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Institute of Biochemistry, Odense University, DK-5230 Odense M Denmark
3To whom correspondence should be addressed.
 |
ABSTRACT |
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 TOP ABSTRACT Acyl-CoA binding proteinTissue acyl-CoA concentrationsConcentration of acyl-CoA in...Long-chain acyl-CoA-regulated...Functions of long-chain acyl-CoA...The ACBP/acyl-CoA complex as...Regulation of gene expression...SUMMARYREFERENCES |
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KEY WORDS: • acyl-CoA • fatty acids • metabolism • cell signaling
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Acyl-CoA binding protein |
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TOPABSTRACTAcyl-CoA binding proteinTissue acyl-CoA concentrationsConcentration of acyl-CoA in...Long-chain acyl-CoA-regulated...Functions of long-chain acyl-CoA...The ACBP/acyl-CoA complex as...Regulation of gene expression...SUMMARYREFERENCES |
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Acyl-CoA binding protein
(ACBP)4
is an 86–103 residue protein with a highly conserved amino acid
sequence. It has been isolated from a wide range of species including
yeasts, plants, reptiles and humans, but also several proteins
translated from gene sequences, especially from Caenorhabditis
elegans, have been suggested. A total of 30 sequences have been
recognized either as proteins or as gene translates (Kragelund et al., 1999
). From the alignment, at least four groups of ACBP can be
identified (Kragelund et al., 1999
).
The first group is the generally expressed ACBP isoform, first isolated
from bovine liver (l-ACBP). It contains no cysteine and is 86–92
residues long. This basic isoform, which is expressed in almost every
tissue in all eukaryotic species tested including yeast, is most likely
the ancestor of all other more specialized ACBP isoforms. The second
group is the testis specific isoform (t-ACBP) also called
endozepine-like protein (ELP). t-ACBP have now been isolated
from three different species and all t-ACBP contain three cysteine
(Pusch et al. 1996
and 1998
). A putative third group may
be a brain specific isoform of ACBP (b-ACBP), which has been deduced
from gene sequences from duck and frog brain containing one single
cysteine at position 43.
The fourth group of ACBP is a group of longer sequences with up to 533 amino acids. Some of these longer sequences are suggested to be membrane-bound ACBP domain proteins, whereas others remain to be isolated as proteins. Many of these longer forms contain cysteine(s).
A sequence analysis of the entire C.
elegans genome reveals four sequences homologous to ACBP
(Kragelund et al., 1999
). One of these sequences codes for the basic
l-ACBP isoform. The three other sequences read from longer putative
protein sequences containing 125,146 and 385 residues. One of these
proteins encodes a potential acyl-CoA dehydratase (Wilson et al. 1994
). The presence of only the basic short l-ACBP
isoform in C. elegans indicates that the
more specialized isoforms evolved later.
Tissue distribution and content of l-ACBP.
In mammals, the highest concentration of l-ACBP is found in liver,
where it is evenly distributed in all hepatocytes (Bovolin et al. 1990
). In other tissues, l-ACBP is reported to be high
in specialized cells such as steroid-producing cells of the adrenal
cortex and testis, in epithelial cells specialized in secretion and in
water and electrolyte transport, all of which are characterized by a
high energy metabolism. In Drosophila melanogaster,
l-ACBP has been found expressed primarily in tissues that
are associated with high energy production or fat metabolism
(Kolmer et al. 1994
). Its broad range of distribution
throughout the animal and plant kingdom and its high degree of sequence
similarity among different species suggest that l-ACBP is a
housekeeping protein. This was further supported by Mandrup et al. (1992)
who demonstrated that the genomic gene of l-ACBP
has all of the characteristics of a housekeeping gene.
Structure and binding properties.
