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Supplementary Figures 1-7, Table 1 from Peptides and Aptamers Targeting HSP70: A Novel Approach for Anticancer Chemotherapy
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posted on 2023-03-30, 20:12 authored by Anne-Laure Rérole, Jessica Gobbo, Aurelie De Thonel, Elise Schmitt, Jean Paul Pais de Barros, Arlette Hammann, David Lanneau, Eric Fourmaux, Oleg Deminov, Olivier Micheau, Laurent Lagrost, Pierre Colas, Guido Kroemer, Carmen GarridoSupplementary Figures 1-7, Table 1 from Peptides and Aptamers Targeting HSP70: A Novel Approach for Anticancer Chemotherapy
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ARTICLE ABSTRACT
The inhibition of heat shock protein 70 (HSP70) is an emerging strategy in cancer therapy. Unfortunately, no specific inhibitors are clinically available. By yeast two-hybrid screening, we have identified multiple peptide aptamers that bind HSP70. When expressed in human tumor cells, two among these peptide aptamers—A8 and A17—which bind to the peptide-binding and the ATP-binding domains of HSP70, respectively, specifically inhibited the chaperone activity, thereby increasing the cells' sensitivity to apoptosis induced by anticancer drugs. The 13-amino acid peptide from the variable region of A17 (called P17) retained the ability to specifically inhibit HSP70 and induced the regression of subcutaneous tumors in vivo after local or systemic injection. This antitumor effect was associated with an important recruitment of macrophages and T lymphocytes into the tumor bed. Altogether, these data indicate that peptide aptamers or peptides that target HSP70 may be considered as novel lead compounds for cancer therapy. Cancer Res; 71(2); 484–95. ©2011 AACR.Usage metrics
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CarcinogenesisAnimal models of carcinogenesisTumor initiation and promotionCell Death And SenescenceEffectors of apoptosisChemotherapyCombination chemotherapyDrug MechanismsDrug-mediated stimulation of cell death pathwaysDrug TargetsGastrointestinal CancersColorectal cancerImmunologyTumor resistance to immune responseProgression, Invasion & MetastasisTumor progressionSkin CancersSmall Molecule Agents
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