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Volume 272, Number 29, Issue of July 18, 1997 pp. 18033-18037
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

Hsp70 Prevents Activation of Stress Kinases
A NOVEL PATHWAY OF CELLULAR THERMOTOLERANCE

(Received for publication, March 14, 1997, and in revised form, April 17, 1997)

Vladimir L. Gabai ^§ , Anatoli B. Meriin , Dick D. Mosser , A. W. Caron , Sophia Rits , Victor I. Shifrin ^** and Michael Y. Sherman

From the  Boston Biomedical Research Institute, Boston, Massachusetts 02114, the ^§ Medical Radiology Research Center, 249020 Obninsk, Russia,  Biotechnology Research Institute, Montreal H4P 2R2, Quebec, Canada, and the ^** Dana Farber Cancer Institute, Boston, Massachusetts 02115

Harmful conditions including heat shock, oxidative stress, UV, and so forth cause programmed cell death, whose triggering requires activation of the Jun N-terminal kinase, JNK. High levels of Hsp72, a heat-inducible member of Hsp70 family, protect cells against a variety of stresses by a mechanism that is unclear at present. Here we report that elevated levels of Hsp72 inhibit a signal transduction pathway leading to programmed cell death by preventing stress-induced activation of JNK. Stress-induced activation of another stress-kinase, p38 (HOG1), is also blocked when the level of Hsp72 is increased. Similarly, addition of a purified recombinant Hsp72 to a crude cell lysate reduced p38 kinase activation, while depletion of the whole family of Hsp70 proteins with a monoclonal antibody enhanced such activation. In addition, we have found that accumulation of abnormal proteins in cells upon incubation with amino acid analogs causes activation of JNK and p38 kinases, which can be prevented by overproduction of Hsp72. Taken together, these data suggest that, in regulation of JNK and p38 kinases, Hsp70 serves as a "sensor" of the build-up of abnormal proteins after heat shock and other stresses. The inhibitory effect of an increased level of Hsp70 on JNK appears to be a major contributor to acquired thermotolerance in mammalian cells.

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				M. A. Miller, S. E. McGowan, K. R. Gantt, M. Champion, S. L. Novick, K. A. Andersen, C. J. Bacchi, N. Yarlett, B. E. Britigan, and M. E. Wilson Inducible Resistance to Oxidant Stress in the Protozoan Leishmania chagasi J. Biol. Chem., October 20, 2000; 275(43): 33883 - 33889. [Abstract] [Full Text] [PDF]

				D. C. H. Ng and M. A. Bogoyevitch The Mechanism of Heat Shock Activation of ERK Mitogen-activated Protein Kinases in the Interleukin 3-dependent ProB Cell Line BaF3 J. Biol. Chem., December 22, 2000; 275(52): 40856 - 40866. [Abstract] [Full Text] [PDF]

				V. L. Gabai, A. B. Meriin, J. A. Yaglom, J. Y. Wei, D. D. Mosser, and M. Y. Sherman Suppression of Stress Kinase JNK Is Involved in HSP72-mediated Protection of Myogenic Cells from Transient Energy Deprivation. HSP72 ALLEVIATES THE STRESS-INDUCED INHIBITION OF JNK DEPHOSPHORYLATION J. Biol. Chem., November 22, 2000; 275(48): 38088 - 38094. [Abstract] [Full Text] [PDF]

				N. R. Madamanchi, S. Li, C. Patterson, and M. S. Runge Thrombin Regulates Vascular Smooth Muscle Cell Growth and Heat Shock Proteins via the JAK-STAT Pathway J. Biol. Chem., May 25, 2001; 276(22): 18915 - 18924. [Abstract] [Full Text] [PDF]

				G. A. Shinder, M.-C. Lacourse, S. Minotti, and H. D. Durham Mutant Cu/Zn-Superoxide Dismutase Proteins Have Altered Solubility and Interact with Heat Shock/Stress Proteins in Models of Amyotrophic Lateral Sclerosis J. Biol. Chem., April 13, 2001; 276(16): 12791 - 12796. [Abstract] [Full Text] [PDF]

				K. F. Winklhofer, A. Reintjes, M. C. Hoener, R. Voellmy, and J. Tatzelt Geldanamycin Restores a Defective Heat Shock Response in Vivo J. Biol. Chem., November 21, 2001; 276(48): 45160 - 45167. [Abstract] [Full Text] [PDF]

				C.-Y. Li, J.-S. Lee, Y.-G. Ko, J.-I. Kim, and J.-S. Seo Heat Shock Protein 70 Inhibits Apoptosis Downstream of Cytochrome c Release and Upstream of Caspase-3 Activation J. Biol. Chem., August 11, 2000; 275(33): 25665 - 25671. [Abstract] [Full Text] [PDF]

				J. G. Kiang, S. C. Kiang, Y.-T. Juang, and G. C. Tsokos Nomega -nitro-L-arginine inhibits inducible HSP-70 via Ca2+, PKC, and PKA in human intestinal epithelial T84 cells Am J Physiol Gastrointest Liver Physiol, March 1, 2002; 282(3): G415 - G423. [Abstract] [Full Text] [PDF]