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.
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Acknowledgements
We wish to thank the Department of Radiation Oncology for their continued support. This work was supported by the National Institutes of Health grant R01CA176326 (SKC).
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Okusha, Y., Calderwood, S.K. (2023). Transfection and Thermotolerance Methods for Analysis of miR-570 Targeting the HSP Chaperone Network. In: Calderwood, S.K., Prince, T.L. (eds) Chaperones. Methods in Molecular Biology, vol 2693. Humana, New York, NY. https://doi.org/10.1007/978-1-0716-3342-7_6
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DOI: https://doi.org/10.1007/978-1-0716-3342-7_6
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