N-Glycosylation pattern of recombinant human CD82 (KAI1), a tumor-associated membrane protein.

Abstract:

: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, (α-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.

journal_name

J Proteomics

journal_title

Journal of proteomics

authors

Wang H,Zhang W,Zhao J,Zhang L,Liu M,Yan G,Yao J,Yu H,Yang P

doi

10.1016/j.jprot.2011.11.013

subject

Has Abstract

pub_date

2012-02-02 00:00:00

pages

1375-85

issue

4

eissn

1874-3919

issn

1876-7737

pii

S1874-3919(11)00638-5

journal_volume

75

pub_type

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