ArticleMolecular and cellular biology2009
Core glycosylation of collagen is initiated by two beta(1-O)galactosyltransferases.
Article in Molecular and cellular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 78 papers, 2 of them syntheses that pooled it.
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Who cites it
78 citing papers in PubMed, 2 syntheses or guidelines pooled it, 152 citations in OpenAlex.
- Type VIII collagen: advances in matrix biology and translational promise.Frontiers in bioengineering and biotechnology · 2025Pooled it
- Pooled it
- Rare protein-coding variation and the genetic architecture of height in >1.4 million individuals.medRxiv : the preprint server for health sciences · 2026Article
- Succinate supplementation ameliorates musculoskeletal defects caused by PLOD3 mutations in a BCARD syndrome model.Genome medicine · 2026Article
- Post-translational modifications of collagen type I in osteogenesis imperfecta: Systematic review and meta-analysis.Bone reports · 2026Article
- Glycan-related genes and genetic disorders.Journal of human genetics · 2026Review
- Molecular basis of collagen galactosylation by GLT25D1.Nature communications · 2026Article
- Collagen IV biosynthesis: Intracellular choreography of post-translational modifications.Matrix biology : journal of the International Society for Matrix Biology · 2025Review
- The Expanding Genetic Architecture of Arteriopathies: From Canonical TAAD Genes to Emerging Connective Tissue and Signaling Pathways.Medical sciences (Basel, Switzerland) · 2025Review
- Enzymatic craftsmanship in collagen glycosylation.Nature communications · 2025Article
- The life cycle of type IV collagen.Matrix biology : journal of the International Society for Matrix Biology · 2025Review
- Structural basis of collagen glucosyltransferase function and its serendipitous role in kojibiose synthesis.Nature communications · 2025Article
- Cloning, expression, and characterization of collagen galactosyltransferases from human, sponge, and sea walnut.Protein expression and purification · 2025Article
- Molecular structure and enzymatic mechanism of the human collagen hydroxylysine galactosyltransferase GLT25D1/COLGALT1.Nature communications · 2025Article
- The collagen-modifying enzyme GLT25D1 is a prognostic indicator related to immunosuppression and malignant phenotypes in hepatocellular carcinoma.Cancer cell international · 2025Article
- Deciphering the shared genetic structure between hip osteoarthritis and femoral neck bone mineral density.Frontiers in genetics · 2025Article
- ColPTMScape: An open access knowledge base for tissue-specific collagen PTM maps.Matrix biology plus · 2024Article
- Glycosylation Modulates the Structure and Functions of Collagen: A Review.Molecules (Basel, Switzerland) · 2024Review
- Procollagen-lysine 2-oxoglutarate 5-dioxygenases are responsible for 5R-hydroxylysine modification of therapeutic T-cell bispecific monoclonal antibodies produced by Chinese hamster ovary cells.Frontiers in bioengineering and biotechnology · 2024Article
- Glycobiology in osteoclast differentiation and function.Bone research · 2023Review
18 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Collagen is a trimer of three left-handed alpha chains representing repeats of the motif Gly-X-Y, where (hydroxy)proline and (hydroxy)lysine residues are often found at positions X and Y. Selected hydroxylysines are further modified by the addition of galactose and glucose-galactose units. Collagen glycosylation takes place in the endoplasmic reticulum before triple-helix formation and is mediated by beta(1-O)galactosyl- and alpha(1-2)glucosyltransferase enzymes. We have identified two collagen galactosyltransferases using affinity chromatography and tandem mass spectrometry protein sequencing. The two collagen beta(1-O)galactosyltransferases corresponded to the GLT25D1 and GLT25D2 proteins. Recombinant GLT25D1 and GLT25D2 enzymes showed a strong galactosyltransferase activity toward various types of collagen and toward the serum mannose-binding lectin MBL, which contains a collagen domain. Amino acid analysis of the products of GLT25D1 and GLT25D2 reactions confirmed the transfer of galactose to hydroxylysine residues. The GLT25D1 gene is constitutively expressed in human tissues, whereas the GLT25D2 gene is expressed only at low levels in the nervous system. The GLT25D1 and GLT25D2 enzymes are similar to CEECAM1, to which we could not attribute any collagen galactosyltransferase activity. The GLT25D1 and GLT25D2 genes now allow addressing of the biological significance of collagen glycosylation and the importance of this posttranslational modification in the etiology of connective tissue disorders.
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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.