J. Lipid Res.
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Journal of Lipid Research, Vol. 41, 538-545, April 2000
Copyright © 2000 by Lipid Research, Inc.

Original Article

Long-chain acyl-CoA esters and acyl-CoA binding protein are present in the nucleus of rat liver cells

Morten Elholma,b, Alexis Garrasa, Søren Nevec, Ditte Tornehaved, Tommy Byskov Lunde, Jon Skorvea, Torgier Flatmarkb, Karsten Kristiansenc, and Rolf Kristian Bergea
a Department of Clinical Chemistry, University of Bergen, N-5021 Bergen, Norway
b Institute of Biochemistry and Molecular Biology, University of Bergen, N-5009 Bergen, Norway
c Department of Molecular Biology, University of Southern Denmark, Odense, DK-5230 Odense M., Denmark
d Department of Anatomy and Cell Biology, Institute of Medical Biology, University of Southern Denmark, Odense, Winsløwparken 19, DK-5000 Odense C., Denmark
e Institute of Human Genetics, Aarhus University, 8000 Aarhus C., Denmark

Correspondence to: Morten Elholm

A detailed analysis of the subcellular distribution of acyl-CoA esters in rat liver revealed that significant amounts of long-chain acyl-CoA esters are present in highly purified nuclei. No contamination of microsomal or mitochondrial marker enzymes was detectable in the nuclear fraction. C16:1 and C18:3-CoA esters were the most abundant species, and thus, the composition of acyl-CoA esters in the nuclear fraction deviates notably from the overall composition of acyl-CoA esters in the cell. After intravenous administration of the non-ß-oxidizable [14C]tetradecylthioacetic acid (TTA), the TTA-CoA ester could be recovered from the nuclear fraction. Acyl-CoA esters bind with high affinity to the ubiquitously expressed acyl-CoA binding protein (ACBP), and several lines of evidence suggest that ACBP functions as a pool former and transporter of acyl-CoA esters in the cytoplasm.

By using immunohistochemistry, immunofluorescence microscopy, and immunoelectron microscopy we demonstrate that ACBP localizes to the nucleus as well as the cytoplasm of rat liver cell and rat hepatoma cells, suggesting that ACBP may also be involved in regulation of acyl-CoA-dependent processes in the nucleus.—Elholm, M., A. Garras, S. Neve, D. Tornehave, T. B. Lund, J. Skorve, T. Flatmark, K. Kristiansen, and R. K. Berge. Long-chain acyl-CoA esters and acyl-CoA binding protein are present in the nucleus of rat liver cells. J. Lipid Res. 2000. 41: 538;–545.

Supplementary key words: long-chain acyl-CoA, acyl-CoA binding protein, nuclear localization, tetradecylthioacetic acid


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