期刊
FRONTIERS IN IMMUNOLOGY
卷 3, 期 -, 页码 -出版社
FRONTIERS MEDIA SA
DOI: 10.3389/fimmu.2012.00063
关键词
heat shock proteins; antigen cross presentation; CTL response; scavenger receptor; antigen presenting cells; soluble vs. particulate antigen; anti-cancer vaccine; tumor immunity
类别
资金
- NIH [RO-1CA047407, R01CA119045, RO-1CA094397]
Heat shock proteins (HSPs) are molecular chaperones that bind tumor antigens and mediate their uptake into antigen presenting cells. HSP antigen complexes are then directed toward either the MHC class I pathway through antigen cross presentation or the conventional class II pathway, leading to activation of T cell subsets. Uptake of HSP-chaperoned polypeptides can involve both receptor-mediated and receptor-independent routes, and mechanisms of antigen sorting between the Class I and II pathways after uptake are currently under investigation. The processes involved in internalization of HSP antigen complexes differ somewhat from the mechanisms previously determined for (unchaper-oned) particulate and free soluble antigens. A number of studies show that HSP-facilitated antigen cross presentation requires uptake of the complexes by scavenger receptors (SR) followed by processing in the proteasome, and loading onto MHC class I molecules. In this review we have examined the roles of HSPs and SR in antigen uptake, sorting, processing, cell signaling, and activation of innate and adaptive immunity.
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