期刊
JOURNAL OF PROTEOMICS
卷 75, 期 4, 页码 1375-1385出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.jprot.2011.11.013
关键词
CD82 (KAI1); Glycosylation; Membrane protein
资金
- National Key Scientific Program of China [2008ZX10208, 2008ZX10207]
- National Science and Technology Key Project of China [2007CB914100, 2006AA02A308, 2011CB910600]
- National Science Foundation of China [20735005, 209750240]
- Shanghai Municipal Natural Science Foundation [11ZR1403800]
- Board of Health of Shanghai Program [C096959]
The membrane glycoprotein CD82 (KAI1) has attracted increasing attention as a suppressor of cell migration, related tumor invasion, as well as metastasis. The glycosylation of CD82 has been shown to be involved in a correlative cell adhesion and motility. However, the N-glycosylation pattern of CD82 has not been described yet. In the current study, a detailed characterization of the recombinant human CD82 N-linked glycosylation pattern was conducted by employing an integrative proteomic and glycomic approach, including glycosidase and protease digestions, glycan permethylation, MS analyses, site-directed mutagenesis, and lectin blots. The results reveal three N-glycosylation sites, and further demonstrate a putative glycosylation site at Asn(157) for the first time. A highly heterogeneous pattern of N-linked glycans is described, which express distinct carbohydrate epitopes, such as bisecting N-acetylglucosamine, (alpha-2,6) N-acetylneuraminic acid, and core fucose. These epitopes are highly associated with various biological functions, including cell adhesion and cancer metastasis, and can possibly influence the anti-cancer inhibition ability of CD82. (C) 2011 Elsevier B.V. All rights reserved.
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