A cholesterol-binding and transporting protein from rat liver mitochondria

Andrew M. Campbell, Aaron Capuano, Samuel H.P. Chan

Research output: Contribution to journalArticlepeer-review

13 Scopus citations


In this communication, we present results indicating a protein isolated from rat liver mitochondrial intermembrane space that is capable of binding cholesterol and transporting it between the inner and outer mitochondrial membranes. This protein has a molecular weight of 57.5 kDa by SDS-PAGE; however, under native conditions, there is cholesterol-binding capability only as a 115 kDa dimer. Our data show that this dimeric protein may play a role in the regulation of mitochondrial membrane cholesterol levels, a perquisite for the optimal activity of inner mitochondrial membrane-associated enzyme complexes. In addition, it appears that this protein is largely responsible for the differences in membrane cholesterol levels observed in normal and hepatoma mitochondria, a discrepancy which may help to explain the lack of energy production via oxidative phosporylation in malignant tumor mitochondria.

Original languageEnglish (US)
Pages (from-to)123-132
Number of pages10
JournalBiochimica et Biophysica Acta-Biomembranes
StatePublished - Dec 23 2002


  • Adenine nucleotide transporter
  • Cholesterol-binding protein
  • Mitochondrial membrane

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Cell Biology


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