Regulation of survival gene hsp70

Rapid expression of the survival gene, inducible heat shock protein 70 (hsp70), is critical for mounting cytoprotection against severe cellular stress, like elevated temperature. Hsp70 protein chaperones the refolding of heatdenatured peptides to minimize proteolytic degradation as a part of an euka...

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Published inCell stress & chaperones Vol. 17; no. 1; pp. 1 - 9
Main Authors Silver, Jordan Thomas, Noble, Earl G.
Format Journal Article
LanguageEnglish
Published Dordrecht Springer 01.01.2012
Springer Netherlands
Springer Nature B.V
Subjects
Biochemistry
Biomedical and Life Sciences
Biomedicine
Cancer Research
Cell Biology
Gene expression
Gene Expression Regulation
Genes
Heat shock proteins
Heat shock response
Heat stress disorders
HSP70 Heat-Shock Proteins - genetics
HSP70 Heat-Shock Proteins - metabolism
Humans
Immunology
Messenger RNA
Mini Review
MINI REVIEWS
Neurosciences
Protein Processing, Post-Translational
Protein synthesis
RNA, Messenger - metabolism
Shock heating
Skeletal muscle
Heat shock response
Regulation
Exercise
Heat stress
Skeletal muscle
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Abstract Rapid expression of the survival gene, inducible heat shock protein 70 (hsp70), is critical for mounting cytoprotection against severe cellular stress, like elevated temperature. Hsp70 protein chaperones the refolding of heatdenatured peptides to minimize proteolytic degradation as a part of an eukaryotically conserved phenomenon referred to as the heat shock response. The physiologic stress associated with exercise, which can include elevated temperature, mechanical damage, hypoxia, lowered pH, and reactive oxygen species generation, may promote protein unfolding, leading to hsp70 gene expression in skeletal myofibers. Although the pre-transcriptional activation of hsp70 gene expression has been thoroughly reviewed, discussion of downstream hsp70 gene regulation is less extensive. The purpose of this brief review was to examine all levels of hsp70 gene regulation in response to heat stress and exercise with a special focus on skeletal myofibers where data are available. In general, while heat stress represses bulk gene expression, hsp70 mRNA expression is enhanced. Posttranscriptionally, intronless hsp70 mRNA circumvents a host of decay pathways, as well as heat stress-repressed premRNA splicing and nuclear export. Pre-translationally, hsp70 mRNA is excluded from stress granules and preferentially translated during heat stress-repressed global cap-dependent translation. Post-translationally, nascent Hsp70 protein is thermodynamically stable at elevated temperatures, allowing for the commencement of chaperoning activity early after synthesis to attenuate the heat shock response and protect against subsequent injury. This review demonstrates that hsp70 mRNA expression is closely coupled with functional protein translation.
AbstractList Rapid expression of the survival gene, inducible heat shock protein 70 ( hsp70 ), is critical for mounting cytoprotection against severe cellular stress, like elevated temperature. Hsp70 protein chaperones the refolding of heat-denatured peptides to minimize proteolytic degradation as a part of an eukaryotically conserved phenomenon referred to as the heat shock response. The physiologic stress associated with exercise, which can include elevated temperature, mechanical damage, hypoxia, lowered pH, and reactive oxygen species generation, may promote protein unfolding, leading to hsp70 gene expression in skeletal myofibers. Although the pre-transcriptional activation of hsp70 gene expression has been thoroughly reviewed, discussion of downstream hsp70 gene regulation is less extensive. The purpose of this brief review was to examine all levels of hsp70 gene regulation in response to heat stress and exercise with a special focus on skeletal myofibers where data are available. In general, while heat stress represses bulk gene expression, hsp70 mRNA expression is enhanced. Post-transcriptionally, intronless hsp70 mRNA circumvents a host of decay pathways, as well as heat stress-repressed pre-mRNA splicing and nuclear export. Pre-translationally, hsp70 mRNA is excluded from stress granules and preferentially translated during heat stress-repressed global cap-dependent translation. Post-translationally, nascent Hsp70 protein is thermodynamically stable at elevated temperatures, allowing for the commencement of chaperoning activity early after synthesis to attenuate the heat shock response and protect against subsequent injury. This review demonstrates that hsp70 mRNA expression is closely coupled with functional protein translation.
