Journal
CELLULAR IMMUNOLOGY
Volume 222, Issue 2, Pages 97-104Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/S0008-8749(03)00115-1
Keywords
chaperokine; heat shock proteins; interferon-gamma; proteasome
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Funding
- NCI NIH HHS [R01 CA091889-02] Funding Source: Medline
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In this study, we demonstrate that the pro-inflammatory cytokine interferon-gamma (IFN-gamma) induces the active release of the constitutive form of the 70-kDa heat shock protein (HSC70) from K562 erythroleukemic cells. Treatment of K562 cells with IFN-gamma induced the upregulation of the inducible form of the 70-kDa heat shock protein (HSP70), but not the constitutive form of HSC70 within the cytosol, in a proteasome-dependent manner. In addition, IFN-gamma induced the downregulation of surface-bound HSC70, but did not significantly alter surface-bound HSP70 expression. These findings indicate that HSC70 can be actively released from tumor cells and is indicative of a previously unknown mechanism by which immune modulators stimulate the release of intracellular HSC70. This mechanism may account for the potent chaperokine activity of heat shock proteins recently observed during heat shock protein-based immunotherapy against a variety of cancers. (C) 2003 Elsevier Science (USA). All rights reserved.
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