期刊
JOURNAL OF MOLECULAR BIOLOGY
卷 369, 期 1, 页码 69-78出版社
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2007.03.002
关键词
ST6GalNAcII; DAKIKI; IgA nephropathy; IgA1 hinge region; sialylation
资金
- NCRR NIH HHS [M01 RR000032-46, M01 RR000211, M01 RR00211, M01 RR00032, M01 RR000211-41, M01 RR000032] Funding Source: Medline
- NIDCR NIH HHS [R01 DE013694, R01 DE013694-05, DE13694] Funding Source: Medline
- NIDDK NIH HHS [P01 DK061525, DK61525, R01 DK071802-01A1, R56 DK078244, DK71802, R24 DK064400-019002, DK47322, DK078244, DK64400, R01 DK078244-01, R24 DK064400, R01 DK071802, P01 DK061525-019001, R01 DK078244] Funding Source: Medline
Glycosylation defects occur in several human diseases. In IgA nephropathy, IgA1 contains O-glycans that are galactose-deficient and consist mostly of core 1 alpha 2,6 sialylated N-acetylgalactosamine, a configuration suspected to prevent beta 1,3 galactosylation. We confirmed the same aberrancy in IgA1 secreted by the human DAKIKI B cell line. Biochemical assays indicated CMP-NeuAc:GalNAc-IgAl alpha 2,6-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 alpha 2,6-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. (c) 2007 Elsevier Ltd. All rights reserved.
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