L-ACBP is folded into a four 
-helix–bundle protein. The
binding site is located in a hydrophobic groove on the surface of
l-ACBP. The acyl chain is buried in the binding pocket and is
completely protected from the aqueous solvent by the acyl-CoA head
group, which forms a lid on the binding pocket by interacting with
specific residues on the rim of the binding cavity. The acyl-CoA
head group is able to bind to l-ACBP with low affinity
(KD = 2 µmol/L
(Robinson et al. 1996
) and plays an important role in
determining binding specificity for acyl-CoA esters only
(Kragelund et al. 1993
). l-ACBP binds medium- and
long-chain acyl-CoA esters with very high affinity, with a
preference for C:14-C:22 acyl-CoA esters (Færgeman et al. 1996
, Rasmussen et al. 1990
, Rosendal et al. 1993
). l-ACBP does not bind fatty acids, acyl
carnitines, cholesterol and a number of nucleotides (Rosendal et al. 1993
). The binding affinities decrease with increasing
ionic strength of the buffer used (Færgeman et al. 1996
).
Function.
A number of in vitro and in vivo experimental results strongly indicate
that ACBP is able to act as an intracellular acyl-CoA transporter
and pool former (Færgeman and Knudsen 1997
). Compelling
evidence that ACBP participates in acyl-CoA transport in vivo has
been obtained from yeast. Disruption of the ACBP-gene in
Saccharomyces cerevisiae results in a dramatic perturbation
of the acyl-CoA level and composition (Schjerling et al. 1996
). The level of total acyl-CoA and stearoyl-CoA was
increased 2.5- and 7.0-fold, respectively. The primary yeast acb1
strain is very slow growing and extremely unstable, and it reverted
with a very high frequency to a faster growing strain. The synthesis of
very-long-chain (26:0) fatty acids was strongly reduced in the primary
acb1 yeast strain (Knudsen, unpublished results).
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Tissue acyl-CoA concentrations |
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TOPABSTRACTAcyl-CoA binding proteinTissue acyl-CoA concentrationsConcentration of acyl-CoA in...Long-chain acyl-CoA-regulated...Functions of long-chain acyl-CoA...The ACBP/acyl-CoA complex as...Regulation of gene expression...SUMMARYREFERENCES |
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, Sterchele et al. 1994
, Tubbs and Garland 1964
), diabetes (Tubbs and Garland 1964
), fat/glucose feeding (Tubbs and Garland 1964
) and ingestion of hypolipidemic drugs (Berge and Bakke 1981
, Berge et al. 1983
, Sterchele et al. 1994
). For example, in rats that were food deprived for
48 h, the total level of acyl-CoA esters increased at least
two- to fourfold (Bortz and Lynen 1963
, Sterchele et al. 1994
).
The compartmentation of long-chain acyl-CoA esters is an important
unsolved problem, and the actual cytosolic concentration of free
long-chain acyl-CoA esters is not known for any tissue. Only a few
attempts to estimate the intracellular distribution of long-chain
acyl-CoA have been reported ( Idell Wenger et al. 1978
,
Moore et al. 1992
, Rasmussen et al. 1993
.
It has been suggested that 20–40% of the total acyl-CoA pool is
cytosolic (Oram et al. 1975
). Deeney et al. (1992)
estimated that the cytosolic long-chain acyl-CoA
level in a clonal ß-cell line constituted ~78% of the total
long-chain acyl-CoA level, giving a cytosolic concentration of 90
µmol/L.
|
Concentration of acyl-CoA in cell cytosol |
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TOPABSTRACTAcyl-CoA binding proteinTissue acyl-CoA concentrationsConcentration of acyl-CoA in...Long-chain acyl-CoA-regulated...Functions of long-chain acyl-CoA...The ACBP/acyl-CoA complex as...Regulation of gene expression...SUMMARYREFERENCES |
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. The concentration of ACBP and long-chain acyl-CoA in liver of fed
rats has been determined to be 40–50 and 40–60 nmol/g tissue,
respectively (Rasmussen et al. 1993
, Sterchele et al. 1994
), indicating that the acyl-CoA/ACBP ratio might be
close to one. At molar ratios of acyl-CoA/ACBP <1, the calculated
concentration of free LCA in the cytosol is <10 nmol/L. As the LCA
concentration reaches the ACBP concentration (50 µmol/L),
the concentration of the unbound acyl-CoA will increase
dramatically and approach the total acyl-CoA concentration.
