ArticleThe Journal of biological chemistry2011
A role for prolyl 3-hydroxylase 2 in post-translational modification of fibril-forming collagens.
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 23 papers.
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Who cites it
23 citing papers in PubMed, 48 citations in OpenAlex.
- Targeting post-translational modifications: novel insights into bone metabolic diseases.Journal of advanced research · 2026Review
- The Impact of Ageing on Fibrillar Collagens.Sub-cellular biochemistry · 2026Review
- Review
- Genetics and Clinical Findings Associated with Early-Onset Myopia and Retinal Detachment in Saudi Arabia.Genes · 2025Review
- Trio-based whole-exome sequencing reveals mutations in early-onset high myopia.BMJ open ophthalmology · 2024Article
- Age-related type I collagen modifications reveal tissue-defining differences between ligament and tendon.Matrix biology plus · 2021Article
- Biochemical and immuno-histochemical localization of type IIA procollagen in annulus fibrosus of mature bovine intervertebral disc.Matrix biology plus · 2021Article
- Prolyl 3-Hydroxylase 2 Is a Molecular Player of Angiogenesis.International journal of molecular sciences · 2021Article
- Heterogeneity in proline hydroxylation of fibrillar collagens observed by mass spectrometry.PloS one · 2021Article
- Collagen Prolyl Hydroxylases Are Bifunctional Growth Regulators in Melanoma.The Journal of investigative dermatology · 2019Review
- Article
- Large-Scale Differentiation and Site Specific Discrimination of Hydroxyproline Isomers by Electron Transfer/Higher-Energy Collision Dissociation (EThcD) Mass Spectrometry.Analytical chemistry · 2018Article
- Fibroblasts profiling in scarring trachoma identifies IL-6 as a functional component of a fibroblast-macrophage pro-fibrotic and pro-inflammatory feedback loop.Scientific reports · 2016Article
- 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
- Post-translationally abnormal collagens of prolyl 3-hydroxylase-2 null mice offer a pathobiological mechanism for the high myopia linked to human LEPREL1 mutations.The Journal of biological chemistry · 2015Article
- 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
- Biological role of prolyl 3-hydroxylation in type IV collagen.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Evolutionary origins of C-terminal (GPP)n 3-hydroxyproline formation in vertebrate tendon collagen.PloS one · 2014Article
- 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 1 institution in 1 country.
Funding
Abstract
The fibrillar collagen types I, II, and V/XI have recently been shown to have partially 3-hydroxylated proline (3Hyp) residues at sites other than the established primary Pro-986 site in the collagen triple helical domain. These sites showed tissue specificity in degree of hydroxylation and a pattern of D-periodic spacing. This suggested a contributory role in fibril supramolecular assembly. The sites in clade A fibrillar α1(II), α2(V), and α1(I) collagen chains share common features with known prolyl 3-hydroxylase 2 (P3H2) substrate sites in α1(IV) chains implying a role for this enzyme. We pursued this possibility using the Swarm rat chondrosarcoma cell line (RCS-LTC) found to express high levels of P3H2 mRNA. Mass spectrometry determined that all the additional candidate 3Hyp substrate sites in the pN type II collagen made by these cells were highly hydroxylated. In RNA interference experiments, P3H2 protein synthesis was suppressed coordinately with prolyl 3-hydroxylation at Pro-944, Pro-707, and the C-terminal GPP repeat of the pNα1(II) chain, but Pro-986 remained fully hydroxylated. Furthermore, when P3H2 expression was turned off, as seen naturally in cultured SAOS-2 osteosarcoma cells, full 3Hyp occupancy at Pro-986 in α1(I) chains was unaffected, whereas 3-hydroxylation of residue Pro-944 in the α2(V) chain was largely lost, and 3-hydroxylation of Pro-707 in α2(V) and α2(I) chains were sharply reduced. The results imply that P3H2 has preferred substrate sequences among the classes of 3Hyp sites in clade A collagen chains.
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