{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,9]],"date-time":"2026-02-09T23:14:56Z","timestamp":1770678896816,"version":"3.49.0"},"reference-count":87,"publisher":"Oxford University Press (OUP)","issue":"5","license":[{"start":{"date-parts":[[2020,12,9]],"date-time":"2020-12-09T00:00:00Z","timestamp":1607472000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/academic.oup.com\/journals\/pages\/open_access\/funder_policies\/chorus\/standard_publication_model"}],"funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["DK109599"],"award-info":[{"award-number":["DK109599"]}],"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":["GM098539"],"award-info":[{"award-number":["GM098539"]}],"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":["DK078244"],"award-info":[{"award-number":["DK078244"]}],"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":["DK082753"],"award-info":[{"award-number":["DK082753"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"name":"Ministry of Health, Czech Republic","award":["00098892"],"award-info":[{"award-number":["00098892"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2021,6,3]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Mucin-type O-glycosylation occurs on many proteins that transit the Golgi apparatus. These glycans impact structure and function of many proteins and have important roles in cellular biosynthetic processes, signaling and differentiation. Although recent technological advances have enhanced our ability to profile glycosylation of glycoproteins, limitations in the understanding of the biosynthesis of these glycan structures remain. Some of these limitations stem from the difficulty to track the biosynthetic process of mucin-type O-glycosylation, especially when glycans occur in dense clusters in repeat regions of proteins, such as the mucins or immunoglobulin A1 (IgA1). Here, we describe a series of nano-liquid chromatography (LC)\u2013mass spectrometry (MS) analyses that demonstrate the range of glycosyltransferase enzymatic activities involved in the biosynthesis of clustered O-glycans on IgA1. By utilizing nano-LC\u2013MS relative quantitation of in vitro reaction products, our results provide unique insights into the biosynthesis of clustered IgA1 O-glycans. We have developed a workflow to determine glycoform-specific apparent rates of a human UDP-N-acetylgalactosamine:polypeptide N-acetylgalactosaminyltrasnfersase (GalNAc-T EC 2.4.1.41) and demonstrated how pre-existing glycans affect subsequent activity of glycosyltransferases, such as core 1 galactosyltransferase and \u03b12,3- and \u03b12,6-specific sialyltransferases, in successive additions in the biosynthesis of clustered O-glycans. In the context of IgA1, these results have potential to provide insight into the molecular mechanisms implicated in the pathogenesis of IgA nephropathy, an autoimmune renal disease involving aberrant IgA1 O-glycosylation. In a broader sense, these methods and workflows are applicable to the studies of the concerted and competing functions of other glycosyltransferases that initiate and extend mucin-type core 1 clustered O-glycosylation.<\/jats:p>","DOI":"10.1093\/glycob\/cwaa111","type":"journal-article","created":{"date-parts":[[2020,12,5]],"date-time":"2020-12-05T12:19:49Z","timestamp":1607170789000},"page":"540-556","source":"Crossref","is-referenced-by-count":13,"title":["Quantitative assessment of successive carbohydrate additions to the clustered<i>O<\/i>-glycosylation sites of IgA1 by glycosyltransferases"],"prefix":"10.1093","volume":"31","author":[{"given":"Tyler J","family":"Stewart","sequence":"first","affiliation":[{"name":"Department of Microbiology, University of Alabama at Birmingham, 845 19th Street South, BBRB 761A, Birmingham, AL 35294, USA"},{"name":"Department of Biochemistry and Molecular Genetics, University of Alabama at Birmingham, 720 20th Street South, KAUL 524, Birmingham, AL 35294, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Kazuo","family":"Takahashi","sequence":"additional","affiliation":[{"name":"Department of Biomedical Molecular Sciences, Fujita Health University School of Medicine, 1-98 Dengakugakubo, Kutsukake, Aichi, Toyoake 470-1192, Japan"},{"name":"Department of Microbiology, University of Alabama at Birmingham, 845 19th Street South, BBRB 761A, Birmingham, AL 35294, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Nuo","family":"Xu","sequence":"additional","affiliation":[{"name":"Department of Management, Information Systems & Quantitative Methods, 710 13th Street South, University of Alabama at Birmingham, Birmingham, AL 35233, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Amol","family":"Prakash","sequence":"additional","affiliation":[{"name":"Optys Tech Corporation, Shrewsbury, MA 01545, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Rhubell","family":"Brown","sequence":"additional","affiliation":[{"name":"Department of Microbiology, University of Alabama at Birmingham, 845 19th Street South, BBRB 761A, Birmingham, AL 35294, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Milan","family":"Raska","sequence":"additional","affiliation":[{"name":"Department of Immunology, Palacky University and University