However, this situation will not appear because at this point, FABP
will take over the LCA buffering function. l-FABP binds
long-chain acyl-CoA with a KD of
~1.0 µmol/L (Rolf et al. 1995
). Assuming
that the maximal obtainable acyl-CoA concentration in liver cytosol
is 150 µmol/L and that the cytosolic FABP concentration is
0.3 mmol/L (0.6 mmol/L binding sites) (Glatz et al. 1988
), the calculated free concentration of acyl-CoA will
never be expected to exceed 200 nmol/L. Long-chain acyl-CoA ester
can also be expected to bind to a number of other proteins in the cell,
including the high affinity binding site on acyl-CoA synthetase and
acyl-CoA–utilizing enzymes, and the above-mentioned putative
membrane-bound ACBP domain proteins. It is tempting to speculate
that membrane-associated ACBP domain proteins bind fatty
acyl-CoA with high affinity and thus, by competing with the
cytosolic ACBP, are able to create a local pool of membrane-bound
acyl-CoA esters.
|
as
1.5 x105 (mol/L)-1 and as
5 x 105 (mol/L)-1 by
Requero et al. (1995)
. If it is assumed that these
values can be applied also to in vivo conditions, the calculated free
concentration of acyl-CoA in a liver cell in the absence of binding
proteins would be ~1 µmol/L if the LCA is allowed to
partition freely into membranes.
An additional control factor for ensuring low concentrations of LCA
under in vivo conditions is the high activity of acyl-CoA
hydrolases, found in most subcellular compartments (Berge and Farstad 1979
, Berge et al. 1984
, Broustas and Hajra. 1995
, Waku 1992
, Yamada et al. 1996
). The only physiologic role ascribed to these enzymes is
termination of fatty acid synthesis by a medium-chain acyl-CoA
hydrolase in the mammary gland (Knudsen et al. 1975
and 1976
). However, recent results show that a yeast peroxisomal
thioesterase homologous to the human peroxisomal thioesterase hTE is
required for growth on fatty acids (Jones et al. 1999
).
A likely explanation for this very unexpected result might be that free
CoA is required for the ß-oxidation process. The function of the
thioesterase would be to "scavenge" excess LCA to ensure sufficient
free CoA for ß-oxidation and to prevent partitioning of LCA into
membranes. This mechanism would require a specific peroxisomal LCA
binding protein to form a protected pool of LCA for ß-oxidation in
the mitochondria. This function might very well be performed by sterol
carrier protein 2 (SCP2; Fig. 1
), which has been shown to be
peroxisomal and to bind LCA with high affinity (Wirtz et al. 1998
). We suggest a similar functional relationship between
cytosolic acyl-CoA hydrolases and ACBP. Finally, large fluctuations
in the cytosolic concentration of free LCA esters will be expected to
be prevented by feedback inhibition of the acyl-CoA synthetase
(Ki = 4 µmol/L)
(Pande 1973
).
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Long-chain acyl-CoA–regulated cell functions |
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TOPABSTRACTAcyl-CoA binding proteinTissue acyl-CoA concentrationsConcentration of acyl-CoA in...Long-chain acyl-CoA-regulated...Functions of long-chain acyl-CoA...The ACBP/acyl-CoA complex as...Regulation of gene expression...SUMMARYREFERENCES |
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).
A major problem involved in performing these types of experiments and
evaluating their physiologic significance is the concentration of LCA
used and the physiochemical conditions under which these experiments
are performed. LCA is an amphipathic molecule and forms micelles at low
concentrations. The critical micellar concentration ranges from 5 to
200 µmol/L depending on chain length, number of double
bonds in the acyl chain and salt concentration (Færgeman and Knudsen 1997
). The actual free concentration is therefore
unknown, if the critical micellar concentration has not been determined
under the experimental conditions used. A further critical problem is
the fact that LCA readily partitions into membranes (see above). In a
large number of the reported experiments with membrane-bound
enzymes and ion channels, acyl-CoA esters have been added directly
to the membrane suspension without the addition of an acyl-CoA
buffering protein. Under these conditions, the added acyl-CoA
esters will accumulate to a very high concentration in/on the membrane.
