Document Detail


Identification and characterization of CMP-NeuAc:GalNAc-IgA1 alpha2,6-sialyltransferase in IgA1-producing cells.
MedLine Citation:
PMID:  17418236     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Glycosylation defects occur in several human diseases. In IgA nephropathy, IgA1 contains O-glycans that are galactose-deficient and consist mostly of core 1 alpha2,6 sialylated N-acetylgalactosamine, a configuration suspected to prevent beta1,3 galactosylation. We confirmed the same aberrancy in IgA1 secreted by the human DAKIKI B cell line. Biochemical assays indicated CMP-NeuAc:GalNAc-IgA1 alpha2,6-sialyltransferase activity in this cell line. However, a candidate enzyme, ST6-GalNAcI, was not transcribed in DAKIKI cells, B cells isolated from blood, or Epstein-Barr virus (EBV)-immortalized IgA1-producing cells from the blood of IgAN patients and healthy controls. Instead, ST6-GalNAcII transcription was detected at a high level. Expression of the ST6-GalNAcII gene and activity of the CMP-NeuAc:GalNAc-IgA1 alpha2,6-sialyltransferase were higher in IgA1-producing cell lines from IgAN patients than in such cells from healthy controls. These data are the first evidence that human cells that lack ST6-GalNAcI can sialylate core 1 GalNAc-Ser/Thr.
Authors:
Milan Raska; Zina Moldoveanu; Hitoshi Suzuki; Rhubell Brown; Rose Kulhavy; Judit Andrasi; Stacy Hall; Huong L Vu; Fredric Carlsson; Gunnar Lindahl; Milan Tomana; Bruce A Julian; Robert J Wyatt; Jiri Mestecky; Jan Novak
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't     Date:  2007-03-12
Journal Detail:
Title:  Journal of molecular biology     Volume:  369     ISSN:  0022-2836     ISO Abbreviation:  J. Mol. Biol.     Publication Date:  2007 May 
Date Detail:
Created Date:  2007-04-30     Completed Date:  2007-07-02     Revised Date:  2014-09-14    
Medline Journal Info:
Nlm Unique ID:  2985088R     Medline TA:  J Mol Biol     Country:  England    
Other Details:
Languages:  eng     Pagination:  69-78     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Cell Line
Cell Line, Transformed
Enzyme-Linked Immunosorbent Assay
Gene Expression Regulation, Enzymologic
Glycosylation
HT29 Cells
Herpesvirus 4, Human / metabolism
Humans
Immunoglobulin A / biosynthesis*
Lectins / metabolism
Leukocytes, Mononuclear / enzymology
RNA, Messenger / genetics,  metabolism
Reverse Transcription / genetics
Sialyltransferases / genetics,  metabolism*
Grant Support
ID/Acronym/Agency:
DE13694/DE/NIDCR NIH HHS; DK078244/DK/NIDDK NIH HHS; DK47322/DK/NIDDK NIH HHS; DK61525/DK/NIDDK NIH HHS; DK64400/DK/NIDDK NIH HHS; DK71802/DK/NIDDK NIH HHS; M01 RR000032-46/RR/NCRR NIH HHS; M01 RR000211-41/RR/NCRR NIH HHS; M01 RR00032/RR/NCRR NIH HHS; M01 RR00211/RR/NCRR NIH HHS; P01 DK061525-019001/DK/NIDDK NIH HHS; R01 DE013694/DE/NIDCR NIH HHS; R01 DE013694-05/DE/NIDCR NIH HHS; R01 DK071802/DK/NIDDK NIH HHS; R01 DK071802-01A1/DK/NIDDK NIH HHS; R01 DK078244/DK/NIDDK NIH HHS; R01 DK078244-01/DK/NIDDK NIH HHS; R24 DK064400/DK/NIDDK NIH HHS; R24 DK064400-019002/DK/NIDDK NIH HHS
Chemical
Reg. No./Substance:
0/Immunoglobulin A; 0/Lectins; 0/RNA, Messenger; EC 2.4.99.-/CMP-acetylneuraminyl N-acetylgalactosaminyl-IgA1 alpha2,6-sialyltransferase, human; EC 2.4.99.-/Sialyltransferases; EC 2.4.99.-/galactosyl-1-3-N-acetylgalactosaminyl-specific 2,6-sialyltransferase; EC 2.4.99.1/beta-D-galactoside alpha 2-6-sialyltransferase; EC 2.4.99.3/CMP-N-acetylneuraminate-alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase
Comments/Corrections

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