ArticleThe Journal of biological chemistry2013
Posttranslational modifications in type I collagen from different tissues extracted from wild type and prolyl 3-hydroxylase 1 null mice.
Article in The Journal of biological chemistry, 2013. 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, 54 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
- Secretion-based production of prolyl-hydroxylated human type III collagen in scalable Physcomitrella photobioreactors.Plant cell reports · 2026Article
- Collagen Mechanics.Sub-cellular biochemistry · 2026Review
- Collagen IV biosynthesis: Intracellular choreography of post-translational modifications.Matrix biology : journal of the International Society for Matrix Biology · 2025Review
- Comprehensive analysis of the effects ofFrontiers in cell and developmental biology · 2025Article
- How Significant Are Marine Invertebrate Collagens? Exploring Trends in Research and Innovation.Marine drugs · 2024Review
- Targeted silencing ofFrontiers in endocrinology · 2024Article
- Milder presentation of osteogenesis imperfecta type VIII due to compound heterozygosity for a predicted loss-of-function variant and novel missense variant inCold Spring Harbor molecular case studies · 2023Article
- Article
- Age-related type I collagen modifications reveal tissue-defining differences between ligament and tendon.Matrix biology plus · 2021Article
- Collagen Biosynthesis, Processing, and Maturation in Lung Ageing.Frontiers in medicine · 2021Review
- Cosmetic Syndrome Correction with Calcium Hydroxylapatite-Based Filler in Patients with Connective Tissue Dysplasia.Dermatology research and practice · 2021Article
- Basic Structure, Physiology, and Biochemistry of Connective Tissues and Extracellular Matrix Collagens.Advances in experimental medicine and biology · 2021Article
- Effect of hydroxylysine-O-glycosylation on the structure of type I collagen molecule: A computational study.Glycobiology · 2020Article
- 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
- Sex effects of dietary protein source and acid load on renal and bone status in the PahPhysiological reports · 2019Article
- The endoplasmic reticulum-resident collagen chaperone Hsp47 interacts with and promotes the secretion of decorin, fibromodulin, and lumican.The Journal of biological chemistry · 2018Article
- The triple helix of collagens - an ancient protein structure that enabled animal multicellularity and tissue evolution.Journal of cell science · 2018Review
- Heat shock protein 47 and 65-kDa FK506-binding protein weakly but synergistically interact during collagen folding in the endoplasmic reticulum.The Journal of biological chemistry · 2017Article
- Ziploc-ing the structure 2.0: Endoplasmic reticulum-resident peptidyl prolyl isomerases show different activities toward hydroxyproline.The Journal of biological chemistry · 2017Article
Corrections and comments
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Authors and funding
10 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Type I collagen extracted from tendon, skin, and bone of wild type and prolyl 3-hydroxylase 1 (P3H1) null mice shows distinct patterns of 3-hydroxylation and glycosylation of hydroxylysine residues. The A1 site (Pro-986) in the α1-chain of type I collagen is almost completely 3-hydroxylated in every tissue of the wild type mice. In contrast, no 3-hydroxylation of this proline residue was found in P3H1 null mice. Partial 3-hydroxylation of the A3 site (Pro-707) was present in tendon and bone, but absent in skin in both α-chains of the wild type animals. Type I collagen extracted from bone of P3H1 null mice shows a large reduction in 3-hydroxylation of the A3 site in both α-chains, whereas type I collagen extracted from tendon of P3H1 null mice shows little difference as compared with wild type. These results demonstrate that the A1 site in type I collagen is exclusively 3-hydroxylated by P3H1, and presumably, this enzyme is required for the 3-hydroxylation of the A3 site of both α-chains in bone but not in tendon. The increase in glycosylation of hydroxylysine in P3H1 null mice in bone was found to be due to an increased occupancy of normally glycosylated sites. Despite the severe disorganization of collagen fibrils in adult tissues, the D-period of the fibrils is unchanged. Tendon fibrils of newborn P3H1 null mice are well organized with only a slight increase in diameter. The absence of 3-hydroxyproline and/or the increased glycosylation of hydroxylysine in type I collagen disturbs the lateral growth of the fibrils.
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