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Redox regulation in neurodegeneration and longevity: role of the heme oxygenase and HSP70 systems in brain stress tolerance.
Antioxid Redox Signal 2004; 6(5):895-913AR

Abstract

Efficient functioning of maintenance and repair processes seems to be crucial for both survival and physical quality of life. This is accomplished by a complex network of the so-called longevity assurance processes, which are composed of several genes termed "vitagenes," among these, the heat shock system, a highly conserved mechanism responsible for the preservation and repair of cellular macromolecules, such as proteins, RNAs, and DNA. Recent studies have shown that the heat shock response contributes to establishing a cytoprotective state in a wide variety of human diseases, including ischemia and reperfusion damage, inflammation, cancer, as well as metabolic and neurodegenerative disorders. Recently, the involvement of the heme oxygenase (HO) pathway in antidegenerative mechanisms has received considerable attention, as it has been demonstrated that the expression of HO is closely related to that of amyloid precursor protein. HO induction occurs together with the induction of other heat shock proteins during various physiopathological conditions. The vasoactive molecule carbon monoxide and the potent antioxidant bilirubin, products of HO-catalyzed reaction, represent a protective system potentially active against brain oxidative injury. Given the broad cytoprotective properties of the heat shock response, molecules inducing this defense mechanism appear to be possible candidates for novel cytoprotective strategies. Particularly, manipulation of endogenous cellular defense mechanisms, via the heat shock response, through nutritional antioxidants or pharmacological compounds, may represent an innovative approach to therapeutic intervention in diseases causing tissue damage, such as neurodegeneration. Consistently, by maintaining or recovering the activity of vitagenes, it is feasible to delay the aging process and decrease the occurrence of age-related diseases with resulting prolongation of a healthy life span.

Authors+Show Affiliations

Section of Biochemistry and Molecular Biology, Department of Chemistry, Faculty of Medicine, University of Catania, Catania, Italy. calabres@mbox.unict.itNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.
Review

Language

eng

PubMed ID

15345150

Citation

Calabrese, Vittorio, et al. "Redox Regulation in Neurodegeneration and Longevity: Role of the Heme Oxygenase and HSP70 Systems in Brain Stress Tolerance." Antioxidants & Redox Signaling, vol. 6, no. 5, 2004, pp. 895-913.
Calabrese V, Stella AM, Butterfield DA, et al. Redox regulation in neurodegeneration and longevity: role of the heme oxygenase and HSP70 systems in brain stress tolerance. Antioxid Redox Signal. 2004;6(5):895-913.
Calabrese, V., Stella, A. M., Butterfield, D. A., & Scapagnini, G. (2004). Redox regulation in neurodegeneration and longevity: role of the heme oxygenase and HSP70 systems in brain stress tolerance. Antioxidants & Redox Signaling, 6(5), pp. 895-913.
Calabrese V, et al. Redox Regulation in Neurodegeneration and Longevity: Role of the Heme Oxygenase and HSP70 Systems in Brain Stress Tolerance. Antioxid Redox Signal. 2004;6(5):895-913. PubMed PMID: 15345150.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Redox regulation in neurodegeneration and longevity: role of the heme oxygenase and HSP70 systems in brain stress tolerance. AU - Calabrese,Vittorio, AU - Stella,A M Giuffrida, AU - Butterfield,D Allan, AU - Scapagnini,Giovanni, PY - 2004/9/4/pubmed PY - 2005/8/17/medline PY - 2004/9/4/entrez SP - 895 EP - 913 JF - Antioxidants & redox signaling JO - Antioxid. Redox Signal. VL - 6 IS - 5 N2 - Efficient functioning of maintenance and repair processes seems to be crucial for both survival and physical quality of life. This is accomplished by a complex network of the so-called longevity assurance processes, which are composed of several genes termed "vitagenes," among these, the heat shock system, a highly conserved mechanism responsible for the preservation and repair of cellular macromolecules, such as proteins, RNAs, and DNA. Recent studies have shown that the heat shock response contributes to establishing a cytoprotective state in a wide variety of human diseases, including ischemia and reperfusion damage, inflammation, cancer, as well as metabolic and neurodegenerative disorders. Recently, the involvement of the heme oxygenase (HO) pathway in antidegenerative mechanisms has received considerable attention, as it has been demonstrated that the expression of HO is closely related to that of amyloid precursor protein. HO induction occurs together with the induction of other heat shock proteins during various physiopathological conditions. The vasoactive molecule carbon monoxide and the potent antioxidant bilirubin, products of HO-catalyzed reaction, represent a protective system potentially active against brain oxidative injury. Given the broad cytoprotective properties of the heat shock response, molecules inducing this defense mechanism appear to be possible candidates for novel cytoprotective strategies. Particularly, manipulation of endogenous cellular defense mechanisms, via the heat shock response, through nutritional antioxidants or pharmacological compounds, may represent an innovative approach to therapeutic intervention in diseases causing tissue damage, such as neurodegeneration. Consistently, by maintaining or recovering the activity of vitagenes, it is feasible to delay the aging process and decrease the occurrence of age-related diseases with resulting prolongation of a healthy life span. SN - 1523-0864 UR - https://www.unboundmedicine.com/medline/citation/15345150/Redox_regulation_in_neurodegeneration_and_longevity:_role_of_the_heme_oxygenase_and_HSP70_systems_in_brain_stress_tolerance_ L2 - https://www.liebertpub.com/doi/full/10.1089/ars.2004.6.895?url_ver=Z39.88-2003&rfr_id=ori:rid:crossref.org&rfr_dat=cr_pub=pubmed DB - PRIME DP - Unbound Medicine ER -