Acyl-CoA binding proteins; structural and functional conservation over 2000 MYA

Færgeman, Nils J.; Wadum, Majken; Feddersen, Søren; Burton, Mark; Kragelund, Birthe B.; Knudsen, Jens

doi:10.1007/s11010-005-9040-3

Cited by 79 publications

(83 citation statements)

References 98 publications

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“…Cytosolic low-molecular mass (approximately 10 kD) acyl-coenzyme A-binding protein (ACBP) consists of a four-a-helix domain capable of binding acyl-CoAs with high affinity in a wide range of eukaryotic organisms (Faergeman et al, 2007). It is believed to serve a housekeeping function of maintaining free acyl-CoA concentrations at low nanomolar levels and, thus, prevents micelle formation and the partitioning of acyl-CoA into membranes (Knudsen et al, 1999).…”

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confidence: 99%

Production of a Brassica napus Low-Molecular Mass Acyl-Coenzyme A-Binding Protein in Arabidopsis Alters the Acyl-Coenzyme A Pool and Acyl Composition of Oil in Seeds

et al. 2014

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Low-molecular mass (10 kD) cytosolic acyl-coenzyme A-binding protein (ACBP) has a substantial influence over fatty acid (FA) composition in oilseeds, possibly via an effect on the partitioning of acyl groups between elongation and desaturation pathways. Previously, we demonstrated that the expression of a Brassica napus ACBP (BnACBP) complementary DNA in the developing seeds of Arabidopsis (Arabidopsis thaliana) resulted in increased levels of polyunsaturated FAs at the expense of eicosenoic acid (20:1 cisD11 ) and saturated FAs in seed oil. In this study, we investigated whether alterations in the FA composition of seed oil at maturity were correlated with changes in the acyl-coenzyme A (CoA) pool in developing seeds of transgenic Arabidopsis expressing BnACBP. Our results indicated that both the acyl-CoA pool and seed oil of transgenic Arabidopsis lines expressing cytosolic BnACBP exhibited relative increases in linoleic acid (18:2 cisD9,12 ; 17.9%-44.4% and 7%-13.2%, respectively) and decreases in 20:1 cisD11 (38.7%-60.7% and 13.8%-16.3%, respectively). However, alterations in the FA composition of the acylCoA pool did not always correlate with those seen in the seed oil. In addition, we found that targeting of BnACBP to the endoplasmic reticulum resulted in FA compositional changes that were similar to those seen in lines expressing cytosolic BnACBP, with the most prominent exception being a relative reduction in a-linolenic acid (18:3 cisD9,12,15 ) in both the acyl-CoA pool and seed oil of the former (48.4%-48.9% and 5.3%-10.4%, respectively). Overall, these data support the role of ACBP in acyl trafficking in developing seeds and validate its use as a biotechnological tool for modifying the FA composition of seed oil.

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confidence: 99%

Production of a Brassica napus Low-Molecular Mass Acyl-Coenzyme A-Binding Protein in Arabidopsis Alters the Acyl-Coenzyme A Pool and Acyl Composition of Oil in Seeds

et al. 2014

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“…It is highly conserved throughout evolution and expressed in all cell types in the eukaryotes investigated (1,2). This, together with the characteristics of the ACBP promoter (3,4), implies a housekeeping function of the gene.…”

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confidence: 99%

Disruption of the Acyl-CoA-binding Protein Gene Delays Hepatic Adaptation to Metabolic Changes at Weaning

