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- W4313351489 startingPage "140.6" @default.
- W4313351489 abstract "Abstract Heat shock proteins (HSPs), such as gp96, harvested from cancer cells elicit potent anti-tumor immunity in mice and in patients with cancer. HSPs in the extracellular environment, released by cells or introduced through vaccination, are taken up by antigen presenting cells of the immune system, which allows for cross-presentation of the HSP-chaperoned peptides to T-cells. The goal of this study is to identify the subset(s) of cells that sample HSPs in vivo prior to initiating T cell responses. By vaccinating mice with fluorescent-labeled gp96, cells in the draining lymph node (dLN) that engage extracellular HSPs have been explored in a time and dose dependent manner. Our results show that CD4+CD11b+ cells are the predominant cells that internalized the HSP in the subcapsular region of the dLN while CD11c+CD8+ cells, which have been shown by other groups to be the major cross-priming dendritic cells, did not significantly internalize the HSP at any time points. Other CD11c+ cells did not appreciably internalize HSP until 24+ hours after. Internalization corresponded to higher CD91 expression by the CD4+CD11b+ cell subset. The functional capabilities of the CD4+CD11b+ and CD11c+ cells in T cell priming are examined. These studies illustrate how HSPs act to alert the immune system to cellular damage and will be useful for optimizing HSP-based vaccination regimes by identifying possible cellular targets." @default.
- W4313351489 created "2023-01-06" @default.
- W4313351489 creator A5034098296 @default.
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- W4313351489 date "2013-05-01" @default.
- W4313351489 modified "2023-10-14" @default.
- W4313351489 title "Cellular sentinels for heat shock protein-peptide complexes in vivo. (P4270)" @default.
- W4313351489 doi "https://doi.org/10.4049/jimmunol.190.supp.140.6" @default.
- W4313351489 hasPublicationYear "2013" @default.
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