CHARACTERIZATION OF N-LINKED OLIGOSACCHARIDES OF AN HLA-DR MOLECULE EXPRESSED IN DIFFERENT CELL-LINES
CHARACTERIZATION OF N-LINKED OLIGOSACCHARIDES OF AN HLA-DR MOLECULE EXPRESSED IN DIFFERENT CELL-LINES
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DOI：
10.1042/bj2440433
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发表时间：
1987-06-01
影响因子：
4.1
通讯作者：
CHARRON, DJ
中科院分区：
文献类型：
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作者：
NEEL, D;MERLU, B;CHARRON, DJ
为了确定影响整体膜蛋白糖基化的因素，我们研究了人类主要组织相容性复合体（MHC） II类HLA-DR抗原分子的n -糖基化。在人epstein - barr病毒转化的B细胞系和共转染DR . α的小鼠成纤维细胞系中研究了该糖蛋白。DR。beta。基因。我们观察到hla - dr -抗原的糖基化模式取决于处理发生的细胞系，并与整个细胞糖蛋白的糖基化模式密切相关。此外，当比较分离的。α。-和。beta。-链，在同一分子中注意到差异，表明单个肽主链对糖基化过程的重要性。
In order to determine the factors that influence the glycosylation of an integral membrane protein, we investigated the N-glycosylation of a molecule of the human major histocompatibility complex (MHC) class II, the HLA-DR antigen. This glycoprotein was studied in a human Epstein-Barr-virus-transformed B cell line and in a mouse fibroblastic cell line co-transfected with DR .alpha. and DR .beta. genes. We observed that the HLA-DR-antigen glycosylation pattern depends on the cell line in which processing takes place and is closely related to the glycosylation pattern of the overall cellular glycoproteins. Furthermore, when comparing the glycosylation of the separated .alpha.- and .beta.-chains, differences were noticed within the same molecule, showing the importance of the individual peptide backbone for the glycosylation process.