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Author Spotlight: Exploring Heat Shock Proteins in Malaria and Tuberculosis Infections
Published on: March 8, 2024
Transfection and Thermotolerance Methods for Analysis of miR-570 Targeting the HSP Chaperone Network
Yuka Okusha1,2, Stuart K Calderwood3
1Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, MA, USA.
Abstract:
Heat shock proteins (HSPs) are key stress proteins induced in cells exposed to proteotoxic insult and are critical for thermotolerance. The dynamic network of chaperone interactions, known as the chaperome, contributes significantly to the proteotoxic cell response and the malignant phenotype in cancer. We identified a potent microRNA, miR-570 that could bind the 3'untranslated regions of multiple HSP mRNAs and inhibit HSP synthesis. Here, we will introduce the transfection and thermotolerance methods for analysis of miR-570 targeting the HSP chaperone network.

