxylation in Tendon Type I Collagen.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 40 citations in OpenAlex.
- The Impact of Ageing on Fibrillar Collagens.Sub-cellular biochemistry · 2026Review
- Lysyl hydroxylase 2 mediated collagen post-translational modifications and functional outcomes.Scientific reports · 2022Article
- Identification of a highly stable bioactive 3-hydroxyproline-containing tripeptide in human blood after collagen hydrolysate ingestion.NPJ science of food · 2022Article
- The Thermal Stability of the Collagen Triple Helix Is Tuned According to the Environmental Temperature.International journal of molecular sciences · 2022Article
- Age-related type I collagen modifications reveal tissue-defining differences between ligament and tendon.Matrix biology plus · 2021Article
- In-depth correlation analysis demonstrates that 4-hydroxyproline at the Yaa position of Gly-Xaa-Yaa repeats dominantly stabilizes collagen triple helix.Matrix biology plus · 2021Article
- Tendon and motor phenotypes in theeLife · 2021Article
- Reticulocalbin 3 is involved in postnatal tendon development by regulating collagen fibrillogenesis and cellular maturation.Scientific reports · 2021Article
- Heterogeneity in proline hydroxylation of fibrillar collagens observed by mass spectrometry.PloS one · 2021Article
- Lowering the culture temperature corrects collagen abnormalities caused by HSP47 gene knockout.Scientific reports · 2019Article
- Role of prolyl hydroxylation in the molecular interactions of collagens.Essays in biochemistry · 2019Review
- Large-Scale Differentiation and Site Specific Discrimination of Hydroxyproline Isomers by Electron Transfer/Higher-Energy Collision Dissociation (EThcD) Mass Spectrometry.Analytical chemistry · 2018Article
- Distinct post-translational features of type I collagen are conserved in mouse and human periodontal ligament.Journal of periodontal research · 2017Article
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- Type I and type V procollagen triple helix uses different subsets of the molecular ensemble for lysine posttranslational modifications in the rER.The Journal of biological chemistryArticle
Corrections and comments
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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
3-Hydroxyproline (3-Hyp), which is unique to collagen, is a fairly rare post-translational modification. Recent studies have suggested a function of prolyl 3-hydroxylation in fibril assembly and its relationships with certain disorders, including recessive osteogenesis imperfecta and high myopia. However, no direct evidence for the physiological and pathological roles of 3-Hyp has been presented. In this study, we first estimated the overall alterations in prolyl hydroxylation in collagens purified from skin, bone, and tail tendon of 0.5-18-month-old rats by LC-MS analysis with stable isotope-labeled collagen, which was recently developed as an internal standard for highly accurate collagen analyses. 3-Hyp was found to significantly increase in tendon collagen until 3 months after birth and then remain constant, whereas increased prolyl 3-hydroxylation was not observed in skin and bone collagen. Site-specific analysis further revealed that 3-Hyp was increased in tendon type I collagen in a specific sequence region, including a previously known modification site at Pro(707) and newly identified sites at Pro(716) and Pro(719), at the early ages. The site-specific alterations in prolyl 3-hydroxylation with aging were also observed in bovine Achilles tendon. We postulate that significant increases in 3-Hyp at the consecutive modification sites are correlated with tissue development in tendon. The present findings suggest that prolyl 3-hydroxylation incrementally regulates collagen fibril diameter in tendon.
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