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VDAC1  -  voltage-dependent anion channel 1

Bos taurus

 
 
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High impact information on VDAC1

  • In situ localization substantiated that the BR1-VDAC is associated with the plasmalemma of astrocytes [1].
  • In protein extracts of bovine spermatozoa, VDAC1, -2, and -3 were detected by specific antibodies, while only VDAC2 and -3 were found as solubilized proteins derived from purified bovine ODFs [2].
  • In addition to the voltage-dependent anion channel (VDAC), mitochondrial outer membranes contain a cationic channel of large conductance, which is blocked by a mitochondrial addressing peptide (peptide-sensitive channel, PSC) [3].
  • VDAC channels switch to lower-conductive closed states at high membrane potentials [4].
  • Characterization and partial purification of the VDAC-channel-modulating protein from calf liver mitochondria [4].
 

Analytical, diagnostic and therapeutic context of VDAC1

  • Simple perfusion of the chamber did not reverse the effect of the modulator on VDAC [4].

References

  1. Cloning and in situ localization of a brain-derived porin that constitutes a large-conductance anion channel in astrocytic plasma membranes. Dermietzel, R., Hwang, T.K., Buettner, R., Hofer, A., Dotzler, E., Kremer, M., Deutzmann, R., Thinnes, F.P., Fishman, G.I., Spray, D.C. Proc. Natl. Acad. Sci. U.S.A. (1994) [Pubmed]
  2. Voltage-dependent anion-selective channels VDAC2 and VDAC3 are abundant proteins in bovine outer dense fibers, a cytoskeletal component of the sperm flagellum. Hinsch, K.D., De Pinto, V., Aires, V.A., Schneider, X., Messina, A., Hinsch, E. J. Biol. Chem. (2004) [Pubmed]
  3. Solubilization and reconstitution of the mitochondrial peptide-sensitive channel. Fèvre, F., Henry, J.P., Thieffry, M. J. Bioenerg. Biomembr. (1993) [Pubmed]
  4. Characterization and partial purification of the VDAC-channel-modulating protein from calf liver mitochondria. Liu, M.Y., Torgrimson, A., Colombini, M. Biochim. Biophys. Acta (1994) [Pubmed]
 
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