Stress Proteins Induced by Arsenic
Identifieur interne : 002D12 ( Main/Exploration ); précédent : 002D11; suivant : 002D13Stress Proteins Induced by Arsenic
Auteurs : Luz M. Del Razo [Mexique] ; Betzabet Quintanilla-Vega [Mexique] ; Eduardo Brambila-Colombres [Mexique] ; Emma S. Calder N-Aranda [Mexique] ; Maurizio Manno [Italie] ; Arnulfo Albores [Mexique]Source :
- Toxicology and Applied Pharmacology [ 0041-008X ] ; 2001.
English descriptors
- KwdEn :
- Teeft :
- Acute exposure, Albores, Alveolar macrophages, Apoptosis, Aposhian, Appl, Arsenate, Arsenic, Arsenic carcinogenesis, Arsenic compounds, Arsenic exposure, Arsenic table, Arsenical, Arsenide, Arsenite, Barchowsky, Bilirubin, Biochem, Biol, Biophys, Boca raton, Broblasts, Carbon monoxide, Carcinogenesis, Cebrian, Cell death, Cell proliferation, Cell stress chap, Cellular, Chaperone, Chem, Chinese hamster ovary cells, Cullen, Cytokine, Dimethylarsinic, Dimethylarsinic acid, Dmas, Drinking water, Embryo, Enzymatic methylation, Epithelial, Eukaryotic cells, Gallium arsenide, Gene, Gene expression, Gene transcription, Germolec, Growth factors, Grps, Hamster, Health effects, Heat shock, Heat shock protein, Heat shock proteins, Heat shock response, Heavy metals, Heme, Heme oxigenase, Heme oxygenase, Hepatic, Hepatoma, Hydrogen peroxide, Important role, Indium arsenide, Inducer, Inducible, Induction, Inorganic arsenic, Inorganic arsenicals, Kato, Keratinocytes, Kinase, Kitchin, Liver slices, Macrophage, Menzel, Metallothionein, Mmas, Molecular chaperones, Mouse, Mrna, Nitric oxide, Normal cells, Other proteins, Ovary, Oxidative, Oxidative damage, Oxidative stress, Oxygenase, Pathway, Pharmacol, Physiol, Physiological conditions, Protective role, Protein, Protein synthesis, Proteolytic pathway, Razo, Reactive, Reactive oxygen species, Receptor, Reductase, Single dose, Sodium arsenite, Somji, Stress protein, Stress proteins, Stress response, Subcutaneous exposure, Toxic effects, Toxicity, Toxicol, Toxicology, Tracheal epithelial cells, Transcription, Transcription factor, Transcription factors, Trivalent, Tubule, Tubule cells, Waalkes, Wang, Wijeweera, Yamanaka.
Abstract
Abstract: The elevated expression of stress proteins is considered to be a universal response to adverse conditions, representing a potential mechanism of cellular defense against disease and a potential target for novel therapeutics. Exposure to arsenicals either in vitro or in vivo in a variety of model systems has been shown to cause the induction of a number of the major stress protein families such as heat shock proteins (Hsp). Among them are members with low molecular weight, such as metallotionein and ubiquitin, as well as ones with masses of 27, 32, 60, 70, 90, and 110 kDa. In most of the cases, the induction of stress proteins depends on the capacity of the arsenical to reach the target, its valence, and the type of exposure, arsenite being the biggest inducer of most Hsp in several organs and systems. Hsp induction is a rapid dose-dependent response (1–8 h) to the acute exposure to arsenite. Thus, the stress response appears to be useful to monitor the sublethal toxicity resulting from a single exposure to arsenite. The present paper offers a critical review of the capacity of arsenicals to modulate the expression and/or accumulation of stress proteins. The physiological consequences of the arsenic-induced stress and its usefulness in monitoring effects resulting from arsenic exposure in humans and other organisms are discussed.
