ArticleBiochemistry2012
Peptidyl 3-hydroxyproline binding properties of type I collagen suggest a function in fibril supramolecular assembly.
Article in Biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
15 citing papers in PubMed, 30 citations in OpenAlex.
- Molecular drivers of osteogenesis imperfecta: a cellular and extracellular collagen disease.Clinical science (London, England : 1979) · 2025Review
- Article
- Substitution of murine type I collagen A1 3-hydroxylation site alters matrix structure but does not recapitulate osteogenesis imperfecta bone dysplasia.Matrix biology : journal of the International Society for Matrix Biology · 2020Article
- Conformational landscape of substituted prolines.Biophysical reviews · 2020Review
- 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
- P3h3-null and Sc65-null Mice Phenocopy the Collagen Lysine Under-hydroxylation and Cross-linking Abnormality of Ehlers-Danlos Syndrome Type VIA.The Journal of biological chemistry · 2017Article
- The development of a mature collagen network in cartilage from human bone marrow stem cells in Transwell culture.Matrix biology : journal of the International Society for Matrix Biology · 2016Article
- Developmental Stage-dependent Regulation of Prolyl 3-Hydroxylation in Tendon Type I Collagen.The Journal of biological chemistry · 2016Article
- Abnormal type I collagen post-translational modification and crosslinking in a cyclophilin B KO mouse model of recessive osteogenesis imperfecta.PLoS genetics · 2014Article
- Molecular properties and fibril ultrastructure of types II and XI collagens in cartilage of mice expressing exclusively the α1(IIA) collagen isoform.Matrix biology : journal of the International Society for Matrix Biology · 2014Article
- Evolutionary origins of C-terminal (GPP)n 3-hydroxyproline formation in vertebrate tendon collagen.PloS one · 2014Article
- Differential effects of collagen prolyl 3-hydroxylation on skeletal tissues.PLoS genetics · 2014Article
- Bone collagen: new clues to its mineralization mechanism from recessive osteogenesis imperfecta.Calcified tissue international · 2013Review
- Posttranslational modifications in type I collagen from different tissues extracted from wild type and prolyl 3-hydroxylase 1 null mice.The Journal of biological chemistry · 2013Article
- Collagen prolyl 3-hydroxylation: a major role for a minor post-translational modification?Connective tissue research · 2013Review
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Proline residues in collagens are extensively hydroxylated post-translationally. A rare form of this modification, (3S,2S)-l-hydroxyproline (3Hyp), remains without a clear function. Disruption of the enzyme complex responsible for prolyl 3-hydroxylation results in severe forms of recessive osteogenesis imperfecta (OI). These OI types exhibit a loss of or reduction in the level of 3-hydroxylation at two proline residues, α1(I) Pro986 and α2(I) Pro707. Whether the resulting brittle bone phenotype is caused by the lack of the 3-hydroxyl addition or by another function of the enzyme complex is unknown. We have speculated that the most efficient mechanism for explaining the chemistry of collagen intermolecular cross-linking is for pairs of collagen molecules in register to be the subunit that assembles into fibrils. In this concept, the exposed hydroxyls from 3Hyp are positioned within mutually interactive binding motifs on adjacent collagen molecules that contribute through hydrogen bonding to the process of fibril supramolecular assembly. Here we report observations on the physical binding properties of 3Hyp in collagen chains from experiments designed to explore the potential for interaction using synthetic collagen-like peptides containing 3Hyp. Evidence of self-association was observed between a synthetic peptide containing 3Hyp and the CB6 domain of the α1(I) chain, which contains the single fully 3-hydroxylated proline. Using collagen from a case of severe recessive OI with a CRTAP defect, in which Pro986 was minimally 3-hydroxylated, such binding was not observed. Further study of the role of 3Hyp in supramolecular assembly is warranted for understanding the evolution of tissue-specific variations in collagen fibril organization.
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Registered trials
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