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Gene Review

CYCS  -  cytochrome c, somatic

Gallus gallus

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Disease relevance of CYCS


High impact information on CYCS

  • Unexpectedly, ANX5(-/-) cells permeabilized in vitro also failed to release mitochondrial cytochrome C, suggesting a possible mechanism for their resistance to apoptosis [4].
  • The specificity of peptide binding was investigated by employing the murine major histocompatibility complex haplotypes I-Ad and I-Ek and fluorescence-labeled peptides of chicken ovalbumin and pigeon cytochrome c, respectively, which are known to be specific for these haplotypes [5].
  • As a result of the elimination of mitochondrial DNA molecules, the establishment of cell populations with a respiration-deficient phenotype was confirmed by measuring cytochrome c oxidase activity as a function of the number of cell generations and the absorption spectrum of mitochondrial cytochromes [6].
  • We discovered that there was high expression in the lens equatorial epithelium (the region of the lens in which differentiation is initiated) of pro-apoptotic molecules such as Bax and Bcl-x(S) and release of cytochrome c from mitochondria [7].
  • Formation of protein tyrosine ortho-semiquinone radical and nitrotyrosine from cytochrome c-derived tyrosyl radical [8].

Biological context of CYCS

  • Analysis of total chicken DNA by genomic blot hybridization indicates that only one cytochrome c gene exists in the chicken genome [9].
  • The two alleles of this single cytochrome c gene have been isolated from a Charon 4A-chicken genomic library [9].
  • The amino acid sequence predicted by these 2 alleles is identical, and agrees with the published chicken cytochrome c protein sequence [9].
  • The remaining antibodies (greater than 70%) bound to the same complex topographic determinant (including residues 3, 103, and 104) on the back surface of pigeon cytochrome c which had been found to dominate the rabbit antibody response to this protein, and to be involved in Ia-restricted T cell stimulation [10].
  • Among the determinants identified were two adjacent genes, one encoding a methyl-accepting chemotaxis protein (MCP), presumably required for proper chemotaxis to a specific environmental component, and another gene encoding a putative cytochrome c peroxidase that may function to reduce periplasmic hydrogen peroxide stress during in vivo growth [11].

Anatomical context of CYCS


Associations of CYCS with chemical compounds

  • The recombinant enzyme has been found to contain the molybdopterin form of the molybdenum cofactor and is active as determined by the sulfite dependent reduction of cytochrome c [15].
  • The linkage region enzyme, viz. galactosyl xylose transferase, distributed with NADH cytochrome c reductase in an earlier and heavier cis compartment [14].
  • Antibodies against native pigeon cytochrome c reacted very poorly with the several cyanogen bromide-cleaved fragments of the molecule, consisting of residues 1 to 65, 1 to 80, 66 to 104, and 81 to 104 [16].
  • The inactivation was preventable by the presence of sulfite, or by the use of cytochrome c as the electron acceptor instead of O2 [17].
  • Osteoclast superoxide production, monitored kinetically by cytochrome c reduction and histochemically by nitroblue tetrazolium reduction staining, was significantly greater in the presence of 121F, but not 29C, Fab treatment [18].

Physical interactions of CYCS

  • Crystallographic structures of the mitochondrial ubiquinol/cytochrome c oxidoreductase (cytochrome bc(1) complex) suggest that the mechanism of quinol oxidation by the bc(1) complex involves a substantial movement of the soluble head of the Rieske iron-sulfur protein (ISP) between reaction domains in cytochrome b and cytochrome c(1) subunits [19].
  • There are two equal and non-interacting cytochrome c binding sites per sulfite oxidase monomer [20].

Enzymatic interactions of CYCS


Other interactions of CYCS

  • One of the sequenced products was identified as subunit I of cytochrome-c oxidase (COX-1), an enzyme which is central to energy metabolism and particularly relevant for developing nervous systems [21].
  • Similar dissociation constants were measured for the binding of these anions by flash photolysis and by steady-state enzyme kinetics using the inhibition of the sulfite/cytochrome c assay reaction for sulfite oxidase [22].
  • After 48 hours, the ultrastructure of superficial tectal layers was analyzed and compared with samples from control tecta injected with cytochrome C. NT-3 increased the number of synapses, synaptic vesicles/profile, synaptic vesicle densities, the number of docked vesicles, and the length of the synaptic profile [23].
  • Twelve hours after addition of the drug, the activities per cell of the mitochondrial enzymes poly A hydrolase (EC 3.1. 4.21), cytochrome c oxidase (EC, and succinate dehydrogenase (EC are greater than that of the control and keep increasing for at least 96 H [24].
  • A peptide, eluted with cytochrome c, called 'big' somatostatin, is the only somatostatin-like immunoreactivity present in the peripheral plasma of the duck [25].

