Effect of Heat Shock on Susceptibility of Normal Lymphoblasts and of a Heat Shock Protein 70‐Defective Tumour Cell Line to Cytotoxic T Lymphocytes <i>In Vitro</i>

Geginat, Gernot; Heine, Lutz; Günther, Eberhard

doi:10.1111/j.1365-3083.1993.tb02559.x

Cited by 8 publications

(10 citation statements)

References 22 publications

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“…1B. Heat shock of 1 h at 42°C or of 30 min at 44°C followed by a 6-h recovery period induced resistance to lysis, confirming data reported earlier (6). Y3 cells are Hsp70 defective and do not express Hsp70-1 and Hsp70-2 transcripts or protein after both heat shock protocols, whereas the activity of the constitutively expressed Hsc70 gene can be detected at the RNA and protein level (Fig.…”

Section: Heat Shock-induced Resistance To Ctl In Hsp70-defective Y3 Csupporting

confidence: 78%

“…After heat shock, these cells become resistant to the cytotoxic effect of alloreactive CTL (6). We now show that Hsp70 is able to prevent the induction of the resistant phenotype.…”

Section: Discussionmentioning

confidence: 89%

“…In addition, in cold target inhibition experiments Y3 cells made resistant by heat shock were as effective as nonresistant cells (Ref. 6 and our unpublished observations). A decrease of MHC class I molecules has been described to occur in some human melanoma cell lines after long and severe heat shock treatment without effect on susceptibility to NK cell cytotoxicity (25).…”

Section: Discussionmentioning

confidence: 99%

“…Suppression of glucose-regulated protein 78 (Grp78), a member of the Hsp70 family, has been demonstrated to eliminate stress-induced resistance of a fibrosarcoma cell line to CTL (9) and also to inhibit tumor progression in vivo (10). We have described heat shock-induced resistance to CTL in the rat myeloma cell line Y3 (6). Y3 cells are unable to express the major heat shock-inducible Hsp70 protein encoded by the MHC-linked Hsp70-1 and Hsp70-2 genes, indicating that Hsp70 is not indispensable for heat shock-induced resistance to occur.…”

mentioning

confidence: 99%

“…n several cell lines heat shock has been shown to induce resistance to cytotoxic immune mechanisms mediated by TNF-␣ (1-5), CTL (4,6), or monocytes (1). Heat shockinduced resistance has been assigned to the expression of heat shock proteins (Hsps) 3 and explained by their function as molecular chaperones.…”

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confidence: 99%

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Heat Shock Protein 70 Is Able to Prevent Heat Shock-Induced Resistance of Target Cells to CTL

Dressel

Elsner

Quentin

et al. 2000

The Journal of Immunology

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Heat shock or transfection with heat shock protein 70 (Hsp70) genes has been shown to protect tumor cell lines against immune mechanisms of cytotoxicity. We have reported previously that heat shock confers resistance to CTL in the rat myeloma cell line Y3 that is Hsp70 defective. Evidence is now presented that Hsp70 is able to prevent the induction of the resistant phenotype. In Con A-stimulated lymphocytes and in lymphocyte × Y3 somatic cell hybrid clones a severe, non-Hsp70-inducing heat shock elicits resistance to CTL in contrast to a heat shock that results in Hsp70 expression. Thus, Hsp70 expression appears to be negatively associated with the development of resistance. Furthermore, loading of Y3 cells with recombinant Hsp70 protein before heat shock is able to prevent resistance. Because apoptosis induced in Y3 cells by heat shock is not affected, Hsp70 appears to interfere selectively with the CTL-induced lethal pathway that is found to be calcium but not caspase dependent. It is suggested that after heat shock Hsp70 enhances the CTL-induced apoptotic pathway by chaperoning certain proteins in the target cell that are involved in the execution of cell death. Thus, although shown to confer protection against many cytotoxic mechanisms, Hsp70 does not appear to be generally cytoprotective. This observation could also be of relevance when interpreting the effectiveness of tumor immunity.

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Section: Heat Shock-induced Resistance To Ctl In Hsp70-defective Y3 Csupporting

confidence: 78%

“…After heat shock, these cells become resistant to the cytotoxic effect of alloreactive CTL (6). We now show that Hsp70 is able to prevent the induction of the resistant phenotype.…”

Section: Discussionmentioning

confidence: 89%

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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Heat Shock Protein 70 Is Able to Prevent Heat Shock-Induced Resistance of Target Cells to CTL

Dressel

Elsner

Quentin

et al. 2000

The Journal of Immunology

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Enhanced susceptibility to cytotoxic T lymphocytes without increase of MHC class I antigen expression after conditional overexpression of heat shock protein 70 in target cells

et al. 1999

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Antigenic peptides have been found associated with heat shock proteins (HSP) including cytoplasmic HSP70 and heat shock cognate protein 70 as well as the endoplasmic reticulum‐resident glucose‐regulated protein 94. Recently, HSP70 transfection has been reported to increase MHC class I cell surface expression and antigen presentation on mouse melanoma B16 cells (Wells et al., Int. Immunol. 1998. 10: 609). To analyze the effect of HSP70 on MHC class I cell surface expression and lysability of target cells we transfected a human melanoma cell line with the rat Hsp70‐1 gene using the Tet‐On system for conditional overexpression of HSP70. Induction of HSP70 did not increase cell surface expression of HLA class I molecules in general or individual HLA‐A and B antigens in particular. Nonetheless, induction of HSP70 enhanced susceptibility of these cells to lysis by allospecific CTL. The same effect was observed using an HLA‐A2‐restricted tyrosinase‐specific CTL clone after pulsing the tyrosinase‐negative target cells with the specific peptide. Thus, HSP70 induction can increase killing by CTL without affecting MHC class I cell surface expression or antigen processing. This effect of HSP70 appears to be different from the commonly found protection exerted by HSP70 against stress like heat shock, and might be mediated by improving CTL‐induced apoptosis.

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Reduced Susceptibility of Electroporated Tumor Cell Lines to Killing by Cytotoxic Lymphocytes

Dressel

Baraki

Langer

et al. 1998

Biochemical and Biophysical Research Communications

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Effect of Heat Shock on Susceptibility of Normal Lymphoblasts and of a Heat Shock Protein 70‐Defective Tumour Cell Line to Cytotoxic T Lymphocytes In Vitro

Cited by 8 publications

References 22 publications

Heat Shock Protein 70 Is Able to Prevent Heat Shock-Induced Resistance of Target Cells to CTL

Heat Shock Protein 70 Is Able to Prevent Heat Shock-Induced Resistance of Target Cells to CTL

Enhanced susceptibility to cytotoxic T lymphocytes without increase of MHC class I antigen expression after conditional overexpression of heat shock protein 70 in target cells

Reduced Susceptibility of Electroporated Tumor Cell Lines to Killing by Cytotoxic Lymphocytes

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