Hospital, Hnevotinska 3, Olomouc 775 15, Czech Republic"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Matthew B","family":"Renfrow","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Genetics, University of Alabama at Birmingham, 720 20th Street South, KAUL 524, Birmingham, AL 35294, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jan","family":"Novak","sequence":"additional","affiliation":[{"name":"Department of Microbiology, University of Alabama at Birmingham, 845 19th Street South, BBRB 761A, Birmingham, AL 35294, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"286","published-online":{"date-parts":[[2020,12,9]]},"reference":[{"key":"2021060422104624100_ref1","doi-asserted-by":"crossref","first-page":"969","DOI":"10.1046\/j.1523-1755.2001.060003969.x","article-title":"Mesangial IgA1 in IgA nephropathy exhibits aberrant O-glycosylation: observations in three patients","volume":"60","author":"Allen","year":"2001","journal-title":"Kidney Int"},{"key":"2021060422104624100_ref2","doi-asserted-by":"crossref","first-page":"7270","DOI":"10.1016\/S0021-9258(19)42101-7","article-title":"Structure of the carbohydrate units of IgA1 immunoglobulin. II. Structure of the O-glycosidically linked oligosaccharide units","volume":"249","author":"Baenziger","year":"1974","journal-title":"J Biol Chem"},{"key":"2021060422104624100_ref3","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":"2021060422104624100_ref4","doi-asserted-by":"crossref","first-page":"e45","DOI":"10.1093\/nar\/gkm047","article-title":"A versatile ligation-independent cloning method suitable for high-throughput expression screening applications","volume":"35","author":"Berrow","year":"2007","journal-title":"Nucleic Acids Res"},{"key":"2021060422104624100_ref5","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0022265","article-title":"ENZO: a web tool for derivation and evaluation of kinetic models of enzyme catalyzed reactions","volume":"6","author":"Bevc","year":"2011","journal-title":"PLoS One"},{"key":"2021060422104624100_ref6","doi-asserted-by":"crossref","first-page":"1421","DOI":"10.1006\/jmbi.1998.2556","article-title":"The Fab and Fc fragments of IgA1 exhibit a different arrangement from that in IgG: a study by X-ray and neutron solution scattering and homology modelling","volume":"286","author":"Boehm","year":"1999","journal-title":"J Mol Biol"},{"key":"2021060422104624100_ref7","doi-asserted-by":"crossref","first-page":"849","DOI":"10.1007\/BF00702349","article-title":"Specificity of O-glycosylation by bovine colostrum UDP-GalNAc: polypeptide \u03b1-N-acetylgalactosaminyltransferase using synthetic glycopeptide substrates","volume":"13","author":"Brockhausen","year":"1996","journal-title":"Glycoconj J"},{"key":"2021060422104624100_ref8","first-page":"219","article-title":"Pathways of mucin O-glycosylation in normal and malignant rat colonic epithelial cells reveal a mechanism for cancer-associated Sialyl-Tn antigen expression","volume":"382","author":"Brockhausen","year":"2001","journal-title":"Biol Chem"},{"key":"2021060422104624100_ref9","doi-asserted-by":"crossref","first-page":"4819","DOI":"10.1073\/pnas.0506855103","article-title":"Probing mucin-type O-linked glycosylation in living animals","volume":"103","author":"Dube","year":"2006","journal-title":"Proc Natl Acad Sci U S A"},{"key":"2021060422104624100_ref10","doi-asserted-by":"crossref","first-page":"5249","DOI":"10.1016\/S0021-9258(19)57206-4","article-title":"Purification and characterization of UDP-N-acetylgalactosamine: polypeptide N-acetylgalactosaminyltransferase from bovine colostrum and murine lymphoma BW5147 cells","volume":"261","author":"Elhammer","year":"1986","journal-title":"J Biol Chem"},{"key":"2021060422104624100_ref11","doi-asserted-by":"crossref","first-page":"3483","DOI":"10.1021\/acs.analchem.6b04527","article-title":"Proteoform profile mapping of the human serum complement component C9 revealing unexpected new features of N-, O-, and C-glycosylation","volume":"89","author":"Franc","year":"2017","journal-title":"Anal Chem"},{"key":"2021060422104624100_ref12","doi-asserted-by":"crossref","first-page":"8613","DOI":"10.1074\/jbc.M513590200","article-title":"Dynamic association between the catalytic and lectin domains of human UDP-GalNAc:polypeptide \u03b1-N-acetylgalactosaminyltransferase-2","volume":"281","author":"Fritz","year":"2006","journal-title":"J Biol Chem"},{"key":"2021060422104624100_ref13","first-page":"571","volume-title":"Protein Identification and Analysis Tools on the ExPASy Server","author":"Gasteiger","year":"2005"},{"key":"2021060422104624100_ref14","doi-asserted-by":"crossref","first-page":"4137","DOI":"10.1021\/bi036306a","article-title":"Kinetic modeling confirms the biosynthesis of mucin core 1 \u03b2-Gal(1-3) \u03b1-GalNAc-O-Ser\/Thr O-glycan structures are modulated by neighboring glycosylation effects","volume":"43","author":"Gerken","year":"2004","journal-title":"Biochemistry"},{"key":"2021060422104624100_ref15","doi-asserted-by":"crossref","first-page":"26580","DOI":"10.1074\/jbc.273.41.26580","article-title":"Site-specific core 1 O-glycosylation pattern of the porcine submaxillary gland mucin tandem repeat. 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