Analytical, diagnostic and therapeutic context of CYCS

  • Comparative sequence analysis with the flanking regions of previously isolated cytochrome c genes (yeast and rat) indicate no significant regions of homology [9].
  • Optical band splitting and electronic perturbations of the heme chromophore in cytochrome C at room temperature probed by visible electronic circular dichroism spectroscopy [26].
  • Chlorophyllin had moderate inhibitory activity, especially on chick cartilage, whereas cytochrome c was inactive in these bioassays [27].
  • Many single-stranded gaps, occurring both individually and clusters, were observed by electron microscopy using either cytochrome c labeling (where the gaps) are thinner than duplex) or gene 32 protein labeling (gaps thicker than duplex) [28].
  • Only one of 10 sequenced products could be identified as cytochrome-c oxidase, subunit I. Northern blot analysis confirmed its twofold upregulation after positive lens wear and also changes in four other unknown genes [29].


  1. Reperfusion, not simulated ischemia, initiates intrinsic apoptosis injury in chick cardiomyocytes. Vanden Hoek, T.L., Qin, Y., Wojcik, K., Li, C.Q., Shao, Z.H., Anderson, T., Becker, L.B., Hamann, K.J. Am. J. Physiol. Heart Circ. Physiol. (2003) [Pubmed]
  2. Avian encephalomyelitis virus nonstructural protein 2C induces apoptosis by activating cytochrome c/caspase-9 pathway. Liu, J., Wei, T., Kwang, J. Virology (2004) [Pubmed]
  3. Cloning and high-level expression of chicken apocytochrome c gene in Escherichia coli. Tong, J.C., Zhu, L.Q., Yang, F.Y. Biochem. Mol. Biol. Int. (1995) [Pubmed]
  4. DT40 cells lacking the Ca2+-binding protein annexin 5 are resistant to Ca2+-dependent apoptosis. Hawkins, T.E., Das, D., Young, B., Moss, S.E. Proc. Natl. Acad. Sci. U.S.A. (2002) [Pubmed]
  5. Specific binding of antigenic peptides to separate alpha and beta chains of class II molecules of the major histocompatibility complex. Rothenhäusler, B., Dornmair, K., McConnell, H.M. Proc. Natl. Acad. Sci. U.S.A. (1990) [Pubmed]
  6. Ethidium bromide-induced loss of mitochondrial DNA from primary chicken embryo fibroblasts. Desjardins, P., Frost, E., Morais, R. Mol. Cell. Biol. (1985) [Pubmed]
  7. The canonical intrinsic mitochondrial death pathway has a non-apoptotic role in signaling lens cell differentiation. Weber, G.F., Menko, A.S. J. Biol. Chem. (2005) [Pubmed]
  8. Formation of protein tyrosine ortho-semiquinone radical and nitrotyrosine from cytochrome c-derived tyrosyl radical. Chen, Y.R., Chen, C.L., Chen, W., Zweier, J.L., Augusto, O., Radi, R., Mason, R.P. J. Biol. Chem. (2004) [Pubmed]
  9. Isolation and characterization of two alleles of the chicken cytochrome c gene. Limbach, K.J., Wu, R. Nucleic Acids Res. (1983) [Pubmed]
  10. The B10.A mouse B cell response to pigeon cytochrome c is directed against the same area of the protein that is recognized by B10.A T cells in association with the Ek beta:Ek alpha Ia molecule. Hannum, C.H., Matis, L.A., Schwartz, R.H., Margoliash, E. J. Immunol. (1985) [Pubmed]
  11. Identification of Campylobacter jejuni genes involved in commensal colonization of the chick gastrointestinal tract. Hendrixson, D.R., DiRita, V.J. Mol. Microbiol. (2004) [Pubmed]
  12. Newcastle disease virus exerts oncolysis by both intrinsic and extrinsic caspase-dependent pathways of cell death. Elankumaran, S., Rockemann, D., Samal, S.K. J. Virol. (2006) [Pubmed]