Neess¹,

Bloksgaard²,

Bek³

et al. 2011

Journal of Biological Chemistry

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The mouse acyl-CoA-binding protein (ACBP) 5 /diazepam binding inhibitor is a 10-kDa intracellular protein consisting of 86 amino acids. It is highly conserved throughout evolution and expressed in all cell types in the eukaryotes investigated (1, 2). This, together with the characteristics of the ACBP promoter (3, 4), implies a housekeeping function of the gene. However, expression levels vary markedly between tissues (5) and in response to different metabolic stimuli (6 -9), thereby indicating that ACBP might perform more specialized functions in some cell types. The ACBP protein binds C 14 -C 22 acyl-CoA esters with high affinity and specificity (10, 11) and has very little or no affinity toward other ligands (11-13). From in vitro studies, ACBP is known to protect acyl-CoA esters from hydrolysis (14 -16) and to relieve acyl-CoA inhibition of a number of enzymes, including long chain acyl-CoA synthetase, acetyl-CoA carboxylase (ACC), adenine nucleotide translocase, fatty acid synthetase (FAS), carnitine palmitoyltransferase, and acyl-CoA:cholesterol acyltransferase (9, 16 -18). In addition, ACBP is known to donate acyl-CoA esters to phospholipid, glycerolipid, and cholesteryl ester (CE) synthesis (14, 18 -21). Finally, proteolytic products of secreted ACBP have been shown to have signaling functions in Dictyostelium as well as mammalian cells (22). Targeted disruption of the yeast ACBP gene (ACB1) revealed that ACBP deficiency results in increased levels of C18:0 acyl-CoA esters and a decrease in the amount of total C26:0 fatty acids, indicating that transport of FA toward elongation is impaired by lack of ACBP. Furthermore, sphingolipid and ceramide amounts were reduced, membrane structure was altered, and vesicular transport was compromised (23-25).The functions of ACBP in lipid metabolism have been further studied in different mammalian cell culture systems and animal models by both knockdown strategies and overexpression of the protein. It has been reported that knockdown of ACBP by small interfering RNA causes growth arrest and lethality in three different mammalian cell lines (26); however, data from our laboratory show that ACBP can be knocked down in many different cell systems without affecting growth and survival (27). 6 Recently, knockdown of ACBP in HepG2 cells was shown to suppress the expression of a number of genes involved in lipid biosynthesis and lead to decreased levels of saturated and monounsaturated fatty acids (28). In 3T3-L1 preadipocytes, knockdown of ACBP caused a mild impairment of adipocyte differentiation and accumulation of triacylglycerol (TAG) (27), whereas overexpression of ACBP in McA-RH7777 rat hepatoma cells resulted in increased intracellular TAG accumulation (29). Overexpression of ACBP in transgenic mice resulted in accumulation of different lipid classes, including TAG in the liver (30). These results suggest *

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“…In rats fasting for 24 hours significantly decreased tissue levels of ACBP in the liver, whereas feeding of a high-fat diet for 48 hours caused ACBP levels to increase [18]. In rainbow trout, the grouth rate of domesticated species were higher than wild species, ACBP expressinon changed in muscle and liver, the genes of domesticated fish mainly for the regulation and control, and a strong ability to control cell division and regulation of structural genes [19].…”

Section: Discussionmentioning

confidence: 97%

“…Acyl-CoA binding protein (ACBP) was known as diazepam binding inhibitor(DBI)/endozepine(EP), is a highly conserved, approximately 10 kDa cytosolic protein [1]. ACBP binds saturated and unsaturated C14-C22 acyl-CoA esters in a one-to-one binding mode with high specificity and affinity(Kd=2^10 nm) [2].…”

Section: Introductionmentioning

confidence: 99%

Acyl-CoA Binding Protein (ACBP) Encoding Gene the Relationship Between Expression Analysis and Different Conditions in Onychostoma Macrolepis

Yang¹,

Xu²,

Li³

et al. 2013

IJBBB

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Abstract-One Acyl-CoA binding protein(ACBP) encoding gene was isolated from testis of Onychostoma macrolepis using homologous cloning and the RACE method. The full Oma-ACBP cDNA(GenBank accession no: JN254628) was 503 bp long and comprised 37 bp of the 5′-Untranslated Regions(UTR), 267 bp of the coding sequence(CDS) encoding a 88 amino acid proteins, and 199 bp of the 3'-Untranslated Regions(UTR) with the polyA tail. A condensed phylogenetic tree show that Oma-ACBP had similarities with vasas of fish species and even mammal and amphibian species, The Oma-ACBP shared 92% sequenced identity with Cyprinus carpio and 91% with Carassius auratus, including a conserved FABP domain, the result enriches our understanding in the study of sequence classification in Onychostoma macrolepis. The Quantitative real-time PCR analysis demonstrated that Oma-ACBP was highly expressed in intestine, spleen and liver, but weakly in testis, ovary, heart, brain, cheek, muscle and eye. It was highly expressed in liver and spleen(42% of dietary protein), weakly expressed in intestine (52% of dietary protein). In starvation challenge, the expression was weakly expressed from 5 day to 8 day, and highly expressed from 3 day to 5 day, and the expression kept stabilizing until the end of the experiment.

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Acyl-CoA binding proteins; structural and functional conservation over 2000 MYA

Cited by 79 publications

References 98 publications

Production of a Brassica napus Low-Molecular Mass Acyl-Coenzyme A-Binding Protein in Arabidopsis Alters the Acyl-Coenzyme A Pool and Acyl Composition of Oil in Seeds

Production of a Brassica napus Low-Molecular Mass Acyl-Coenzyme A-Binding Protein in Arabidopsis Alters the Acyl-Coenzyme A Pool and Acyl Composition of Oil in Seeds

Disruption of the Acyl-CoA-binding Protein Gene Delays Hepatic Adaptation to Metabolic Changes at Weaning

Acyl-CoA Binding Protein (ACBP) Encoding Gene the Relationship Between Expression Analysis and Different Conditions in Onychostoma Macrolepis

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