The function of acyl-CoA-binding protein (ACBP)/diazepam binding inhibitor (DBI)
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The function of acyl-CoA-binding protein (ACBP)/diazepam binding inhibitor (DBI). / Knudsen, J; Mandrup, S; Rasmussen, J T; Andreasen, P H; Poulsen, F; Kristiansen, K.
In: Molecular and Cellular Biochemistry, Vol. 123, No. 1-2, 1993, p. 129-38.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - The function of acyl-CoA-binding protein (ACBP)/diazepam binding inhibitor (DBI)
AU - Knudsen, J
AU - Mandrup, S
AU - Rasmussen, J T
AU - Andreasen, P H
AU - Poulsen, F
AU - Kristiansen, K
N1 - Keywords: Acyl Coenzyme A; Amino Acid Sequence; Animals; Carrier Proteins; Diazepam Binding Inhibitor; Fatty Acids; Humans; Molecular Sequence Data; Sequence Homology, Amino Acid
PY - 1993
Y1 - 1993
N2 - 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.
AB - 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.
U2 - 10.1007/BF01076484
DO - 10.1007/BF01076484
M3 - Journal article
C2 - 8232254
VL - 123
SP - 129
EP - 138
JO - Molecular and Cellular Biochemistry
JF - Molecular and Cellular Biochemistry
SN - 0300-8177
IS - 1-2
ER -
ID: 11231284