HSP90 inhibition by 17-DMAG attenuates oxidative stress in experimental atherosclerosis | Zendy

Julio MadrigalMatute | Zendy; Carlos Ernesto FernandezGarcia | Zendy; Carmen GómezGuerrero | Zendy; Óscar López-Franco | Zendy; Begoña MuñozGarcía | Zendy; Jesús Egido | Zendy; Luis Miguel BlancoColio | Zendy; José Luis Martı́n-Ventura | Zendy

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HSP90 inhibition by 17-DMAG attenuates oxidative stress in experimental atherosclerosis

Author(s) -

Julio MadrigalMatute,

Carlos Ernesto FernandezGarcia,

Carmen GómezGuerrero,

Óscar López-Franco,

Begoña MuñozGarcía,

Jesús Egido,

Luis Miguel BlancoColio,

José Luis Martı́n-Ventura

Publication year - 2012

Publication title -

cardiovascular research

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.774

H-Index - 219

eISSN - 1755-3245

pISSN - 0008-6363

DOI - 10.1093/cvr/cvs158

Subject(s) - oxidative stress , heat shock protein , hsp90 , protein kinase a , nadph oxidase , oxidative phosphorylation , inflammation , reactive oxygen species , chemistry , microbiology and biotechnology , biochemistry , cancer research , pharmacology , kinase , biology , immunology , gene

Reactive oxygen species (ROS) participate in atherogenesis through different mechanisms including oxidative stress and inflammation. Proteins implicated in both processes, such as mitogen-activated protein kinase kinase (MEK) and some NADPH oxidase (NOX) subunits, are heat shock protein-90 (HSP90) client proteins. In this work, we investigated the antioxidant properties of the HSP90 inhibitor, 17-dimethylaminoethylamino-17-demethoxygeldanamycin (17-DMAG) in experimental atherosclerosis.

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