ArticleThe Journal of biological chemistry2011
A novel 3-hydroxyproline (3Hyp)-rich motif marks the triple-helical C terminus of tendon type I collagen.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 55 citations in OpenAlex.
- Prolyl-3-hydroxylase 1 is a central regulator of collagen post-translational modifications and the collagen biosynthetic network.The Journal of biological chemistry · 2026Article
- The Impact of Ageing on Fibrillar Collagens.Sub-cellular biochemistry · 2026Review
- Loss of the long form of Plod2 phenocopies contractures of Bruck syndrome-osteogenesis imperfecta.Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research · 2024Article
- Impact of Bioinformatics Search Parameters for Peptides' Identification and Their Post-Translational Modifications: A Case Study of Proteolysed Gelatines from Beef, Pork, and Fish.Foods (Basel, Switzerland) · 2023Article
- Age-related type I collagen modifications reveal tissue-defining differences between ligament and tendon.Matrix biology plus · 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
- Use of osteoblast-derived matrix to assess the influence of collagen modifications on cancer cells.Matrix biology plus · 2020Article
- Conformational landscape of substituted prolines.Biophysical reviews · 2020Review
- Down-Regulation of Collagen Hydroxylation in Colorectal Liver Metastasis.Frontiers in oncology · 2020Article
- Role of prolyl hydroxylation in the molecular interactions of collagens.Essays in biochemistry · 2019Review
- Quantitative proteomic profiling of extracellular matrix and site-specific collagen post-translational modifications in anMatrix biology plus · 2019Article
- Large-Scale Differentiation and Site Specific Discrimination of Hydroxyproline Isomers by Electron Transfer/Higher-Energy Collision Dissociation (EThcD) Mass Spectrometry.Analytical chemistry · 2018Article
- The triple helix of collagens - an ancient protein structure that enabled animal multicellularity and tissue evolution.Journal of cell science · 2018Review
- Distinct post-translational features of type I collagen are conserved in mouse and human periodontal ligament.Journal of periodontal research · 2017Article
- Genome-wide analysis identifies differential promoter methylation of Leprel2, Foxf1, Mmp25, Igfbp6, and Peg12 in murine tendinopathy.Journal of orthopaedic research : official publication of the Orthopaedic Research Society · 2017Article
- Collagen cross-linking: insights on the evolution of metazoan extracellular matrix.Scientific reports · 2016Article
- The supramolecular structure of bone: X-ray scattering analysis and lateral structure modeling.Acta crystallographica. Section D, Structural biology · 2016Article
- Osteogenesis imperfecta.Lancet (London, England) · 2016Review
- Developmental Stage-dependent Regulation of Prolyl 3-Hydroxylation in Tendon Type I Collagen.The Journal of biological chemistry · 2016Article
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Authors and funding
5 authors at 1 institution in 1 country.
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Abstract
Because of its unique physical and chemical properties, rat tail tendon collagen has long been favored for crystallographic and biochemical studies of fibril structure. In studies of the distribution of 3-hydroxyproline in type I collagen of rat bone, skin, and tail tendon by mass spectrometry, the repeating sequences of Gly-Pro-Pro (GPP) triplets at the C terminus of α1(I) and α2(I) chains were shown to be heavily 3-hydroxylated in tendon but not in skin and bone. By isolating the tryptic peptides and subjecting them to Edman sequence analysis, the presence of repeating 3-hydroxyprolines in consecutive GPP triplets adjacent to 4-hydroxyproline was confirmed as a unique feature of the tendon collagen. A 1960s study by Piez et al. (Piez, K. A., Eigner, E. A., and Lewis, M. S. (1963) Biochemistry 2, 58-66) in which they compared the amino acid compositions of rat skin and tail tendon type I collagen chains indeed showed 3-4 residues of 3Hyp in tendon α1(I) and α2(I) chains but only one 3Hyp residue in skin α1(I) and none in α2(I). The present work therefore confirms this difference and localizes the additional 3Hyp to the GPP repeat at the C terminus of the triple-helix. We speculate on the significance in terms of a potential function in contributing to the unique assembly mechanism and molecular packing in tendon collagen fibrils and on mechanisms that could regulate 3-hydroxylation at this novel substrate site in a tissue-specific manner.
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