The concentration of LCA that the enzyme or ion channel is exposed to
might therefore be much higher than the added concentration.
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Functions of long-chain acyl-CoA in cellular regulation |
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TOPABSTRACTAcyl-CoA binding proteinTissue acyl-CoA concentrationsConcentration of acyl-CoA in...Long-chain acyl-CoA-regulated...Functions of long-chain acyl-CoA...The ACBP/acyl-CoA complex as...Regulation of gene expression...SUMMARYREFERENCES |
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) will be expected to be
limited to the regulation of acetyl-CoA carboxylase and gene
expression in Escherichia coli, unless the acyl-CoA/ACBP
complex can donate acyl-CoA directly to the regulatory protein in
question or the complex itself can act as a regulator or enzyme
substrate. |
The ACBP/acyl-CoA complex as enzyme substrate and regulator |
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TOPABSTRACTAcyl-CoA binding proteinTissue acyl-CoA concentrationsConcentration of acyl-CoA in...Long-chain acyl-CoA-regulated...Functions of long-chain acyl-CoA...The ACBP/acyl-CoA complex as...Regulation of gene expression...SUMMARYREFERENCES |
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).
ACBP also stimulated incorporation of arachidonic acid from
arachidonoyl-CoA into phospholipids by the
acyl-CoA-lysophospholipid acyltransferase in red blood cells at low
arachidonoyl-CoA concentrations (Fyrst et al. 1995
).
This situation is not unique for ACBP bound ligands. It has been
demonstrated recently that the retinal/cellular retinol binding protein
(CRBP) complex rather than free retinal is the preferred substrate for
lecithin-retinol acyltransferase (Ong. 1994
) and for
the microsomal retinol dehydrogenase (Boerman and Napoli. 1996
). The ability of the acyl-CoA/ACBP complex to donate
acyl-CoA to utilizing or acyl-CoA–regulated systems is not
universal. Acetyl-CoA carboxylase was completely protected
against inhibition by acyl-CoA at all concentrations up to 5
µmol/L at acyl-CoA/ACBP ratios <0.8 (Rasmussen et al. 1994
). It is tempting, therefore, to speculate that, by
binding LCAA, ACBP creates a pool of long-chain acyl-CoA available
for specific purposes only.
The regulatory functions of the ACBP/acyl-CoA complex were investigated
in experiments with the ryanodine receptor Ca2+
release channel from rabbit muscle terminal cisternae. This channel has
been shown to be activated by palmitoyl-CoA in the micromolar range
(Fulceri et al. 1994
). In these experiments,
palmitoyl-CoA (6 µmol/L) was added to the rabbit
muscle terminal cisternae without the addition of an acyl-CoA
buffering protein. However, palmitoyl-CoA appeared to act directly
on the channel. Both palmitoyl-CoA and its nonhydrolysable ether
analog were able to activate it, and the activation could be blocked by
the specific channel blocker Ruthenium red (Fulceri et al. 1994
). To elucidate the role of ACBP in the regulation of the
channel, we decided to reinvestigate the activation of the ryanodine
receptor by LCA in the presence of physiologic concentrations of ACBP.
Addition of 6 µmol/L palmitoyl-CoA in the presence
of 6.6 µmol/L bovine ACBP to the terminal cisternae
did not affect Ca2+ release significantly; but it reduced
significantly the rate of reuptake of an added Ca2+ pulse.
However, preincubation of the terminal cisternae membranes with
increasing concentrations of palmitoyl-CoA/ACBP complex strongly
potentiated caffeine-induced Ca2+ release. This effect
was proportional to the complex concentration and independent of the
calculated free palmitoyl-CoA concentration (Fulceri et al. 1997
). These results strongly indicate that the acyl-CoA/ACBP
complex can either donate acyl-CoA directly to the ryanodine
receptor or act as a regulator of the receptor itself.
