ArticleThe Journal of biological chemistry
Type I and type V procollagen triple helix uses different subsets of the molecular ensemble for lysine posttranslational modifications in the rER.
Article in The Journal of biological chemistry. 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, 26 citations in OpenAlex.
- Comparative Study of the Positions of Glycosylated Residues in the Chains of Fibril-Forming Collagens and the Role that These Residues Play in Axial and Lateral Assembly.Sub-cellular biochemistry · 2026Review
- Structure and Function of the Extracellular Matrix in Normal and Pathological Conditions: Looking at the Bicuspid Aortic Valve.International journal of molecular sciences · 2025Review
- Evidence for the major role of PH4⍺EFB in the prolyl 4-hydroxylation of Drosophila collagen IV.Matrix biology : journal of the International Society for Matrix Biology · 2025Article
- Collagen IV biosynthesis: Intracellular choreography of post-translational modifications.Matrix biology : journal of the International Society for Matrix Biology · 2025Review
- Collagen Biosynthesis and Its Molecular Ensemble: What Remains Unexplored.Biochemistry · 2025Review
- A multifunction murine Col4a1 allele reveals potential gene therapy parameters for Gould syndrome.The Journal of cell biology · 2025Article
- Cloning, expression, and characterization of collagen galactosyltransferases from human, sponge, and sea walnut.Protein expression and purification · 2025Article
- Biochemical characterization of collagen I in Warmblood Fragile Foal Syndrome horse lysyl hydroxylase 1 mutation.microPublication biology · 2025Article
- Role of ZNF334 in cervical cancer: implications for EMT reversal and tumor suppression.Medical oncology (Northwood, London, England) · 2024Article
- ColPTMScape: An open access knowledge base for tissue-specific collagen PTM maps.Matrix biology plus · 2024Article
- Review
- Classification of osteogenesis imperfecta: Importance for prophylaxis and genetic counseling.World journal of clinical cases · 2023Review
- Collagen V α1 Chain Decrease in Papillary Dermis from Early Systemic Sclerosis: A New Proposal in Cutaneous Fibrosis Molecular Structure.International journal of molecular sciences · 2022Article
- Lysyl hydroxylase 2 mediated collagen post-translational modifications and functional outcomes.Scientific reports · 2022Article
- The Thermal Stability of the Collagen Triple Helix Is Tuned According to the Environmental Temperature.International journal of molecular sciences · 2022Article
- Lysyl hydroxylase 1 (LH1) deficiency promotes angiotensin II (Ang II)-induced dissecting abdominal aortic aneurysm.Theranostics · 2021Article
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Authors and funding
13 authors at 5 institutions in 3 countries.
Funding
Abstract
Collagen is the most abundant protein in humans. It has a characteristic triple-helix structure and is heavily posttranslationally modified. The complex biosynthesis of collagen involves processing by many enzymes and chaperones in the rough endoplasmic reticulum. Lysyl hydroxylase 1 (LH1) is required to hydroxylate lysine for cross-linking and carbohydrate attachment within collagen triple helical sequences. Additionally, a recent study of prolyl 3-hydroxylase 3 (P3H3) demonstrated that this enzyme may be critical for LH1 activity; however, the details surrounding its involvement remain unclear. If P3H3 is an LH1 chaperone that is critical for LH1 activity, P3H3 and LH1 null mice should display a similar deficiency in lysyl hydroxylation. To test this hypothesis, we compared the amount and location of hydroxylysine in the triple helical domains of type V and I collagen from P3H3 null, LH1 null, and wild-type mice. The amount of hydroxylysine in type V collagen was reduced in P3H3 null mice, but surprisingly type V collagen from LH1 null mice contained as much hydroxylysine as type V collagen from wild-type mice. In type I collagen, our results indicate that LH1 plays a global enzymatic role in lysyl hydroxylation. P3H3 is also involved in lysyl hydroxylation, particularly at cross-link formation sites, but is not required for all lysyl hydroxylation sites. In summary, our study suggests that LH1 and P3H3 likely have two distinct mechanisms to recognize different collagen types and to distinguish cross-link formation sites from other sites in type I collagen.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.