  13. The initiator caspase, caspase-10beta, and the BH-3-only molecule, Bid, demonstrate evolutionary conservation in Xenopus of their pro-apoptotic activities in the extrinsic and intrinsic pathways. Kominami, K., Takagi, C., Kurata, T., Kitayama, A., Nozaki, M., Sawasaki, T., Kuida, K., Endo, Y., Manabe, N., Ueno, N., Sakamaki, K. Genes Cells (2006) [Pubmed]
  14. Subfractionation of chick embryo epiphyseal cartilage Golgi. Localization of enzymes involved in the synthesis of the polysaccharide portion of proteochondroitin sulfate. Sugumaran, G., Silbert, J.E. J. Biol. Chem. (1991) [Pubmed]
  15. Molecular cloning of rat liver sulfite oxidase. Expression of a eukaryotic Mo-pterin-containing enzyme in Escherichia coli. Garrett, R.M., Rajagopalan, K.V. J. Biol. Chem. (1994) [Pubmed]
  16. Assembled topographic antigenic determinants of pigeon cytochrome c. Hannum, C.H., Margoliash, E. J. Immunol. (1985) [Pubmed]
  17. The mechanisms of inactivation of sulfite oxidase by periodate and arsenite. Gardlik, S., Rajagopalan, K.V. J. Biol. Chem. (1991) [Pubmed]
  18. Inhibition of avian osteoclast bone resorption by monoclonal antibody 121F: a mechanism involving the osteoclast free radical system. Collin-Osdoby, P., Li, L., Rothe, L., Anderson, F., Kirsch, D., Oursler, M.J., Osdoby, P. J. Bone Miner. Res. (1998) [Pubmed]
  19. Steered molecular dynamics simulation of the Rieske subunit motion in the cytochrome bc(1) complex. Izrailev, S., Crofts, A.R., Berry, E.A., Schulten, K. Biophys. J. (1999) [Pubmed]
  20. Sulfite oxidase from chicken liver. Further characterization of the role of carboxyl groups in the reaction with cytochrome c. Ritzmann, M., Bosshard, H.R. Eur. J. Biochem. (1988) [Pubmed]
  21. Cytochrome-c oxidase is one of several genes elevated in marginal retina of the chick embryo. Paraoanu, L.E., Weiss, B., Robitzki, A.A., Layer, P.G. Neuroscience (2005) [Pubmed]
  22. Electron transfer in sulfite oxidase: effects of pH and anions on transient kinetics. Sullivan, E.P., Hazzard, J.T., Tollin, G., Enemark, J.H. Biochemistry (1993) [Pubmed]
  23. Presynaptic neurotrophin-3 increases the number of tectal synapses, vesicle density, and number of docked vesicles in chick embryos. Wang, X., Butowt, R., von Bartheld, C.S. J. Comp. Neurol. (2003) [Pubmed]
  24. Protein content and enzyme levels of cultured chick embryo cells treated with camptothecin and actinomycin D. Morais, R. Can. J. Biochem. (1977) [Pubmed]
  25. The biological activity of duck 'big' somatostatin on chicken adipose tissue. Di Scala-Guenot, D., Strosser, M.T., Mialhe, P. Biochim. Biophys. Acta (1985) [Pubmed]
  26. Optical band splitting and electronic perturbations of the heme chromophore in cytochrome C at room temperature probed by visible electronic circular dichroism spectroscopy. Dragomir, I., Hagarman, A., Wallace, C., Schweitzer-Stenner, R. Biophys. J. (2007) [Pubmed]
  27. Tetrapyrroles as inhibitors of normal cartilage metabolism: relative potency of different compounds. Vassilopoulou-Sellin, R., Oyedeji, C.O. J. Bone Miner. Res. (1988) [Pubmed]
  28. Deoxyribonuclease I generates single-stranded gaps in chromatin deoxyribonucleic acid. Riley, D.E. Biochemistry (1980) [Pubmed]
  29. Changes in retinal and choroidal gene expression during development of refractive errors in chicks. Feldkaemper, M.P., Wang, H.Y., Schaeffel, F. Invest. Ophthalmol. Vis. Sci. (2000) [Pubmed]
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