Url:
DOI: 10.1006/taap.2001.9291
Affiliations:
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xml:lang="fr">Mexique</country><wicri:regionArea>Sección de Toxicologı́a, Centro de Investigación y Estudios Avanzados del Instituto Politécnico National, Mexico City</wicri:regionArea><wicri:noRegion>Mexico City</wicri:noRegion></affiliation></author></analytic><monogr></monogr><series><title level="j">Toxicology and Applied Pharmacology</title><title level="j" type="abbrev">YTAAP</title><idno type="ISSN">0041-008X</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="2001">2001</date><biblScope unit="volume">177</biblScope><biblScope unit="issue">2</biblScope><biblScope unit="page" from="132">132</biblScope><biblScope unit="page" to="148">148</biblScope></imprint><idno type="ISSN">0041-008X</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0041-008X</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>arsenic</term><term>heat shock proteins</term><term>heme oxygenase</term><term>metallothionein</term><term>stress proteins</term></keywords><keywords scheme="Teeft" xml:lang="en"><term>Acute exposure</term><term>Albores</term><term>Alveolar macrophages</term><term>Apoptosis</term><term>Aposhian</term><term>Appl</term><term>Arsenate</term><term>Arsenic</term><term>Arsenic carcinogenesis</term><term>Arsenic compounds</term><term>Arsenic exposure</term><term>Arsenic table</term><term>Arsenical</term><term>Arsenide</term><term>Arsenite</term><term>Barchowsky</term><term>Bilirubin</term><term>Biochem</term><term>Biol</term><term>Biophys</term><term>Boca raton</term><term>Broblasts</term><term>Carbon monoxide</term><term>Carcinogenesis</term><term>Cebrian</term><term>Cell death</term><term>Cell proliferation</term><term>Cell stress chap</term><term>Cellular</term><term>Chaperone</term><term>Chem</term><term>Chinese hamster ovary cells</term><term>Cullen</term><term>Cytokine</term><term>Dimethylarsinic</term><term>Dimethylarsinic acid</term><term>Dmas</term><term>Drinking water</term><term>Embryo</term><term>Enzymatic methylation</term><term>Epithelial</term><term>Eukaryotic cells</term><term>Gallium arsenide</term><term>Gene</term><term>Gene expression</term><term>Gene transcription</term><term>Germolec</term><term>Growth factors</term><term>Grps</term><term>Hamster</term><term>Health effects</term><term>Heat shock</term><term>Heat shock protein</term><term>Heat shock proteins</term><term>Heat shock response</term><term>Heavy metals</term><term>Heme</term><term>Heme oxigenase</term><term>Heme oxygenase</term><term>Hepatic</term><term>Hepatoma</term><term>Hydrogen peroxide</term><term>Important role</term><term>Indium arsenide</term><term>Inducer</term><term>Inducible</term><term>Induction</term><term>Inorganic arsenic</term><term>Inorganic arsenicals</term><term>Kato</term><term>Keratinocytes</term><term>Kinase</term><term>Kitchin</term><term>Liver slices</term><term>Macrophage</term><term>Menzel</term><term>Metallothionein</term><term>Mmas</term><term>Molecular chaperones</term><term>Mouse</term><term>Mrna</term><term>Nitric oxide</term><term>Normal cells</term><term>Other proteins</term><term>Ovary</term><term>Oxidative</term><term>Oxidative damage</term><term>Oxidative stress</term><term>Oxygenase</term><term>Pathway</term><term>Pharmacol</term><term>Physiol</term><term>Physiological conditions</term><term>Protective role</term><term>Protein</term><term>Protein synthesis</term><term>Proteolytic pathway</term><term>Razo</term><term>Reactive</term><term>Reactive oxygen species</term><term>Receptor</term><term>Reductase</term><term>Single dose</term><term>Sodium arsenite</term><term>Somji</term><term>Stress protein</term><term>Stress proteins</term><term>Stress response</term><term>Subcutaneous exposure</term><term>Toxic effects</term><term>Toxicity</term><term>Toxicol</term><term>Toxicology</term><term>Tracheal epithelial cells</term><term>Transcription</term><term>Transcription factor</term><term>Transcription factors</term><term>Trivalent</term><term>Tubule</term><term>Tubule cells</term><term>Waalkes</term><term>Wang</term><term>Wijeweera</term><term>Yamanaka</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: The elevated expression of stress proteins is considered to be a universal response to adverse conditions, representing a potential mechanism of cellular defense against disease and a potential target for novel therapeutics. Exposure to arsenicals either in vitro or in vivo in a variety of model systems has been shown to cause the induction of a number of the major stress protein families such as heat shock proteins (Hsp). Among them are members with low molecular weight, such as metallotionein and ubiquitin, as well as ones with masses of 27, 32, 60, 70, 90, and 110 kDa. In most of the cases, the induction of stress proteins depends on the capacity of the arsenical to reach the target, its valence, and the type of exposure, arsenite being the biggest inducer of most Hsp in several organs and systems. Hsp induction is a rapid dose-dependent response (1–8 h) to the acute exposure to arsenite. Thus, the stress response appears to be useful to monitor the sublethal toxicity resulting from a single exposure to arsenite. The present paper offers a critical review of the capacity of arsenicals to modulate the expression and/or accumulation of stress proteins. The physiological consequences of the arsenic-induced stress and its usefulness in monitoring effects resulting from arsenic exposure in humans and other organisms are discussed.</div></front></TEI><affiliations><list><country><li>Italie</li><li>Mexique</li></country><region><li>Vénétie</li></region><settlement><li>Padoue</li></settlement><orgName><li>Université de Padoue</li></orgName></list><tree><country name="Mexique"><noRegion><name sortKey="Del Razo, Luz M" sort="Del Razo, Luz M" uniqKey="Del Razo L" first="Luz M" last="Del Razo">Luz M. Del Razo</name></noRegion><name sortKey="Albores, Arnulfo" sort="Albores, Arnulfo" uniqKey="Albores A" first="Arnulfo" last="Albores">Arnulfo Albores</name><name sortKey="Brambila Colombres, Eduardo" sort="Brambila Colombres, Eduardo" uniqKey="Brambila Colombres E" first="Eduardo" last="Brambila-Colombres">Eduardo Brambila-Colombres</name><name sortKey="Calder N Aranda, Emma S" sort="Calder N Aranda, Emma S" uniqKey="Calder N Aranda E" first="Emma S" last="Calder N-Aranda">Emma S. Calder N-Aranda</name><name sortKey="Quintanilla Vega, Betzabet" sort="Quintanilla Vega, Betzabet" uniqKey="Quintanilla Vega B" first="Betzabet" last="Quintanilla-Vega">Betzabet Quintanilla-Vega</name></country><country name="Italie"><region name="Vénétie"><name sortKey="Manno, Maurizio" sort="Manno, Maurizio" uniqKey="Manno M" first="Maurizio" last="Manno">Maurizio Manno</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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