Heat shock proteins and hormesis in the diagnosis and treatment of neurodegenerative diseases

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Abstract

Modulation of endogenous cellular defense mechanisms via the vitagene system represents an innovative approach to therapeutic intervention in diseases causing chronic tissue damage, such as in neurodegeneration. The possibility of high-throughoutput screening using proteomic techniques, particularly redox proteomics, provide more comprehensive overview of the interaction of proteins, as well as the interplay among processes involved in neuroprotection. Here by introducing the hormetic dose response concept, the mechanistic foundations and applications to the field of neuroprotection, we discuss the emerging role of heat shock protein as prominent member of vitagene network in neuroprotection and redox proteomics as a tool for investigating redox modulation of stress responsive vitagenes. Hormetic mechanisms are reviewed as possibility of targeted therapeutic manipulation in a cell-, tissue- and/or pathway-specific manner at appropriate points in the neurodegenerative disease process.

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Proteomic analysis of post-translational modifications.

Matthias Mann, Ole N. Jensen (2003)

Post-translational modifications modulate the activity of most eukaryote proteins. Analysis of these modifications presents formidable challenges but their determination generates indispensable insight into biological function. Strategies developed to characterize individual proteins are now systematically applied to protein populations. The combination of function- or structure-based purification of modified 'subproteomes', such as phosphorylated proteins or modified membrane proteins, with mass spectrometry is proving particularly successful. To map modification sites in molecular detail, novel mass spectrometric peptide sequencing and analysis technologies hold tremendous potential. Finally, stable isotope labeling strategies in combination with mass spectrometry have been applied successfully to study the dynamics of modifications.

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Cellular stress responses, the hormesis paradigm, and vitagenes: novel targets for therapeutic intervention in neurodegenerative disorders.

Vittorio Calabrese, Carolin Cornelius, Albena T. Dinkova-Kostova … (2010)

Despite the capacity of chaperones and other homeostatic components to restore folding equilibrium, cells appear poorly adapted for chronic oxidative stress that increases in cancer and in metabolic and neurodegenerative diseases. Modulation of endogenous cellular defense mechanisms represents an innovative approach to therapeutic intervention in diseases causing chronic tissue damage, such as in neurodegeneration. This article introduces the concept of hormesis and its applications to the field of neuroprotection. It is argued that the hormetic dose response provides the central underpinning of neuroprotective responses, providing a framework for explaining the common quantitative features of their dose-response relationships, their mechanistic foundations, and their relationship to the concept of biological plasticity, as well as providing a key insight for improving the accuracy of the therapeutic dose of pharmaceutical agents within the highly heterogeneous human population. This article describes in mechanistic detail how hormetic dose responses are mediated for endogenous cellular defense pathways, including sirtuin and Nrf2 and related pathways that integrate adaptive stress responses in the prevention of neurodegenerative diseases. Particular attention is given to the emerging role of nitric oxide, carbon monoxide, and hydrogen sulfide gases in hormetic-based neuroprotection and their relationship to membrane radical dynamics and mitochondrial redox signaling.

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Proteotoxic stress and inducible chaperone networks in neurodegenerative disease and aging.

Richard Morimoto (2008)

The long-term health of the cell is inextricably linked to protein quality control. Under optimal conditions this is accomplished by protein homeostasis, a highly complex network of molecular interactions that balances protein biosynthesis, folding, translocation, assembly/disassembly, and clearance. This review will examine the consequences of an imbalance in homeostasis on the flux of misfolded proteins that, if unattended, can result in severe molecular damage to the cell. Adaptation and survival requires the ability to sense damaged proteins and to coordinate the activities of protective stress response pathways and chaperone networks. Yet, despite the abundance and apparent capacity of chaperones and other components of homeostasis to restore folding equilibrium, the cell appears poorly adapted for chronic proteotoxic stress when conformationally challenged aggregation-prone proteins are expressed in cancer, metabolic disease, and neurodegenerative disease. The decline in biosynthetic and repair activities that compromises the integrity of the proteome is influenced strongly by genes that control aging, thus linking stress and protein homeostasis with the health and life span of the organism.

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Author and article information

Contributors

Sandro Dattilo: oaicsandro@msn.com

Cesare Mancuso: cmancuso@rm.unicatt.it

Guido Koverech: ggmax@hotmail.it

Paola Di Mauro: paola_mp86@hotmail.it

Maria Laura Ontario: marialaura.ontario@ontariosrl.it

Antonino Petralia: petralia@unict.it

Luigi Maiolino: maiolino@policlinico.unict.it

Agostino Serra: serra@policlinico.unict.it

Edward J. Calabrese: edwardc@schoolph.umass.edu

Vittorio Calabrese: 0039-095-7384067 , calabres@unict.it

Journal

Journal ID (nlm-ta): Immun Ageing

Journal ID (iso-abbrev): Immun Ageing

Title: Immunity & Ageing : I & A

Publisher: BioMed Central (London )

ISSN (Electronic): 1742-4933

Publication date (Electronic): 4 November 2015

Publication date PMC-release: 4 November 2015

Publication date Collection: 2015

Volume: 12

Electronic Location Identifier: 20

Affiliations

[ ]Department of Biomedical and Biotechnological Sciences, University of Catania, Via Andrea Doria, 95100 Catania, Italy

[ ]Department of Medical and Surgery Specialties, University of Catania, Catania, Italy

[ ]Department of Clinical and Experimental Medicine, School of Medicine, University of Catania, Catania, Italy

[ ]Institute of Pharmacology, Catholic University School of Medicine, Rome, Italy

[ ]Environmental Health Sciences Division, School of Public Health, University of Massachusetts, Amherst, MA USA

[ ]University College London Hospitals, NHS Foundation Trust, London, UK

Article

Publisher ID: 46

DOI: 10.1186/s12979-015-0046-8

PMC ID: 4634585

PubMed ID: 26543490

SO-VID: 9f66d212-efa4-4689-abcd-4f3f0f2fe039

License:

Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License ( http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver ( http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.

History

Date received : 1 August 2015

Date accepted : 15 October 2015

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ScienceOpen disciplines: Immunology

Keywords: alzheimer’s disease,heat shock proteins,heme oxygenase,oxidative stress,bilirubin,neurodegenerative disorders,vitagenes

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ScienceOpen disciplines: Immunology

Keywords: alzheimer’s disease, heat shock proteins, heme oxygenase, oxidative stress, bilirubin, neurodegenerative disorders, vitagenes

Heat shock proteins and hormesis in the diagnosis and treatment of neurodegenerative diseases

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Abstract

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Most cited references 200

Proteomic analysis of post-translational modifications.

Cellular stress responses, the hormesis paradigm, and vitagenes: novel targets for therapeutic intervention in neurodegenerative disorders.

Proteotoxic stress and inducible chaperone networks in neurodegenerative disease and aging.

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