Document Detail

A cholesterol-binding and transporting protein from rat liver mitochondria.
MedLine Citation:
PMID:  12488045     Owner:  NLM     Status:  MEDLINE    
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 prerequisite 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 phosphorylation in malignant tumor mitochondria.
Andrew M Campbell; Aaron Capuano; Samuel H P Chan
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Biochimica et biophysica acta     Volume:  1567     ISSN:  0006-3002     ISO Abbreviation:  Biochim. Biophys. Acta     Publication Date:  2002 Dec 
Date Detail:
Created Date:  2002-12-18     Completed Date:  2003-02-12     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  0217513     Medline TA:  Biochim Biophys Acta     Country:  Netherlands    
Other Details:
Languages:  eng     Pagination:  123-32     Citation Subset:  IM    
Department of Biology, College of Arts and Sciences, Syracuse University, 130 College Place, Syracuse, NY 13244, USA.
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MeSH Terms
Cholesterol / metabolism*
Electrophoresis, Polyacrylamide Gel
Mitochondria, Liver / metabolism*
Protein Binding
Rats, Sprague-Dawley
Grant Support
Reg. No./Substance:

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