@article{c9c3db100f0611de8478000ea68e967b,
title = "The function of acyl-CoA-binding protein (ACBP)/diazepam binding inhibitor (DBI)",
abstract = "Acyl-CoA-binding protein has been isolated independently by five different groups based on its ability to (1) displace diazepam from the GABAA receptor, (2) affect cell growth, (3) induce medium-chain acyl-CoA-ester synthesis, (4) stimulate steroid hormone synthesis, and (5) affect glucose-induced insulin secretion. In this survey evidence is presented to show that ACBP is able to act as an intracellular acyl-CoA transporter and acyl-CoA pool former. The rat ACBP genomic gene consists of 4 exons and is actively expressed in all tissues tested with highest concentration being found in liver. ACBP consists of 86 amino acid residues and contains 4 alpha-helices which are folded into a boomerang type of structure with alpha-helices 1, 2 and 4 in the one arm and alpha-helix 3 and an open loop in the other arm of the boomerang. ACBP is able to stimulate mitochondrial acyl-CoA synthetase by removing acyl-CoA esters from the enzyme. ACBP is also able to desorb acyl-CoA esters from immobilized membranes and transport and deliver these for mitochondrial beta-oxidation. ACBP efficiently protects acetyl-CoA carboxylase and the mitochondrial ADP/ATP translocase against acyl-CoA inhibition. Finally, ACBP is shown to be able to act as an intracellular acyl-CoA pool former by overexpression in yeast. The possible role of ACBP in lipid metabolism is discussed.",
author = "J Knudsen and S Mandrup and Rasmussen, {J T} and Andreasen, {P H} and F Poulsen and K Kristiansen",
note = "Keywords: Acyl Coenzyme A; Amino Acid Sequence; Animals; Carrier Proteins; Diazepam Binding Inhibitor; Fatty Acids; Humans; Molecular Sequence Data; Sequence Homology, Amino Acid",
year = "1993",
doi = "10.1007/BF01076484",
language = "English",
volume = "123",
pages = "129--38",
journal = "Molecular and Cellular Biochemistry",
issn = "0300-8177",
publisher = "Springer",
number = "1-2",
}