Cytochrome b-245, alpha polypeptide

Identifiers

External IDs

OMIM: 608508 MGI: 1316658 HomoloGene: 80 GeneCards: CYBA Gene

Gene Ontology
Molecular function	• protein binding • electron carrier activity • electron carrier activity • superoxide-generating NADPH oxidase activity • oxidoreductase activity • SH3 domain binding • heme binding • metal ion binding • protein heterodimerization activity
Cellular component	• cytoplasm • mitochondrion • Golgi apparatus • membrane • apical plasma membrane • stored secretory granule • dendrite • NADPH oxidase complex • NADPH oxidase complex • neuronal cell body
Biological process	• positive regulation of endothelial cell proliferation • negative regulation of glomerular filtration by angiotensin • superoxide metabolic process • transport • inflammatory response • regulation of blood pressure • smooth muscle hypertrophy • cytochrome complex assembly • electron transport chain • positive regulation of cell growth • response to nutrient levels • superoxide anion generation • innate immune response • respiratory burst • hydrogen peroxide biosynthetic process • oxidation-reduction process • response to interleukin-1 • cellular response to amino acid stimulus • cellular response to mechanical stimulus • cellular response to glucose stimulus • cellular response to tumor necrosis factor • cellular response to organic cyclic compound • cellular response to gamma radiation
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 16:
88.71 – 88.72 Mb

Chr 8:
124.95 – 124.96 Mb

PubMed search

[1]

[2]

Cytochrome b-245 light chain is a protein that in humans is encoded by the CYBA gene involved in superoxide production and phagocytosis.^[1]

Cytochrome b is composed of a light chain (alpha) and a heavy chain (beta). This gene encodes the light, alpha subunit, which has been proposed as a primary component of the microbicidal oxidase system of phagocytes. Mutations in this gene are associated with autosomal recessive chronic granulomatous disease (CGD), which is characterized by the failure of activated phagocytes to generate superoxide, which is important for the microbicidal activity of these cells.^[2]

References

^ Dinauer MC, Pierce EA, Bruns GA, Curnutte JT, Orkin SH (Dec 1990). "Human neutrophil cytochrome b light chain (p22-phox). Gene structure, chromosomal location, and mutations in cytochrome-negative autosomal recessive chronic granulomatous disease". J Clin Invest 86 (5): 1729–37. doi:10.1172/JCI114898. PMC 296926. PMID 2243141. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=296926.
^ "Entrez Gene: CYBA cytochrome b-245, alpha polypeptide". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1535.

