Munro S, Pelham H R
Cell. 1986 Jul 18;46(2):291-300. doi: 10.1016/0092-8674(86)90746-4.
We have characterized a cDNA clone that encodes a protein related to the 70 kd heat shock protein, but is expressed in normal rat liver. This protein has a hydrophobic leader and is secreted into the endoplasmic reticulum. We show that it is identical with two previously described proteins: GRP78, whose synthesis is induced by glucose starvation, and BiP, which is found bound to immunoglobulin heavy chains in pre-B cells. This protein, which is abundant in antibody-secreting cells, can be released from heavy chains by ATP, a reaction analogous to the release of hsp70 from heat shocked nuclear structures. We propose a specific role for this protein in the assembly of secreted and membrane-bound proteins.
我们鉴定了一个编码与70kd热休克蛋白相关蛋白质的cDNA克隆，但该蛋白在正常大鼠肝脏中表达。这种蛋白质有一个疏水前导序列，并分泌到内质网中。我们发现它与两种先前描述的蛋白质相同：GRP78，其合成由葡萄糖饥饿诱导；以及BiP，它存在于前B细胞中与免疫球蛋白重链结合。这种在抗体分泌细胞中丰富的蛋白质可以通过ATP从重链上释放出来，这一反应类似于热休克核结构中hsp70的释放。我们提出这种蛋白质在分泌蛋白和膜结合蛋白的组装中具有特定作用。
