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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Gene Review: 

NCF2  -  neutrophil cytosolic factor 2

Bos taurus

 
 
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High impact information on NCF2

  • Comparison of the bovine sequences with those of the human and murine homologs showed that they were highly conserved, but also revealed important information regarding key structural features of p47-phox and p67-phox, including location of putative phosphorylation sites [1].
  • Following incubation of a cytosolic extract from nonactivated bovine neutrophil with protein A-Sepharose bound to anti-p67phox antibodies, the recovered immunoprecipitate contained the S100 protein, p47phox and p67phox [2].
  • Both green tea polyphenols (GTP) and black tea polyphenols (BTP) down-regulated the expression of NADPH oxidase subunits p22phox and p67phox while up-regulating catalase expression (p < 0.05, respectively) [3].
 

Other interactions of NCF2

  • When neutrophils are exposed to a variety of particulate or soluble stimuli, the oxidase becomes activated, due to the assembly on the membrane-bound flavocytochrome b of three cytosolic factors, p47phox, p67phox and Rac 2 (or Rac 1) [4].

References

  1. Cloning and expression of bovine p47-phox and p67-phox: comparison with the human and murine homologs. Bunger, P.L., Swain, S.D., Clements, M.K., Siemsen, D.W., Davis, A.R., Gauss, K.A., Quinn, M.T. J. Leukoc. Biol. (2000) [Pubmed]
  2. The S100A8/A9 protein as a partner for the cytosolic factors of NADPH oxidase activation in neutrophils. Doussiere, J., Bouzidi, F., Vignais, P.V. Eur. J. Biochem. (2002) [Pubmed]
  3. Tea polyphenols regulate nicotinamide adenine dinucleotide phosphate oxidase subunit expression and ameliorate angiotensin II-induced hyperpermeability in endothelial cells. Ying, C.J., Xu, J.W., Ikeda, K., Takahashi, K., Nara, Y., Yamori, Y. Hypertens. Res. (2003) [Pubmed]
  4. Phenylarsine oxide as an inhibitor of the activation of the neutrophil NADPH oxidase--identification of the beta subunit of the flavocytochrome b component of the NADPH oxidase as a target site for phenylarsine oxide by photoaffinity labeling and photoinactivation. Doussiere, J., Poinas, A., Blais, C., Vignais, P.V. Eur. J. Biochem. (1998) [Pubmed]
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