{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,23]],"date-time":"2026-07-23T16:26:35Z","timestamp":1784823995251,"version":"3.55.0"},"reference-count":33,"publisher":"Elsevier BV","issue":"4","license":[{"start":{"date-parts":[[2024,4,1]],"date-time":"2024-04-01T00:00:00Z","timestamp":1711929600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2024,4,1]],"date-time":"2024-04-01T00:00:00Z","timestamp":1711929600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2024,3,11]],"date-time":"2024-03-11T00:00:00Z","timestamp":1710115200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["Z01-DE000713"],"award-info":[{"award-number":["Z01-DE000713"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["DE000649"],"award-info":[{"award-number":["DE000649"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000072","name":"National Institute of Dental and Craniofacial Research","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100000072","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["jbc.org","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Biological Chemistry"],"published-print":{"date-parts":[[2024,4]]},"DOI":"10.1016\/j.jbc.2024.107164","type":"journal-article","created":{"date-parts":[[2024,3,12]],"date-time":"2024-03-12T12:14:36Z","timestamp":1710245676000},"page":"107164","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":2,"title":["Loss of the glycosyltransferase Galnt11 affects vitamin D\u00a0homeostasis and bone composition"],"prefix":"10.1016","volume":"300","author":[{"given":"E.","family":"Tian","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Caroline","family":"Rothermel","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-5220-4046","authenticated-orcid":false,"given":"Zachary","family":"Michel","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Luis Fernandez","family":"de Castro","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jeeyoung","family":"Lee","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tina","family":"Kilts","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tristan","family":"Kent","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Michael T.","family":"Collins","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2057-8120","authenticated-orcid":false,"given":"Kelly G.","family":"Ten Hagen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.jbc.2024.107164_bib1","doi-asserted-by":"crossref","first-page":"736","DOI":"10.1093\/glycob\/cwr182","article-title":"Control of mucin-type O-glycosylation: a classification of the polypeptide GalNAc-transferase gene family","volume":"22","author":"Bennett","year":"2012","journal-title":"Glycobiology"},{"key":"10.1016\/j.jbc.2024.107164_bib2","doi-asserted-by":"crossref","first-page":"6921","DOI":"10.1074\/jbc.R112.418558","article-title":"Mucin-type O-glycosylation during development","volume":"288","author":"Tran","year":"2013","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2024.107164_bib3","doi-asserted-by":"crossref","first-page":"3508","DOI":"10.1038\/s41467-018-05978-9","article-title":"A\u00a0molecular switch orchestrates enzyme specificity and secretory granule morphology","volume":"9","author":"Ji","year":"2018","journal-title":"Nat. Commun."},{"key":"10.1016\/j.jbc.2024.107164_bib4","doi-asserted-by":"crossref","first-page":"35039","DOI":"10.1074\/jbc.M303836200","article-title":"Functional characterization and expression analysis of members of the UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase family from Drosophila melanogaster","volume":"278","author":"Ten Hagen","year":"2003","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2024.107164_bib5","doi-asserted-by":"crossref","first-page":"102","DOI":"10.1093\/glycob\/cwn096","article-title":"Glycobiology on the fly: developmental and mechanistic insights from Drosophila","volume":"19","author":"ten Hagen","year":"2009","journal-title":"Glycobiology"},{"key":"10.1016\/j.jbc.2024.107164_bib6","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1093\/glycob\/cwj051","article-title":"Expression of the UDP-GalNAc: polypeptide N-acetylgalactosaminyltransferase family is spatially and temporally regulated during Drosophila development","volume":"16","author":"Tian","year":"2006","journal-title":"Glycobiology"},{"key":"10.1016\/j.jbc.2024.107164_bib7","doi-asserted-by":"crossref","first-page":"360","DOI":"10.1093\/glycob\/cwv108","article-title":"Mucin-type O-glycosylation is controlled by short- and long-range glycopeptide substrate recognition that varies among members of the polypeptide GalNAc transferase family","volume":"26","author":"Revoredo","year":"2016","journal-title":"Glycobiology"},{"key":"10.1016\/j.jbc.2024.107164_bib8","doi-asserted-by":"crossref","first-page":"2543","DOI":"10.1210\/en.2008-0877","article-title":"Ablation of the Galnt3 gene leads to low-circulating intact fibroblast growth factor 23 (Fgf23) concentrations and hyperphosphatemia despite increased Fgf23 expression","volume":"150","author":"Ichikawa","year":"2009","journal-title":"Endocrinology"},{"key":"10.1016\/j.jbc.2024.107164_bib9","doi-asserted-by":"crossref","first-page":"869","DOI":"10.1038\/ncomms1874","article-title":"O-glycosylation modulates integrin and FGF signalling by influencing the secretion of basement membrane components","volume":"3","author":"Tian","year":"2012","journal-title":"Nat. Commun."