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- W2037299442 abstract "gp96 (GRP94) elicits antigen-presenting cell (APC) activation and can direct peptides into the cross- presentation pathways of APC. These responses arise through interactions of gp96 with Toll-like (APC activation) and endocytic (cross-presentation) receptors of APC. Previously, CD91, the alpha2-macroglobulin receptor, was identified as the heat shock/chaperone protein receptor of APC. Recent data indicates, however, that inhibition of CD91 ligand binding does not alter gp96 recognition and uptake. Furthermore, CD91 expression is not itself sufficient for gp96 binding and internalization. We now report that scavenger receptor class-A (SR-A), a prominent scavenger receptor of macrophages and dendritic cells, serves a primary role in gp96 and calreticulin recognition and internalization. gp96 internalization and peptide re-presentation are inhibited by the SR-A inhibitory ligand fucoidin, although fucoidin was without effect on alpha2-macroglobulin binding or uptake. Ectopic expression of SR-A in HEK 293 cells yielded gp96 recognition and uptake activity. In addition, macrophages derived from SR-A-/- mice were substantially impaired in gp96 binding and uptake. These data identify new roles for SR-A in the regulation of cellular responses to heat shock proteins." @default.
- W2037299442 created "2016-06-24" @default.
- W2037299442 creator A5009018441 @default.
- W2037299442 creator A5020706311 @default.
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- W2037299442 creator A5059378741 @default.
- W2037299442 creator A5073306910 @default.
- W2037299442 creator A5090928660 @default.
- W2037299442 date "2003-11-17" @default.
- W2037299442 modified "2023-09-25" @default.
- W2037299442 title "Scavenger receptor-A mediates gp96/GRP94 and calreticulin internalization by antigen-presenting cells" @default.
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