Literature DB >> 10562718

The neuroprotective potential of heat shock protein 70 (HSP70).

M A Yenari1, R G Giffard, R M Sapolsky, G K Steinberg.   

Abstract

In response to many metabolic disturbances and injuries, including stroke, neurodegenerative disease, epilepsy and trauma, the cell mounts a stress response with induction of a variety of proteins, most notably the 70-kDa heat shock protein (HSP70). Whether stress proteins are neuroprotective has been hotly debated, as these proteins might be merely an epiphenomenon unrelated to cell survival. Only recently, with the availability of transgenic animals and gene transfer, has it become possible to overexpress the gene encoding HSP70 to test directly the hypothesis that stress proteins protect cells from injury. A few groups have now shown that overproduction of HSP70 leads to protection in several different models of nervous system injury. This review will cover these studies, along with the potential mechanisms by which HSP70 might mediate cellular protection.

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Year:  1999        PMID: 10562718     DOI: 10.1016/s1357-4310(99)01599-3

Source DB:  PubMed          Journal:  Mol Med Today        ISSN: 1357-4310


  50 in total

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2.  Administration of Hsp70 in vivo inhibits motor and sensory neuron degeneration.

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Journal:  Cell Stress Chaperones       Date:  2004-03       Impact factor: 3.667

Review 3.  The kinder side of killer proteases: caspase activation contributes to neuroprotection and CNS remodeling.

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4.  Astrocyte targeted overexpression of Hsp72 or SOD2 reduces neuronal vulnerability to forebrain ischemia.

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5.  Cloning HSP70 and HSP90 genes of kaluga (Huso dauricus) and the effects of temperature and salinity stress on their gene expression.

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6.  Expression profiling of p53-target genes in copper-mediated neuronal apoptosis.

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7.  Bag1 is essential for differentiation and survival of hematopoietic and neuronal cells.

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8.  Genome-wide transcriptome profiling of region-specific vulnerability to oxidative stress in the hippocampus.

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9.  Brain distribution of carboxy terminus of Hsc70-interacting protein (CHIP) and its nuclear translocation in cultured cortical neurons following heat stress or oxygen-glucose deprivation.

Authors:  Lauren G Anderson; Rick B Meeker; Winona E Poulton; David Y Huang
Journal:  Cell Stress Chaperones       Date:  2009-12-02       Impact factor: 3.667

10.  Luteal serum BDNF and HSP70 levels in women with premenstrual dysphoric disorder.

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