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Heat Shock Protein 70 and Other Heat Shock Proteins in Diseased Retina
2018Heat shock proteins (HSP) belong to a family of stress-induced proteins essential to cell survival. HSP have multiple protective roles through assistance in protein folding, maintaining mitochondrial homeostasis, suppressing proinflammatory cytokines, resisting ischemic damage and protecting cells from apoptotic and necrotic death.
Ting Zhang, Bobak Bahrami, Ling Zhu
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Carbenoxolone, a new inducer of heat shock protein 70
Life Sciences, 2001Heat shock protein 70 (Hsp70) is capable of protecting cells, tissues, organs, and animals from a subsequent, normally lethal heating, as well as from numerous disease states. Therefore, it would be of great therapeutic benefit to discover compounds that are clinically safe yet able to induce Hsp70 in patients.
S, Nagayama +8 more
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Immunolocalization of heat shock protein 70 in bovine spermatozoa
Andrologia, 2004Heat shock protein 70 (HSP70) is part of a superfamily of molecular chaperones, which protect cells from chemical and heat shock. The objectives of this study were to determine the presence of HSP70 in bovine spermatozoa and its subcellular localization during different stages of spermatogenesis.
M, Kamaruddin +4 more
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Journal of Neurochemistry, 1991
Abstract: The expression of strictly inducible hsp70 mRNAs and constitutively expressed hsc70 mRNAs was compared in cerebellum and cerebral cortex of control rats, heat‐shocked rats, and rats made hyperthermic with amphetamine. An hsc70‐specific oligonucleotide probe identified a 2.55‐kb mRNA in cerebellum and cerebral cortex of all rats.
E K, Miller +2 more
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Abstract: The expression of strictly inducible hsp70 mRNAs and constitutively expressed hsc70 mRNAs was compared in cerebellum and cerebral cortex of control rats, heat‐shocked rats, and rats made hyperthermic with amphetamine. An hsc70‐specific oligonucleotide probe identified a 2.55‐kb mRNA in cerebellum and cerebral cortex of all rats.
E K, Miller +2 more
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Heat shock protein 70 expression in skeletal muscle
Biochemical Society Transactions, 1996A, McArdle, M J, Jackson
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