CD91: a receptor for heat shock protein gp96
CD91: a receptor for heat shock protein gp96
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DOI：
10.1038/77835
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发表时间：
2000-08-01
影响因子：
30.5
通讯作者：
Srivastava, PK
中科院分区：
文献类型：
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作者：
Binder, RJ;Han, DK;Srivastava, PK
抗原提呈细胞（Antigen presenting cells, APCs）可以吸收以热休克蛋白gp96为伴的外源性抗原肽，并通过内源性途径在其主要的组织相容性I类分子上进行再现。这一过程的高效率先前归因于apc上的gp96受体，CD91分子（也称为α(2)-巨球蛋白受体或低密度脂蛋白相关蛋白）在这里被证明是热休克蛋白gp96的细胞表面受体，CD91直接结合gp96，而不是通过CD91的另一个配体。先前已知的CD91配体，α(2)-巨球蛋白，抑制巨噬细胞对gp96伴侣抗原肽的再递呈，CD91抗体也是如此。由于gp96仅存在于细胞内，并且由于坏死细胞而非凋亡细胞死亡而释放，因此我们提出CD91可作为坏死细胞死亡的传感器。
Antigen presenting cells (APCs) can take up exogenous antigenic peptides chaperoned by heat shock protein gp96 and re-present them through the endogenous pathway on their major histocompatibility class I molecules. The high efficiency of this process has been attributed previously to a receptor for gp96 on APCs, The CD91 molecule (also called alpha(2)-macroglobulin receptor or the low density lipoprotein-related protein) is shown here to be a cell surface receptor for the heat shock protein gp96, CD91 binds gp96 directly, rather than through another ligand for CD91. The previously known CD91 ligand, alpha(2)-macroglobulin, inhibits re-presentation of gp96-chaperoned antigenic peptides by macrophages, as do antibodies to CD91. As gp96 is exclusively intracellular and is released as a result of necrotic but not apoptotic cell death, we propose that CD91 acts as a sensor for necrotic cell death.