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NADPH oxidase, expression

Furthermore, as already mentioned above, the interaction of superoxide with NO synthase in vascular tissue may lead to uncoupling of this enzyme and increasing superoxide production [117]. Therefore, the overproduction of superoxide may affect superoxide/nitric oxide by different ways, resulting in cell injury. It is interesting that some biomolecules may be useful for improving this balance. Thus, 17(3-estradiol upregulated NO synthase expression and inhibited NADPH oxidase expression in human endothelial cells [136]. [Pg.729]

Steinbeck, M.J., Appel, W.H., Jr., Verhoeven, A.J., and Kamovsky, M.J. 1994. NADPH-oxidase expression and in situ production of superoxide by osteoclasts actively resorbing bone. J. Cell Biol. 126, 765-772. [Pg.162]

Wagner, A.H., Schroeter, M.R., and Hecker, M. 2001. 17b-Estradiol inhibition of NADPH oxidase expression in human endothelial cells. FASEB J. 15, 2121-2130. [Pg.164]

Al-Awwadi, N. A., Araiz, C., Bomet, A., Delbosc, S., Ciistol, J. R, Linck, N., Azay, J., Teisse-dre, P. L., Cros, G. (2005). Extracts enriched in different polyphenoUc families normalize increased cardiac NADPH oxidase expression while having differential effects on insulin resistance, hypertension, and cardiac hypertrophy in high-fructose-fed rats. J. Agric. Food Chem., 53, 151-157. [Pg.582]

Holland et al. [125] have shown that the potent vascular smooth muscle cell mitogen and phospholipase A2 activator thrombin stimulated superoxide production in human endothelial cells, which was inhibited by the NADPH oxidase inhibitors. Similarly, thrombin enhanced the production of oxygen species and the expression of )Alphos and Rac2 subunits of NADPH oxidase in VSMCs [126,127]. Greene et al. [128] demonstrated that the activator of NO synthase neuropeptide bradykinin is also able to stimulate NADPH oxidase in VSMCs. Similar to XO, NADPH oxidase enhanced superoxide production in pulmonary artery smooth muscle cells upon exposure to hypoxia [129]. [Pg.727]

Itou, T. et al., Oxygen radical generation and expression of NADPH oxidase genes in bottlenose dolphin (Tursiops truncatus) neutrophils, Develop. Comp. Immunol., 25, 47, 2001. [Pg.417]

In mature neutrophils, interferon-7induces the expression of FC7RI, increases antibody-dependent cytotoxicity, primes the ability to generate reactive oxidants and selectively stimulates protein biosynthesis. These effects are described in detail in Chapter 7. Additionally, this cytokine has been used clinically for the treatment of chronic granulomatous disease (CGD), which is associated with an increased susceptibility to infections due to an impairment of NADPH oxidase function ( 8.2). [Pg.92]

The cytochrome (by virtue of its ability to accept and donate electrons during its function in electron transport) can exist in either the oxidised or the reduced state. In reduced-minus-oxidised difference spectra, it has absorption maxima at 426, 530 and 558 nm, typical of many b-type cytochromes. The ease with which the cytochrome can accept and donate electrons is expressed by its redox (reduction-oxidation) potential, which is measured in millivolts. Unlike most mammalian b cytochromes, which have much higher midpoint potentials, that of the cytochrome of the NADPH oxidase is -245 mV. Be-... [Pg.159]

Volpp, B. D., Nauseef, W. M Donelson, J. E Moser, D. R Clark, R. A. (1989). Cloning of the cDNA and functional expression of the 47-kilodalton cytosolic component of human respiratory burst oxidase. Proc. Natl. Acad. Sci. USA 86, 7195-9. Watson, F., Robinson, J. J., Edwards, S. W. (1991). Protein kinase C dependent and independent activation of the NADPH oxidase of human neutrophils. J. Biol. Chem. 266, 7432-9. [Pg.187]

Cassatella, M. A., Bazzoni, F., Calzetti, F., Guasparri, I., Rossi, F., Trinchieri, G. (1991). Interferon-/transcriptionally modulates the expression of the genes for the high affinity IgG-Fc receptor and the 47-kDa cytosolic component of NADPH oxidase in human polymorphonuclear leukocytes. J. Biol. Chem. 266, 22079-82. [Pg.259]


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NADPH oxidase

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