},{"key":"10.1016\/j.jbc.2024.107164_bib10","doi-asserted-by":"crossref","first-page":"5243","DOI":"10.1074\/jbc.M111.306159","article-title":"Multiple members of the UDP-GalNAc: polypeptide N-acetylgalactosaminyltransferase family are essential for viability in Drosophila","volume":"287","author":"Tran","year":"2012","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2024.107164_bib11","doi-asserted-by":"crossref","first-page":"7296","DOI":"10.1073\/pnas.1322264111","article-title":"O-glycosylation regulates polarized secretion by modulating Tango1 stability","volume":"111","author":"Zhang","year":"2014","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2024.107164_bib12","doi-asserted-by":"crossref","first-page":"21231","DOI":"10.1074\/jbc.M117.809848","article-title":"Loss of the mucosal barrier alters the progenitor cell niche via Janus kinase\/signal transducer and activator of transcription (JAK\/STAT) signaling","volume":"292","author":"Zhang","year":"2017","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2024.107164_bib13","doi-asserted-by":"crossref","first-page":"40122","DOI":"10.1074\/jbc.M111.287912","article-title":"A\u00a0systematic study of site-specific GalNAc-type O-glycosylation modulating proprotein convertase processing","volume":"286","author":"Schjoldager","year":"2011","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2024.107164_bib14","doi-asserted-by":"crossref","first-page":"14623","DOI":"10.1073\/pnas.1511175112","article-title":"A\u00a0systematic study of modulation of ADAM-mediated ectodomain shedding by site-specific O-glycosylation","volume":"112","author":"Goth","year":"2015","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2024.107164_bib15","doi-asserted-by":"crossref","DOI":"10.1016\/j.molmet.2022.101472","article-title":"A\u00a0novel role for GalNAc-T2 dependent glycosylation in energy homeostasis","volume":"60","author":"Verzijl","year":"2022","journal-title":"Mol. Metab."},{"key":"10.1016\/j.jbc.2024.107164_bib16","doi-asserted-by":"crossref","first-page":"579","DOI":"10.1038\/ng1358","article-title":"Mutations in GALNT3, encoding a protein involved in O-linked glycosylation, cause familial tumoral calcinosis","volume":"36","author":"Topaz","year":"2004","journal-title":"Nat. Genet."},{"key":"10.1016\/j.jbc.2024.107164_bib17","doi-asserted-by":"crossref","first-page":"1114","DOI":"10.1093\/brain\/awaa063","article-title":"Novel congenital disorder of O-linked glycosylation caused by GALNT2 loss of function","volume":"143","author":"Zilmer","year":"2020","journal-title":"Brain"},{"key":"10.1016\/j.jbc.2024.107164_bib18","doi-asserted-by":"crossref","first-page":"1017","DOI":"10.1038\/ki.2014.361","article-title":"Genome-wide association study of kidney function decline in individuals of European descent","volume":"87","author":"Gorski","year":"2015","journal-title":"Kidney Int."},{"key":"10.1016\/j.jbc.2024.107164_bib19","doi-asserted-by":"crossref","first-page":"25196","DOI":"10.1073\/pnas.1909573116","article-title":"Galnt11 regulates kidney function by glycosylating the endocytosis receptor megalin to modulate ligand binding","volume":"116","author":"Tian","year":"2019","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2024.107164_bib20","doi-asserted-by":"crossref","first-page":"3690","DOI":"10.3390\/nu14183690","article-title":"Megalin and vitamin D metabolism-implications in non-renal tissues and kidney disease","volume":"14","author":"Khan","year":"2022","journal-title":"Nutrients"},{"key":"10.1016\/j.jbc.2024.107164_bib21","doi-asserted-by":"crossref","first-page":"718","DOI":"10.3389\/fendo.2019.00718","article-title":"Vitamin D binding protein and the biological activity of vitamin D","volume":"10","author":"Chun","year":"2019","journal-title":"Front. Endocrinol. (Lausanne)"},{"key":"10.1016\/j.jbc.2024.107164_bib22","series-title":"Endotext","article-title":"Vitamin D: production, metabolism and mechanisms of action","author":"Bikle","year":"2000"},{"key":"10.1016\/j.jbc.2024.107164_bib23","doi-asserted-by":"crossref","first-page":"777","DOI":"10.1007\/s00467-002-0919-x","article-title":"Cell biology of renal osteodystrophy","volume":"17","author":"Kuizon","year":"2002","journal-title":"Pediatr. Nephrol."