CD91 is a common receptor for heat shock proteins gp96, hsp90, hsp70, and calreticulin
CD91 is a common receptor for heat shock proteins gp96, hsp90, hsp70, and calreticulin
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DOI：
10.1016/s1074-7613(01)00111-x
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发表时间：
2001-03-01
期刊：
影响因子：
32.4
通讯作者：
Srivastava, PK
中科院分区：
文献类型：
--
作者：
Basu, S;Binder, RJ;Srivastava, PK
热休克蛋白gp 96和抗原肽的复合物被抗原呈递细胞摄取并由MHC I类分子呈递。为了解释这个过程的不寻常的效率，gp 96的摄取被假定通过最近被鉴定为CD 91的受体发生。我们在这里表明，复合物的肽与热休克蛋白热休克蛋白90，钙网蛋白，热休克蛋白70也采取了巨噬细胞和树突状细胞和重新提出的MHC I类分子。所有的热休克蛋白都利用CD 91受体，尽管有些蛋白彼此之间没有同源性。gp 96-伴侣肽的摄取后加工需要蛋白酶体和与抗原加工相关的转运蛋白，利用经典的内源性抗原呈递途径。
Complexes of the heat shock protein gp96 and antigenic peptides are taken up by antigen-presenting cells and presented by MHC class I molecules. In order to explain the unusual efficiency of this process, the uptake of gp96 had been postulated to occur through a receptor, identified recently as CD91. We show here that complexes of peptides with heat shock proteins hsp90, calreticulin, and hsp70 are also taken up by macrophages and dendritic cells and re-presented by MHC class I molecules. All heat shock proteins utilize the CD91 receptor, even though some of the proteins have no homology with each other. Postuptake processing of gp96-chaperoned peptides requires proteasomes and the transporters associated with antigen processing, utilizing the classical endogenous antigen presentation pathway.