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Stress–inducible responses and heat shock proteins: New pharmacologic targets for cytoprotection

Nature Biotechnology volume 16, pages 833–838 (1998)Cite this article

Abstract

Molecular chaperones protect proteins against environmental and physiologic stress and from the deleterious consequences of an imbalance in protein homeostasis. Many of these stresses, if prolonged, result in defective development and pathologies associated with a diverse array of diseases due to tissue injury and repair including stroke, myocardial reperfusion damage, ischemia, cancer, amyloidosis, and other neurodegenerative diseases. We discuss the molecular nature of the stress signals, the mechanisms that underlie activation of the heat shock response, the role of heat shock proteins as cytoprotective molecules, and strategies for pharmacologically active molecules as regulators of the heat shock response.

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  1. Richard I. Morimoto: Corresponding author (e-mail: r-morimoto@nwu.edu).

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  1. Department of Biochemistry, Molecular Biology and Cell Biology, Rice Institute for Biomedical Research, Northwestern University, Evanston, IL, 60208

    Richard I. Morimoto

  2. Department of Biology, University of Rome, Tor Vergata and Institute of Experimental Medicine, CNR, 00133, Rome, Italy

    M.Gabriella Santoro

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Morimoto, R., Santoro, M. Stress–inducible responses and heat shock proteins: New pharmacologic targets for cytoprotection. Nat Biotechnol 16, 833–838 (1998). https://doi.org/10.1038/nbt0998-833

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