Nakaki T, Deans R J, Lee A S
Department of Biochemistry, Norris Cancer Research Institute, University of Southern California School of Medicine, Los Angeles 90033-0800.
Mol Cell Biol. 1989 May;9(5):2233-8. doi: 10.1128/mcb.9.5.2233-2238.1989.
The 78,000-dalton glucose-regulated protein (GRP78) is a stress-inducible protein localized in the endoplasmic reticulum. It has been identified as the immunoglobulin heavy-chain-binding protein. We report here a high level of GRP78 expression in a B-cell myeloma line, NS-1, which produces only kappa light-chain proteins but is unable to secrete them. GRP78 transcription was enhanced in NS-1 cells, resulting in higher levels of GRP78 mRNA and protein than in non-immunoglobulin-producing cells. Furthermore, the nonsecreted light chains in NS-1 cells were found in specific association with GRP78. We hypothesize that in nonsecreting lymphoid cells, the presence of free, unassembled light chains in the endoplasmic reticulum could result in increased transcription of the GRP78 gene and that GRP78 can also bind to immunoglobulin light chains.
78000道尔顿的葡萄糖调节蛋白(GRP78)是一种定位于内质网的应激诱导蛋白。它已被鉴定为免疫球蛋白重链结合蛋白。我们在此报告,在一种B细胞骨髓瘤细胞系NS-1中GRP78表达水平很高,该细胞系仅产生κ轻链蛋白但无法分泌它们。GRP78转录在NS-1细胞中增强,导致GRP78 mRNA和蛋白水平高于非免疫球蛋白产生细胞。此外,发现NS-1细胞中未分泌的轻链与GRP78特异性结合。我们推测,在内质网中存在游离、未组装的轻链的非分泌性淋巴细胞中,可能会导致GRP78基因转录增加,并且GRP78也能与免疫球蛋白轻链结合。