{"doi":"10.1074/jbc.m114.603266","title":"GlcUAβ1–3Galβ1–3Galβ1–4Xyl(2-O-phosphate) Is the Preferred Substrate for Chondroitin N-Acetylgalactosaminyltransferase-1","abstract":null,"journal":"Journal of Biological Chemistry","year":2015,"id":632427,"datarank":0.5333022092234121,"base_score":3.5553480614894135,"endowment":3.5553480614894135,"self_citation_contribution":0.5333022092234121,"citation_network_contribution":0.0,"self_endowment_contribution":0.5333022092234121,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":34,"citer_count":0,"citers_with_citation_signal":0,"citers_with_endowment":0,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":null,"is_data_producer":false,"deposit_databanks":null,"is_oa":false,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":null,"fair_score":null,"fair_percentile":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":1639336,"name":"Ban Sato","orcid":null,"position":1,"is_corresponding":false},{"id":1639337,"name":"Tadahisa Mikami","orcid":null,"position":2,"is_corresponding":false},{"id":1639338,"name":"Jun-ichi Tamura","orcid":null,"position":3,"is_corresponding":false},{"id":185982,"name":"Michihiro Igarashi","orcid":null,"position":4,"is_corresponding":false},{"id":184944,"name":"Hiroshi Kitagawa","orcid":"0000-0002-9307-7079","position":5,"is_corresponding":false},{"id":186289,"name":"Tomomi Izumikawa","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"GlcUAβ1–3Galβ1–3Galβ1–4Xyl(2-O-phosphate) Is the Preferred Substrate for Chondroitin N-Acetylgalactosaminyltransferase-1","abstract":"A deficiency in chondroitin N -acetylgalactosaminyltransferase-1 (ChGn-1) was previously shown to reduce the number of chondroitin sulfate (CS) chains, leading to skeletal dysplasias in mice, suggesting that ChGn-1 regulates the number of CS chains for normal cartilage development. Recently, we demonstrated that 2-phosphoxylose phosphatase (XYLP) regulates the number of CS chains by dephosphorylating the Xyl residue in the glycosaminoglycan-protein linkage region of proteoglycans. However, the relationship between ChGn-1 and XYLP in controlling the number of CS chains is not clear. In this study, we for the first time detected a phosphorylated tetrasaccharide linkage structure, GlcUAβ1–3Galβ1–3Galβ1–4Xyl(2- O -phosphate), in ChGn-1 −/− growth plate cartilage but not in ChGn-2 −/− or wild-type growth plate cartilage. In contrast, the truncated linkage tetrasaccharide GlcUAβ1–3Galβ1–3Galβ1–4Xyl was detected in wild-type, ChGn-1 −/− , and ChGn-2 −/− growth plate cartilage. Consistent with the findings, ChGn-1 preferentially transferred N -acetylgalactosamine to the phosphorylated tetrasaccharide linkage in vitro . Moreover, ChGn-1 and XYLP interacted with each other, and ChGn-1-mediated addition of N -acetylgalactosamine was accompanied by rapid XYLP-dependent dephosphorylation during formation of the CS linkage region. Taken together, we conclude that the phosphorylated tetrasaccharide linkage is the preferred substrate for ChGn-1 and that ChGn-1 and XYLP cooperatively regulate the number of CS chains in growth plate cartilage. Background The relationship between chondroitin N -acetylgalactosaminyltransferase-1 (ChGn-1) and 2-phosphoxylose phosphatase (XYLP) in controlling the number of chondroitin sulfate chains is unclear. Results GlcUAβ1–3Galβ1–3Galβ1–4Xyl(2- O -phosphate) was detected in ChGn-1 −/− but not in wild-type cartilage. ChGn-1-mediated addition of N -acetylgalactosamine was accompanied by rapid XYLP-dependent dephosphorylation. Conclusion GlcUAβ1–3Galβ1–3Galβ1–4Xyl(2- O -phosphate) is the preferred substrate for ChGn-1. Significance ChGn-1 and XYLP cooperatively regulate the number of CS chains.","is_dataset_classified":null,"base_score":3.5553480614894135,"endowment":3.5553480614894135,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"25568321","pmcid":"PMC4342460","openalex_id":"https://openalex.org/W1994535727","authors":[],"funders":[],"total_grants":0,"fwci":2.4748,"citation_percentile":0.88315853,"influential_citations":0,"citation_trend":[{"year":2015,"count":1},{"year":2016,"count":6},{"year":2017,"count":4},{"year":2018,"count":6},{"year":2019,"count":3},{"year":2020,"count":2},{"year":2021,"count":2},{"year":2022,"count":4},{"year":2023,"count":3},{"year":2024,"count":1},{"year":2025,"count":2}],"oa_status":"hybrid","license":"cc-by","oa_locations":[{"url":"http://www.jbc.org/article/S002192581946821X/pdf","host_type":"journal"},{"url":"http://www.jbc.org/article/S002192581946821X/pdf","host_type":"publisher"},{"url":"https://api.elsevier.com/content/article/PII:S002192581946821X?httpAccept=text/xml","host_type":"publisher"},{"url":"https://api.elsevier.com/content/article/PII:S002192581946821X?httpAccept=text/plain","host_type":"publisher"},{"url":"https://syndication.highwire.org/content/doi/10.1074/jbc.M114.603266","host_type":"publisher"},{"url":"https://doi.org/10.1074/jbc.m114.603266","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/25568321","host_type":"repository"},{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/4342460","host_type":"repository"}],"fields_of_study":["Proteoglycans and glycosaminoglycans research","Glycosylation and Glycoproteins Research","Polysaccharides Composition and Applications","Acetylgalactosamine","Animals","Animals, Newborn","Biosynthetic Pathways","Blotting, Western","COS Cells","Carbohydrate Sequence","Cartilage","Cells, Cultured","Chlorocebus aethiops","Chondrocytes","Chondroitin Sulfates","Glycoproteins","Glycosaminoglycans","Growth Plate","Mice, Inbred C57BL","Mice, Knockout","Molecular Sequence Data","N-Acetylgalactosaminyltransferases","Oligosaccharides","Phosphates","Phosphoric Monoester Hydrolases","Phosphorylation","Substrate Specificity","Xylose"],"mesh_terms":["Acetylgalactosamine","Animals","Animals, Newborn","Carbohydrate Sequence","Cartilage","Cells, Cultured","Chlorocebus aethiops","Chondroitin Sulfates","Glycoproteins","Glycosaminoglycans","Growth Plate","Mice, Inbred C57BL","Molecular Sequence Data","Oligosaccharides","Phosphates","Phosphoric Monoester Hydrolases","Phosphorylation","Substrate Specificity","Xylose","Blotting, Western","N-Acetylgalactosaminyltransferases","Mice, Knockout","COS Cells","Chondrocytes","Biosynthetic Pathways"],"keywords":["Tetrasaccharide","Chondroitin sulfate","Chemistry","Cartilage","Chondroitin","Biochemistry","Phosphorylation","Glycosaminoglycan","Biology","Polysaccharide","Anatomy","Phosphatase","Glycosyltransferase","Proteoglycan Synthesis"],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[{"name":"pdb"}],"source":"live","citation_network_status":"fetched"},"created_at":"2026-08-06T09:45:09.771829Z","pmid":null,"pmcid":null,"fwci":null,"citation_percentile":null,"influential_citations":0,"oa_status":null,"license":null,"views":0,"total_file_size_bytes":0,"version_count":0,"fair_f":null,"fair_a":null,"fair_i":null,"fair_r":null,"fair_zscore":null,"fair_rationale":null,"fair_model":null,"fair_agent_version":null,"fair_fulltext_source":null,"fair_has_llm":null,"fair_computed_at":null,"clinical_trials":[],"software_tools":[],"db_accessions":[],"linked_datasets":[],"topics":[]}