Rapid expression of the survival gene, inducible heat shock protein 70 (hsp70), is critical for mounting cytoprotection against severe cellular stress, like elevated temperature. Hsp70 protein chaperones the refolding of heat-denatured peptides to minimize proteolytic degradation as a part of an eukaryotically conserved phenomenon referred to as the heat shock response. The physiologic stress associated with exercise, which can include elevated temperature, mechanical damage, hypoxia, lowered pH, and reactive oxygen species generation, may promote protein unfolding, leading to hsp70 gene expression in skeletal myofibers. Although the pre-transcriptional activation of hsp70 gene expression has been thoroughly reviewed, discussion of downstream hsp70 gene regulation is less extensive. The purpose of this brief review was to examine all levels of hsp70 gene regulation in response to heat stress and exercise with a special focus on skeletal myofibers where data are available. In general, while heat stress represses bulk gene expression, hsp70 mRNA expression is enhanced. Post-transcriptionally, intronless hsp70 mRNA circumvents a host of decay pathways, as well as heat stress-repressed pre-mRNA splicing and nuclear export. Pre-translationally, hsp70 mRNA is excluded from stress granules and preferentially translated during heat stress-repressed global cap-dependent translation. Post-translationally, nascent Hsp70 protein is thermodynamically stable at elevated temperatures, allowing for the commencement of chaperoning activity early after synthesis to attenuate the heat shock response and protect against subsequent injury. This review demonstrates that hsp70 mRNA expression is closely coupled with functional protein translation.[PUBLICATION ABSTRACT]
Rapid expression of the survival gene, inducible heat shock protein 70 (hsp70), is critical for mounting cytoprotection against severe cellular stress, like elevated temperature. Hsp70 protein chaperones the refolding of heat-denatured peptides to minimize proteolytic degradation as a part of an eukaryotically conserved phenomenon referred to as the heat shock response. The physiologic stress associated with exercise, which can include elevated temperature, mechanical damage, hypoxia, lowered pH, and reactive oxygen species generation, may promote protein unfolding, leading to hsp70 gene expression in skeletal myofibers. Although the pre-transcriptional activation of hsp70 gene expression has been thoroughly reviewed, discussion of downstream hsp70 gene regulation is less extensive. The purpose of this brief review was to examine all levels of hsp70 gene regulation in response to heat stress and exercise with a special focus on skeletal myofibers where data are available. In general, while heat stress represses bulk gene expression, hsp70 mRNA expression is enhanced. Post-transcriptionally, intronless hsp70 mRNA circumvents a host of decay pathways, as well as heat stress-repressed pre-mRNA splicing and nuclear export. Pre-translationally, hsp70 mRNA is excluded from stress granules and preferentially translated during heat stress-repressed global cap-dependent translation. Post-translationally, nascent Hsp70 protein is thermodynamically stable at elevated temperatures, allowing for the commencement of chaperoning activity early after synthesis to attenuate the heat shock response and protect against subsequent injury. This review demonstrates that hsp70 mRNA expression is closely coupled with functional protein translation.
Rapid expression of the survival gene, inducible heat shock protein 70 (hsp70), is critical for mounting cytoprotection against severe cellular stress, like elevated temperature. Hsp70 protein chaperones the refolding of heatdenatured peptides to minimize proteolytic degradation as a part of an eukaryotically conserved phenomenon referred to as the heat shock response. The physiologic stress associated with exercise, which can include elevated temperature, mechanical damage, hypoxia, lowered pH, and reactive oxygen species generation, may promote protein unfolding, leading to hsp70 gene expression in skeletal myofibers. Although the pre-transcriptional activation of hsp70 gene expression has been thoroughly reviewed, discussion of downstream hsp70 gene regulation is less extensive. The purpose of this brief review was to examine all levels of hsp70 gene regulation in response to heat stress and exercise with a special focus on skeletal myofibers where data are available. In general, while heat stress represses bulk gene expression, hsp70 mRNA expression is enhanced. Posttranscriptionally, intronless hsp70 mRNA circumvents a host of decay pathways, as well as heat stress-repressed premRNA splicing and nuclear export. Pre-translationally, hsp70 mRNA is excluded from stress granules and preferentially translated during heat stress-repressed global cap-dependent translation. Post-translationally, nascent Hsp70 protein is thermodynamically stable at elevated temperatures, allowing for the commencement of chaperoning activity early after synthesis to attenuate the heat shock response and protect against subsequent injury. This review demonstrates that hsp70 mRNA expression is closely coupled with functional protein translation.
Author Silver, Jordan Thomas
Noble, Earl G.
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ISSN 1355-8145
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Fri Aug 16 22:41:36 EDT 2024
Wed Sep 25 02:13:51 EDT 2024
Thu Sep 12 21:08:29 EDT 2024
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Sat Dec 16 12:00:38 EST 2023
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Issue 1
Keywords Heat shock response
Regulation
Exercise
Heat stress
Skeletal muscle
Language English
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OpenAccessLink https://doi.org/10.1007/s12192-011-0290-6
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PublicationDate 2012-01-01
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PublicationSubtitle A Comprehensive Journal of Stress Biology and Medicine
PublicationTitle Cell stress & chaperones
PublicationTitleAbbrev Cell Stress and Chaperones
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PublicationYear 2012
Publisher Springer
Springer Netherlands
Springer Nature B.V
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SSID ssj0007771
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SecondaryResourceType review_article
Snippet Rapid expression of the survival gene, inducible heat shock protein 70 (hsp70), is critical for mounting cytoprotection against severe cellular stress, like...
Rapid expression of the survival gene, inducible heat shock protein 70 ( hsp70 ), is critical for mounting cytoprotection against severe cellular stress, like...
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SourceType Open Access Repository
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StartPage 1
SubjectTerms Biochemistry
Biomedical and Life Sciences
Biomedicine
Cancer Research
Cell Biology
Gene expression
Gene Expression Regulation
Genes
Heat shock proteins
Heat shock response
Heat stress disorders
HSP70 Heat-Shock Proteins - genetics
HSP70 Heat-Shock Proteins - metabolism
Humans
Immunology
Messenger RNA
Mini Review
MINI REVIEWS
Neurosciences
Protein Processing, Post-Translational
Protein synthesis
RNA, Messenger - metabolism
Shock heating
Skeletal muscle
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Title Regulation of survival gene hsp70
URI https://www.jstor.org/stable/41412281
https://link.springer.com/article/10.1007/s12192-011-0290-6
https://www.ncbi.nlm.nih.gov/pubmed/21874533
https://www.proquest.com/docview/907041829/abstract/
https://search.proquest.com/docview/907996933
https://pubmed.ncbi.nlm.nih.gov/PMC3227850
Volume 17
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