Hsp70 and its molecular role in nervous system diseases
- PMID: 21403864
- PMCID: PMC3049350
- DOI: 10.1155/2011/618127
Hsp70 and its molecular role in nervous system diseases
Abstract
Heat shock proteins (HSPs) are induced in response to many injuries including stroke, neurodegenerative disease, epilepsy, and trauma. The overexpression of one HSP in particular, Hsp70, serves a protective role in several different models of nervous system injury, but has also been linked to a deleterious role in some diseases. Hsp70 functions as a chaperone and protects neurons from protein aggregation and toxicity (Parkinson disease, Alzheimer disease, polyglutamine diseases, and amyotrophic lateral sclerosis), protects cells from apoptosis (Parkinson disease), is a stress marker (temporal lobe epilepsy), protects cells from inflammation (cerebral ischemic injury), has an adjuvant role in antigen presentation and is involved in the immune response in autoimmune disease (multiple sclerosis). The worldwide incidence of neurodegenerative diseases is high. As neurodegenerative diseases disproportionately affect older individuals, disease-related morbidity has increased along with the general increase in longevity. An understanding of the underlying mechanisms that lead to neurodegeneration is key to identifying methods of prevention and treatment. Investigators have observed protective effects of HSPs induced by preconditioning, overexpression, or drugs in a variety of models of brain disease. Experimental data suggest that manipulation of the cellular stress response may offer strategies to protect the brain during progression of neurodegenerative disease.
Figures
Similar articles
-
Heat shock proteins and protection of the nervous system.Ann N Y Acad Sci. 2007 Oct;1113:147-58. doi: 10.1196/annals.1391.032. Epub 2007 Jul 26. Ann N Y Acad Sci. 2007. PMID: 17656567 Review.
-
Antiapoptotic and anti-inflammatory mechanisms of heat-shock protein protection.Ann N Y Acad Sci. 2005 Aug;1053:74-83. doi: 10.1196/annals.1344.007. Ann N Y Acad Sci. 2005. PMID: 16179510 Review.
-
Oxidative stress, mitochondrial dysfunction and cellular stress response in Friedreich's ataxia.J Neurol Sci. 2005 Jun 15;233(1-2):145-62. doi: 10.1016/j.jns.2005.03.012. J Neurol Sci. 2005. PMID: 15896810 Review.
-
Heat shock proteins and neuroprotection.Adv Exp Med Biol. 2002;513:281-99. doi: 10.1007/978-1-4615-0123-7_10. Adv Exp Med Biol. 2002. PMID: 12575825 Review.
-
Positive or negative involvement of heat shock proteins in multiple sclerosis pathogenesis: an overview.J Neuropathol Exp Neurol. 2014 Dec;73(12):1092-106. doi: 10.1097/NEN.0000000000000136. J Neuropathol Exp Neurol. 2014. PMID: 25383635 Review.
Cited by
-
Polyglutamine (PolyQ) Diseases: Navigating the Landscape of Neurodegeneration.ACS Chem Neurosci. 2024 Aug 7;15(15):2665-2694. doi: 10.1021/acschemneuro.4c00184. Epub 2024 Jul 12. ACS Chem Neurosci. 2024. PMID: 38996083 Free PMC article. Review.
-
Structural insights into GrpEL1-mediated nucleotide and substrate release of human mitochondrial Hsp70.bioRxiv [Preprint]. 2024 May 13:2024.05.10.593630. doi: 10.1101/2024.05.10.593630. bioRxiv. 2024. PMID: 38798347 Free PMC article. Preprint.
-
Chaperone Hsp70 helps Salmonella survive infection-relevant stress by reducing protein synthesis.PLoS Biol. 2024 Apr 4;22(4):e3002560. doi: 10.1371/journal.pbio.3002560. eCollection 2024 Apr. PLoS Biol. 2024. PMID: 38574172 Free PMC article.
-
Cell-Permeable HSP70 Protects Neurons and Astrocytes Against Cell Death in the Rotenone-Induced and Familial Models of Parkinson's Disease.Mol Neurobiol. 2024 Oct;61(10):7785-7795. doi: 10.1007/s12035-024-04077-9. Epub 2024 Mar 2. Mol Neurobiol. 2024. PMID: 38429623 Free PMC article.
-
Glucose transporter 1 deficiency, AMP-activated protein kinase activation and immune dysregulation in autism spectrum disorder: Novel biomarker sources for clinical diagnosis.Saudi J Biol Sci. 2023 Dec;30(12):103849. doi: 10.1016/j.sjbs.2023.103849. Epub 2023 Oct 20. Saudi J Biol Sci. 2023. PMID: 38020228 Free PMC article.
References
-
- Anfinsen CB. Principles that govern the folding of protein chains. Science. 1973;181(4096):223–230. - PubMed
-
- Ellis RJ. The molecular chaperone concept. Seminars in Cell Biology. 1990;1(1):1–9. - PubMed
-
- Georgopoulos C, Welch WJ. Role of the major heat shock proteins as molecular chaperones. Annual Review of Cell Biology. 1993;9:601–634. - PubMed
-
- Hartl FU. Molecular chaperones in cellular protein folding. Nature. 1996;381(6583):571–580. - PubMed
LinkOut - more resources
Full Text Sources
Other Literature Sources
Research Materials