title: 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.
authors: Institutes of Biomedical Sciences, Fudan University, Shanghai 200032, China.
authors: Hong
authors: H
authors: Wang
authors: Wei
authors: W
authors: Zhang
authors: Jian
authors: J
authors: Zhao
authors: Lei
authors: L
authors: Zhang
authors: Mingqi
authors: M
authors: Liu
authors: Guoquan
authors: G
authors: Yan
authors: Jun
authors: J
authors: Yao
authors: Hongxiu
authors: H
authors: Yu
authors: Pengyuan
authors: P
authors: Yang
mesh_terms: D000595:Amino Acid Sequence; D002462:Cell Membrane / Q000378:metabolism*; D002853:Chromatography, Liquid / Q000379:methods; D015972:Gene Expression Regulation, Neoplastic; D006031:Glycosylation; D057809:HEK293 Cells; D006801:Humans; D051861:Kangai-1 Protein / Q000378:metabolism*; D037102:Lectins / Q000737:chemistry; D013058:Mass Spectrometry / Q000379:methods; D008565:Membrane Proteins / Q000378:metabolism*; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D009362:Neoplasm Metastasis; D010447:Peptide Hydrolases / Q000737:chemistry; D011134:Polysaccharides / Q000737:chemistry; D040901:Proteomics / Q000379:methods; D011994:Recombinant Proteins / Q000737:chemistry*
chemical_list: D051861:Kangai-1 Protein; D037102:Lectins; D008565:Membrane Proteins; D011134:Polysaccharides; D011994:Recombinant Proteins; D010447:Peptide Hydrolases