Zalba G, San José G, Moreno MU, et al. (2006). "NADPH oxidase-mediated oxidative stress: genetic studies of the p22(phox) gene in hypertension.". Antioxid. Redox Signal. 7 (9-10): 1327–36. doi:10.1089/ars.2005.7.1327. PMID 16115038.
de Boer M, de Klein A, Hossle JP, et al. (1992). "Cytochrome b558-negative, autosomal recessive chronic granulomatous disease: two new mutations in the cytochrome b558 light chain of the NADPH oxidase (p22-phox).". Am. J. Hum. Genet. 51 (5): 1127–35. PMC 1682833. PMID 1415254. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1682833.
Dinauer MC, Pierce EA, Erickson RW, et al. (1992). "Point mutation in the cytoplasmic domain of the neutrophil p22-phox cytochrome b subunit is associated with a nonfunctional NADPH oxidase and chronic granulomatous disease.". Proc. Natl. Acad. Sci. U.S.A. 88 (24): 11231–5. doi:10.1073/pnas.88.24.11231. PMC 53108. PMID 1763037. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=53108.
Bu-Ghanim HN, Casimir CM, Povey S, Segal AW (1991). "The alpha subunit of cytochrome b-245 mapped to chromosome 16.". Genomics 8 (3): 568–70. doi:10.1016/0888-7543(90)90045-V. PMID 2286377.
Verhoeven AJ, Bolscher BG, Meerhof LJ, et al. (1989). "Characterization of two monoclonal antibodies against cytochrome b558 of human neutrophils.". Blood 73 (6): 1686–94. PMID 2469497.
Parkos CA, Allen RA, Cochrane CG, Jesaitis AJ (1987). "Purified cytochrome b from human granulocyte plasma membrane is composed of two polypeptides with relative molecular weights of 91,000 and 22,000.". J. Clin. Invest. 80 (3): 732–42. doi:10.1172/JCI113128. PMC 442297. PMID 3305576. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=442297.
Parkos CA, Dinauer MC, Walker LE, et al. (1988). "Primary structure and unique expression of the 22-kilodalton light chain of human neutrophil cytochrome b.". Proc. Natl. Acad. Sci. U.S.A. 85 (10): 3319–23. doi:10.1073/pnas.85.10.3319. PMC 280200. PMID 3368442. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=280200.
Leto TL, Adams AG, de Mendez I (1994). "Assembly of the phagocyte NADPH oxidase: binding of Src homology 3 domains to proline-rich targets.". Proc. Natl. Acad. Sci. U.S.A. 91 (22): 10650–4. doi:10.1073/pnas.91.22.10650. PMC 45079. PMID 7938008. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=45079.
Leusen JH, Bolscher BG, Hilarius PM, et al. (1994). "156Pro-->Gln substitution in the light chain of cytochrome b558 of the human NADPH oxidase (p22-phox) leads to defective translocation of the cytosolic proteins p47-phox and p67-phox.". J. Exp. Med. 180 (6): 2329–34. doi:10.1084/jem.180.6.2329. PMC 2191792. PMID 7964505. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2191792.
Ushio-Fukai M, Zafari AM, Fukui T, et al. (1996). "p22phox is a critical component of the superoxide-generating NADH/NADPH oxidase system and regulates angiotensin II-induced hypertrophy in vascular smooth muscle cells.". J. Biol. Chem. 271 (38): 23317–21. doi:10.1074/jbc.271.38.23317. PMID 8798532.
Yagisawa M, Yuo A, Yonemaru M, et al. (1996). "Superoxide release and NADPH oxidase components in mature human phagocytes: correlation between functional capacity and amount of functional proteins.". Biochem. Biophys. Res. Commun. 228 (2): 510–6. doi:10.1006/bbrc.1996.1691. PMID 8920944.
Sathyamoorthy M, de Mendez I, Adams AG, Leto TL (1997). "p40(phox) down-regulates NADPH oxidase activity through interactions with its SH3 domain.". J. Biol. Chem. 272 (14): 9141–6. doi:10.1074/jbc.272.14.9141. PMID 9083043.
Rinckel LA, Faris SL, Hitt ND, Kleinberg ME (1999). "Rac1 disrupts p67phox/p40phox binding: a novel role for Rac in NADPH oxidase activation.". Biochem. Biophys. Res. Commun. 263 (1): 118–22. doi:10.1006/bbrc.1999.1334. PMID 10486263.
Yamada M, Ariga T, Kawamura N, et al. (2000). "Genetic studies of three Japanese patients with p22-phox-deficient chronic granulomatous disease: detection of a possible common mutant CYBA allele in Japan and a genotype-phenotype correlation in these patients.". Br. J. Haematol. 108 (3): 511–7. doi:10.1046/j.1365-2141.2000.01857.x. PMID 10759707.
Grizot S, Grandvaux N, Fieschi F, et al. (2001). "Small angle neutron scattering and gel filtration analyses of neutrophil NADPH oxidase cytosolic factors highlight the role of the C-terminal end of p47phox in the association with p40phox.". Biochemistry 40 (10): 3127–33. doi:10.1021/bi0028439. PMID 11258927.
Dahan I, Issaeva I, Gorzalczany Y, et al. (2002). "Mapping of functional domains in the p22(phox) subunit of flavocytochrome b(559) participating in the assembly of the NADPH oxidase complex by "peptide walking".". J. Biol. Chem. 277 (10): 8421–32. doi:10.1074/jbc.M109778200. PMID 11733522.
Mott J, Rikihisa Y, Tsunawaki S (2002). "Effects of Anaplasma phagocytophila on NADPH oxidase components in human neutrophils and HL-60 cells.". Infect. Immun. 70 (3): 1359–66. doi:10.1128/IAI.70.3.1359-1366.2002. PMC 127795. PMID 11854221. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=127795.
Li JM, Shah AM (2002). "Intracellular localization and preassembly of the NADPH oxidase complex in cultured endothelial cells.". J. Biol. Chem. 277 (22): 19952–60. doi:10.1074/jbc.M110073200. PMID 11893732.
Pettit AI, Wong RK, Lee V, et al. (2002). "Increased free radical production in hypertension due to increased expression of the NADPH oxidase subunit p22(phox) in lymphoblast cell lines.". J. Hypertens. 20 (4): 677–83. doi:10.1097/00004872-200204000-00025. PMID 11910303.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

Cytochrome b-245, alpha polypeptide

References

Further reading