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Nox/Duox Family of NADPH Oxidases: Lessons from Knockout Mouse Models.
Sirokmány, Gábor; Donkó, Ágnes; Geiszt, Miklós.
Afiliación
  • Sirokmány G; Department of Physiology, Semmelweis University, Faculty of Medicine, "Momentum" Peroxidase Enzyme Research Group of the Semmelweis University and the Hungarian Academy of Sciences, PO Box 259, H-1444 Budapest, Hungary.
  • Donkó Á; Department of Physiology, Semmelweis University, Faculty of Medicine, "Momentum" Peroxidase Enzyme Research Group of the Semmelweis University and the Hungarian Academy of Sciences, PO Box 259, H-1444 Budapest, Hungary.
  • Geiszt M; Department of Physiology, Semmelweis University, Faculty of Medicine, "Momentum" Peroxidase Enzyme Research Group of the Semmelweis University and the Hungarian Academy of Sciences, PO Box 259, H-1444 Budapest, Hungary. Electronic address: geiszt@eok.sote.hu.
Trends Pharmacol Sci ; 37(4): 318-327, 2016 Apr.
Article en En | MEDLINE | ID: mdl-26861575
ABSTRACT
Nox/Duox NADPH oxidases are now considered the primary, regulated sources of reactive oxygen species (ROS). These enzymes are expressed in diverse cells and tissues, and their products are essential in several physiological settings. Knockout mouse models are instrumental in identifying the physiological functions of Nox/Duox enzymes as well as in exploring the impact of their pharmacological targeting on disease progression. The currently available data from experiments on knockout animals suggest that the lack of non-phagocytic Nox/Duox enzymes often modifies the course and phenotype in many disease models. Nevertheless, as illustrated by studies on Nox4-deficient animals, the absence of Nox-derived ROS can also lead to aggravated disease manifestation, reinforcing the need for a more balanced view on the role of ROS in health and disease.
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Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: NADH NADPH Oxidorreductasas Límite: Animals / Humans Idioma: En Revista: Trends Pharmacol Sci Año: 2016 Tipo del documento: Article País de afiliación: Hungria

Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: NADH NADPH Oxidorreductasas Límite: Animals / Humans Idioma: En Revista: Trends Pharmacol Sci Año: 2016 Tipo del documento: Article País de afiliación: Hungria