First identification of a 2-ketoglutarate/isocitrate transport system in mammalian peroxisomes and its characterization

Biochem Biophys Res Commun. 2006 Oct 6;348(4):1224-31. doi: 10.1016/j.bbrc.2006.07.049. Epub 2006 Jul 20.

Abstract

Peroxisomes contain specific transporter proteins required for the translocation of various metabolites across its membrane. The presence of several members of the ATP-binding cassette (ABC) transporter family is well established, and the characterization of transporters for adenine nucleotides and (pyro)phosphate in the peroxisomal membrane has been described recently. Previously published data strongly suggest the presence of additional transporters that facilitate the translocation of reducing equivalents and acetyl-units across the peroxisomal membrane. In this paper, we demonstrate the presence of transporter activity for 2-ketoglutarate and isocitrate in the peroxisomal membrane, by functional reconstitution of bovine kidney peroxisomal membrane protein in proteoliposomes. This transporter activity is assumed to be required to sustain the activity of intraperoxisomal isocitrate-dehydrogenase, which is involved in the regeneration of NADPH in the peroxisomal matrix.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Biological Transport / drug effects
  • Cattle
  • Centrifugation, Density Gradient
  • Dicarboxylic Acid Transporters / isolation & purification
  • Dicarboxylic Acid Transporters / metabolism*
  • Isocitrates / metabolism*
  • Ketoglutaric Acids / metabolism*
  • Peroxisomes / enzymology
  • Peroxisomes / metabolism*
  • Proteolipids / metabolism
  • Substrate Specificity

Substances

  • Dicarboxylic Acid Transporters
  • Isocitrates
  • Ketoglutaric Acids
  • Proteolipids
  • proteoliposomes
  • isocitric acid