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Regulation of gene expression by long-chain acyl-CoA ester and ACBP |
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TOPABSTRACTAcyl-CoA binding proteinTissue acyl-CoA concentrationsConcentration of acyl-CoA in...Long-chain acyl-CoA-regulated...Functions of long-chain acyl-CoA...The ACBP/acyl-CoA complex as...Regulation of gene expression...SUMMARYREFERENCES |
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).
However, a mutant strain of S. cerevisiae that is
defective in acyl-CoA synthetase exhibits little repression of
acetyl-CoA carboxylase by fatty acids, indicating that the
activation of exogenously supplied fatty acids is required for
repression of acetyl-CoA carboxylase (Kamiryo et al. 1976
). Similar observations have been made with regard to
repression of transcription of the OLE1 gene, coding for the
9-desaturase, by 9-unsaturated fatty acids in yeast (Choi et al. 1996
). These observations, combined with the observation
that deletion of the yeast ACB1 gene, coding for yeast ACBP, induced a
three- to fivefold increase in the level of 9- desaturase mRNA
(Choi et al. 1996
, Schjerling et al. 1996,
) strongly indicate that ACBP is involved in donating LCA
for gene regulation.
In E. coli, fatty acid biosynthesis and
degradation are coordinately regulated at a transcriptional level by
the product of the fadR gene, FadR (DiRusso et al. 1992
). Using DNA-protein gel retardation assays,
DiRusso et al. (1992)
demonstrated that binding of
purified FadR to DNA containing the fadB-promoter was
prevented by LCA, but not by short-chain acyl-CoA esters and fatty
acids. The Ki for palmitoyl-CoA
and oleoyl-CoA was ~5 nmol/L, and for myristoyl-CoA and
decanoyl-CoA 250 nmol/L and 2 amol/L, respectively. These data
provide strong evidence that long-chain acyl-CoA esters bind to
FadR and thereby inhibit DNA-binding activity of FadR. A direct
interaction between long-chain acyl-CoA and FadR was shown with the
use of a fluorescence quenching assay; the
KD for FadR binding of oleoyl-CoA
was determined to be 12.1 nmol/L (Raman and DiRusso 1995
).
The above-mentioned repression of acetyl-CoA carboxylase and
9-desaturase strongly indicates that a transcription factor similar
to FadR might also exist in yeast and that ACBP may play a role in
regulation of gene expression by delivering LCA to, or interact
directly with this transcription factor.
Reduction of ACBP expression in 3T3-L1 cells by expression of an ACBP
antisense cDNA has been shown to block differentiation into adipocytes
(Baldursson et al. 1995
, Mandrup et al. 1998
). The cause of this defect at the molecular level is
unknown. One difficulty in explaining these results is the fact that
there is no correlation between the inhibitory effect of the antisense
and the antisense RNA expression level and ACBP level (Knudsen,
unpublished results).
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SUMMARY |
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TOPABSTRACTAcyl-CoA binding proteinTissue acyl-CoA concentrationsConcentration of acyl-CoA in...Long-chain acyl-CoA-regulated...Functions of long-chain acyl-CoA...The ACBP/acyl-CoA complex as...Regulation of gene expression...SUMMARYREFERENCES |
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ACKNOWLEDGMENTS |
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FOOTNOTES |
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2 Supported by CISFEM Carlsberg Foundation and The Danish Natural Science Research Council.
4 Abbreviations used: ACBP, acyl-CoA binding protein; ACC, acetyl-CoA carboxylase; CRBP, cellular retinol binding protein; FABP, fatty acid binding protein; LCA, long-chain acyl-CoA ester.
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REFERENCES |
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TOPABSTRACTAcyl-CoA binding proteinTissue acyl-CoA concentrationsConcentration of acyl-CoA in...Long-chain acyl-CoA-regulated...Functions of long-chain acyl-CoA...The ACBP/acyl-CoA complex as...Regulation of gene expression...SUMMARYREFERENCES |
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