The Gene Encoding Acyl-CoA-binding Protein Is Subject to Metabolic Regulation by Both Sterol Regulatory Element-binding Protein and Peroxisome Proliferator-activated Receptor α in Hepatocytes

Sandberg, Maria Boysen; Bloksgaard, Maria; Durán-Sandoval, Daniel; Duval, Caroline; Staels, Bart; Mandrup, Susanne

doi:10.1074/jbc.m407515200

Cited by 45 publications

(27 citation statements)

References 52 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…7 The targeting vector was generated by replacing exon 2 and parts of introns 1 and 2 with a 2-kb loxP-flanked neomycin resistance cassette under control of the PGK1 (phosphoglycerate kinase 1) promoter. The vector also contained a cassette for negative selection (PGK1 promoter-driven thymidine kinase cassette 5Ј of the Acbp gene).…”

Section: Methodsmentioning

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

Self Cite

View full text Add to dashboard Cite

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 *

show abstract

Section: Methodsmentioning

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

Self Cite

View full text Add to dashboard Cite

show abstract

“…Following 1 h preincubation, 7 Ci/ml [1][2][3][4][5][6][7][8][9][10][11][12][13][14] C]oleic acid (PerkinElmer) complexed to BSA (1:4, BSA:FA) was added to each explant and incubation was continued for an additional 4 h. Explants were then transferred to ice cold 10 mM EDTA in PBS to stop the reaction ( 44 Histological examination of the skin from ACBP Ϫ / Ϫ mice and ACBP +/+ controls revealed that there are no morphological differences between genotypes in either the thick epidermis of the foot ( Fig. 2D, E ) or the skin from the back ( Fig.…”

Section: Fa Elongation Activity Assaymentioning

confidence: 99%

“…The radiolabeled FAMEs were detected using a Molecular Dynamics Storage phosphor screen and Typhoon Trio Scanner (Amersham Biosciences) and quantifi ed by ImageQuant 5.0. The detected FAMEs were normalized to [1][2][3][4][5][6][7][8][9][10][11][12][13][14] C]oleic acid content.…”

Section: Bcecf Fl Uorescence Lifetime Imaging Microscopy On Fresh Moumentioning

confidence: 99%

The acyl-CoA binding protein is required for normal epidermal barrier function in mice

Bloksgaard

Bek

Marcher

et al. 2012

Journal of Lipid Research

Self Cite

View full text Add to dashboard Cite

This article is available online at http://www.jlr.org Supplementary key words stratum corneum • very long chain fatty acids • mono alkyl diacyl glycerol • transepidermal water loss • multiphoton excitation microscopy • lipid mass spectrometryThe acyl-CoA binding protein (ACBP)/diazepam binding inhibitor (DBI) (Entrez Gene ID: 13167) is a 10 kDa intracellular protein that specifi cally binds medium and long chain acyl-CoA esters (C 14 -C 22 ) with very high affi nity (K d ‫ف‬ 1-10 nM) ( 1, 2 ). The protein is expressed in all eukaryotic species and in all mammalian tissues investigated ( 3-5 ); however, expression levels differs markedly between different tissues and cell types examined, with particularly high levels in epithelial cell types and in cells with a high turn-over of fatty acids (FA) ( 6 ). Consistently with this, we have shown that the ACBP gene is activated by lipogenic transcription factors, such as the peroxisome proliferatoractivated receptor ␥ ( 7 ) and members of the sterol-regulatory element binding protein family ( 7-10 ). In vitro studies indicate that ACBP plays a role in transport of acyl-CoA esters and may deliver acyl-CoA esters to phospholipid

show abstract

“…In mice, the ACBP expression level decreased significantly after 24 hours of hunger, and then feeded, the ACBP expression level reach the minimum point after 12 hours, the the ACBP expression returned to normal levels after 24 hours [16]. Another study, cute fasting dramatically reduces ACBP/DBI mRNA levels in the hypothalamus and the ependyma bordering the third and lateral ventricles [21].…”

Section: Discussionmentioning

confidence: 99%

“…In animals, ACBP is also ubiquitously expressed in various tissues such as the intestine, the testis, the brain, and the liver [4]- [16]. Recently, bacterial challenge implicated that ACBP may have a relationship between regulator of immune and Infection responses in shrimp intestine [5].…”

Section: Discussionmentioning

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

View full text Add to dashboard Cite

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.

show abstract

The Gene Encoding Acyl-CoA-binding Protein Is Subject to Metabolic Regulation by Both Sterol Regulatory Element-binding Protein and Peroxisome Proliferator-activated Receptor α in Hepatocytes

Cited by 45 publications

References 52 publications

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

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

The acyl-CoA binding protein is required for normal epidermal barrier function in mice

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

Contact Info

Product

Resources

About