Biology:NOX5
From HandWiki
 Generic protein structure example |
NADPH oxidase, EF-hand calcium binding domain 5, also known as NOX5, is a protein which in humans is encoded by the NOX5 gene.[1][2]
Function
NOX5 is a novel NADPH oxidase that generates superoxide.[1]
Nox5 interacts with c-abl, superoxide production leads to phosphorylation of c-abl, while inhibition of c-abl kinase activity inhibits Nox5 superoxide production.[3]
References
- ↑ 1.0 1.1 "Entrez Gene: NOX5 NADPH oxidase, EF-hand calcium binding domain 5". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=79400.
- ↑ "A Ca(2+)-activated NADPH oxidase in testis, spleen, and lymph nodes". J. Biol. Chem. 276 (40): 37594–601. October 2001. doi:10.1074/jbc.M103034200. PMID 11483596.
- ↑ "Novel redox-dependent regulation of NOX5 by the tyrosine kinase c-Abl". Free Radic. Biol. Med. 44 (5): 868–81. March 2008. doi:10.1016/j.freeradbiomed.2007.11.020. PMID 18160052.
Further reading
- "Amplification of the Inflammatory Cellular Redox State by Human Immunodeficiency Virus Type 1-Immunosuppressive Tat and gp160 Proteins". J. Virol. 73 (2): 1447–52. 1999. doi:10.1128/JVI.73.2.1447-1452.1999. PMID 9882350.
- "Homologs of gp91phox: cloning and tissue expression of Nox3, Nox4, and Nox5". Gene 269 (1–2): 131–40. 2001. doi:10.1016/S0378-1119(01)00449-8. PMID 11376945.
- "A Ca(2+)-activated NADPH oxidase in testis, spleen, and lymph nodes". J. Biol. Chem. 276 (40): 37594–601. 2001. doi:10.1074/jbc.M103034200. PMID 11483596.
- "A comparison of the NADPH oxidase in human sperm and white blood cells". Int. J. Androl. 25 (4): 223–9. 2002. doi:10.1046/j.1365-2605.2002.00351.x. PMID 12121572.
- "Participation of Rac GTPase activating proteins in the deactivation of the phagocytic NADPH oxidase". Biochemistry 41 (34): 10710–6. 2002. doi:10.1021/bi0257033. PMID 12186557.
- "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. 2004. doi:10.1038/ng1285. PMID 14702039.
- "Mechanism of Ca2+ activation of the NADPH oxidase 5 (NOX5)". J. Biol. Chem. 279 (18): 18583–91. 2004. doi:10.1074/jbc.M310268200. PMID 14982937.
- "Human Immunodeficiency Virus Type 1 gp120 Induces Apoptosis in Human Primary Neurons through Redox-Regulated Activation of Neutral Sphingomyelinase". J. Neurosci. 24 (43): 9531–40. 2005. doi:10.1523/JNEUROSCI.3085-04.2004. PMID 15509740.
- "Point mutations in the proline-rich region of p22phox are dominant inhibitors of Nox1- and Nox2-dependent reactive oxygen generation". J. Biol. Chem. 280 (36): 31859–69. 2005. doi:10.1074/jbc.M501882200. PMID 15994299.
- "Synergy between extracellular group IIA phospholipase A2 and phagocyte NADPH oxidase in digestion of phospholipids of Staphylococcus aureus ingested by human neutrophils". J. Immunol. 175 (7): 4653–61. 2005. doi:10.4049/jimmunol.175.7.4653. PMID 16177112.
- "NAD(P)H oxidase 4 mediates transforming growth factor-beta1-induced differentiation of cardiac fibroblasts into myofibroblasts". Circ. Res. 97 (9): 900–7. 2005. doi:10.1161/01.RES.0000187457.24338.3D. PMID 16179589.
- "Expression and activity of NOX5 in the circulating malignant B cells of hairy cell leukemia". J. Immunol. 175 (12): 8424–30. 2006. doi:10.4049/jimmunol.175.12.8424. PMID 16339585.
- "cAMP-response element-binding protein mediates acid-induced NADPH oxidase NOX5-S expression in Barrett esophageal adenocarcinoma cells". J. Biol. Chem. 281 (29): 20368–82. 2006. doi:10.1074/jbc.M603353200. PMID 16707484.
- "NO-mediated regulation of NAD(P)H oxidase by laminar shear stress in human endothelial cells". J. Physiol. 576 (Pt 2): 557–67. 2006. doi:10.1113/jphysiol.2006.111070. PMID 16873416.
- "Superoxide production and NADPH oxidase expression in human rheumatoid synovial cells: regulation by interleukin-1beta and tumour necrosis factor-alpha". Inflamm. Res. 55 (11): 483–90. 2007. doi:10.1007/s00011-006-6036-8. PMID 17122966.
- "Novel mechanism of activation of NADPH oxidase 5. calcium sensitization via phosphorylation". J. Biol. Chem. 282 (9): 6494–507. 2007. doi:10.1074/jbc.M608966200. PMID 17164239.
- "NOX5 variants are functionally active in endothelial cells". Free Radic. Biol. Med. 42 (4): 446–59. 2007. doi:10.1016/j.freeradbiomed.2006.10.054. PMID 17275676.
- "NADPH oxidase 5 (NOX5) interacts with and is regulated by calmodulin". FEBS Lett. 581 (6): 1202–8. 2007. doi:10.1016/j.febslet.2007.02.047. PMID 17346712.
- "Inhibition of NADPH oxidase reduces myocardial oxidative stress and apoptosis and improves cardiac function in heart failure after myocardial infarction". Free Radic. Biol. Med. 43 (2): 271–81. 2007. doi:10.1016/j.freeradbiomed.2007.04.021. PMID 17603936.
 |
