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Zeitschriftenartikel

Tissue oxygen sensor function of NADPH oxidase isoforms, an unusual cytochrome aa3 and reactive oxygen species

MPG-Autoren

Porwol,  Torsten
Max Planck Institute of Molecular Physiology, Max Planck Society;

Ehleben,  Wilhelm
Max Planck Institute of Molecular Physiology, Max Planck Society;

Brand,  Verena
Max Planck Institute of Molecular Physiology, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons98672

Acker,  Helmut
Sonstige Wissenschaftliche Organisationseinheiten, Max Planck Institute of Molecular Physiology, Max Planck Society;

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Zitation

Porwol, T., Ehleben, W., Brand, V., & Acker, H. (2001). Tissue oxygen sensor function of NADPH oxidase isoforms, an unusual cytochrome aa3 and reactive oxygen species. Respiration Physiology, 128(3): 1, pp. 331-348. Retrieved from http://dx.doi.org/10.1016/S0034-5687(01)00310-3.


Zitierlink: http://hdl.handle.net/11858/00-001M-0000-0014-0F7E-C
Zusammenfassung
NADPH oxidase isoforms with different gp91phox subunits as well as an unusual cytochrome aa3 with a heme a/a3 relationship of 9:91 are discussed as putative oxygen sensor proteins influencing gene expression and ion channel conductivity. Reactive oxygen species (ROS) are important second messengers of the oxygen sensing signal cascade determining the stability of transcription factors or the gating of ion channels. The formation of ROS by a perinuclear Fenton reaction is imaged by 1 and 2 photon confocal microscopy revealing mitochondrial and non-mitochondrial generation. (C) 2001 Elsevier Science B.V. All rights reserved.