},{"key":"10.1016\/j.jbc.2024.107164_bib24","doi-asserted-by":"crossref","first-page":"8889","DOI":"10.1038\/s41598-020-65921-1","article-title":"PTH(1-34) treatment and\/or mechanical loading have different osteogenic effects on the trabecular and cortical bone in the ovariectomized C57BL\/6 mouse","volume":"10","author":"Roberts","year":"2020","journal-title":"Sci. Rep."},{"key":"10.1016\/j.jbc.2024.107164_bib25","doi-asserted-by":"crossref","first-page":"5620","DOI":"10.1074\/jbc.274.9.5620","article-title":"Megalin antagonizes activation of the parathyroid hormone receptor","volume":"274","author":"Hilpert","year":"1999","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2024.107164_bib26","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1006\/abbi.2000.1970","article-title":"Regulation of 25-hydroxyvitamin D3 1alpha-hydroxylase gene expression by parathyroid hormone and 1,25-dihydroxyvitamin D3","volume":"381","author":"Brenza","year":"2000","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.jbc.2024.107164_bib27","doi-asserted-by":"crossref","first-page":"1184","DOI":"10.1016\/j.kint.2016.06.041","article-title":"Parathyroid hormone metabolism and signaling in health and chronic kidney disease","volume":"90","author":"Evenepoel","year":"2016","journal-title":"Kidney Int."},{"key":"10.1016\/j.jbc.2024.107164_bib28","doi-asserted-by":"crossref","first-page":"637","DOI":"10.1038\/s41574-018-0076-3","article-title":"Role of phosphate sensing in bone and mineral metabolism","volume":"14","author":"Chande","year":"2018","journal-title":"Nat. Rev. Endocrinol."},{"key":"10.1016\/j.jbc.2024.107164_bib29","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1053\/j.jrn.2010.10.007","article-title":"Vitamin D biology: from the discovery to its significance in chronic kidney disease","volume":"21","author":"Cuppari","year":"2011","journal-title":"J.\u00a0Ren. Nutr."},{"key":"10.1016\/j.jbc.2024.107164_bib30","doi-asserted-by":"crossref","first-page":"299","DOI":"10.1056\/NEJMoa2202106","article-title":"Supplemental vitamin D and incident fractures in midlife and older adults","volume":"387","author":"LeBoff","year":"2022","journal-title":"N.\u00a0Engl. J. Med."},{"key":"10.1016\/j.jbc.2024.107164_bib31","doi-asserted-by":"crossref","DOI":"10.1016\/j.nut.2023.112151","article-title":"Supplementation of vitamin D isolated or calcium-associated with bone remodeling and fracture risk in postmenopausal women without osteoporosis: a systematic review of randomized clinical trials","volume":"116","author":"Reis","year":"2023","journal-title":"Nutrition"},{"key":"10.1016\/j.jbc.2024.107164_bib32","doi-asserted-by":"crossref","first-page":"281","DOI":"10.1007\/s00223-005-0039-2","article-title":"Compartmental bone morphometry in the mouse femur: reproducibility and resolution dependence of microtomographic measurements","volume":"77","author":"Kohler","year":"2005","journal-title":"Calcif. Tissue Int."},{"key":"10.1016\/j.jbc.2024.107164_bib33","doi-asserted-by":"crossref","first-page":"1468","DOI":"10.1002\/jbmr.141","article-title":"Guidelines for assessment of bone microstructure in rodents using micro-computed tomography","volume":"25","author":"Bouxsein","year":"2010","journal-title":"J.\u00a0Bone Miner. Res."}],"container-title":["Journal of Biological Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925824016594?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925824016594?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,11,3]],"date-time":"2025-11-03T16:47:23Z","timestamp":1762188443000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0021925824016594"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2024,4]]},"references-count":33,"journal-issue":{"issue":"4","published-print":{"date-parts":[[2024,4]]}},"alternative-id":["S0021925824016594"],"URL":"https:\/\/doi.org\/10.1016\/j.jbc.2024.107164","relation":{},"ISSN":["0021-9258"],"issn-type":[{"value":"0021-9258","type":"print"}],"subject":[],"published":{"date-parts":[[2024,4]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Loss of the glycosyltransferase Galnt11 affects vitamin D\u00a0homeostasis and bone composition","name":"articletitle","label":"Article Title"},{"value":"Journal of Biological Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.jbc.2024.107164","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"Published by Elsevier Inc on behalf of American Society for Biochemistry and Molecular Biology.","name":"copyright","label":"Copyright"}],"article-number":"107164"}}