Induction of acyl-CoA-binding protein and its mRNA in 3T3-L1 cells by insulin during preadipocyte-to-adipocyte differentiation

Hansen, H O; Andreasen, Per Hove; Mandrup, Susanne; Kristiansen, Karsten; Knudsen, Jens

doi:10.1042/bj2770341

Cited by 51 publications

(32 citation statements)

References 28 publications

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“…These results suggest that increased ACBP expression may be linked to lipid accumulation. In keeping with that, ACBP expression is drastically induced during adipocyte differentiation of 3T3-L1 preadipocytes (13). This induction is most likely mediated, at least in part, by the peroxisome proliferator-activated receptor ␥ (PPAR␥).…”

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confidence: 61%

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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

Bloksgaard

Durán-Sandoval

et al. 2005

Journal of Biological Chemistry

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The acyl-CoA-binding protein (ACBP) is a 10-kDa intracellular lipid-binding protein that transports acylCoA esters. The protein is expressed in most cell types at low levels; however, expression is particularly high in cells with a high turnover of fatty acids. Here we confirm a previous observation that ACBP expression in rodent liver is down-regulated by fasting, and we show that insulin but not glucose is the inducer of ACBP expression in primary rat hepatocytes. In keeping with the regulation by insulin, we show that ACBP is a sterol regulatory element-binding protein 1c (SREBP-1c) target gene in hepatocytes. Members of the SREBP family activate the rat ACBP gene through binding sites for SREBP and the auxiliary factors Sp1 and nuclear factor Y in the proximal promoter. In addition, we show that ACBP is a peroxisome proliferator-activated receptor (PPAR) ␣ target gene in cultured hepatocytes and is induced in the liver by fibrates in a PPAR␣-dependent manner. Thus, ACBP is a dual PPAR␣ and SREBP-1c target gene in hepatocytes. Fasting leads to reduced activity of SREBP but increased activity of PPAR␣ in hepatocytes, and in keeping with ACBP being a dual target gene, we show that ACBP expression is significantly lower in livers from PPAR␣ knock-out mice than in livers from wild type mice. In conclusion, expression of ACBP in rodent hepatocytes is subject to dual metabolic regulation by PPAR␣ and SREBP-1c, which may reflect the need for ACBP during lipogenic as well as lipo-oxidative conditions.

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confidence: 61%

“…adipocytes and hepatocytes, have high levels of ACBP expression. We have shown previously that ACBP is significantly induced during adipocyte differentiation (13) and is a direct PPAR␥ target gene in adipocytes (10). In this report we have investigated the transcriptional regulation of ACBP expression in hepatocytes.…”

Section: Discussionmentioning

confidence: 99%

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

Bloksgaard

Durán-Sandoval

et al. 2005

Journal of Biological Chemistry

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“…Phenotypical differences between ACBP ϩ/ϩ and ACBP Ϫ/Ϫ pups become evident around 16 days of age, when a significant fur and skin phenotype develops. 8 Around weaning, the ACBP Ϫ/Ϫ mice appear physically weak and display an increased mortality rate unless provided easy access to water and soaked food in the bottom of the cage. The growth rate of the ACBP Ϫ/Ϫ pups is similar to that of ACBP ϩ/ϩ pups until 19 days of age (i.e.…”

Section: Resultsmentioning

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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“…relative contribution of lipids from the Harderian gland to fur lipid in mice is unclear ( 23,42 ), our results indicate that stimulation of the Harderian gland could indeed contribute to fur lipids. We show that, similar to other lipogenic cells ( 4,5,30,31,43 ), the acinar cells of the Harderian gland express very high levels of ACBP. We therefore initially speculated that the Harderian gland phenotype was caused directly by failure to express ACBP in these cells.…”

Section: Impairment Of the Epidermal Barrier Activates The Harderian mentioning

confidence: 80%

“…Immediately thereafter, similar-sized explants (approximately half a gland) were incubated for 2 h in Krebs ringer buffer with 1% fatty acid-free BSA containing 0.5 µCi/ml 14 C-acetic acid ( [1][2][3][4][5][6][7][8][9][10][11][12][13][14] C] acetic acid, sodium salt; Amersham Biosciences) at 37°C. Explants were removed and washed, and the weight was determined.…”

Section: Ex Vivo Secretion Of De Novo Synthesized Madagmentioning

confidence: 99%

Compromised epidermal barrier stimulates Harderian gland activity and hypertrophy in ACBP−/− mice

Bek

Neess

Dixen

et al. 2015

Journal of Lipid Research

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Induction of acyl-CoA-binding protein and its mRNA in 3T3-L1 cells by insulin during preadipocyte-to-adipocyte differentiation

Cited by 51 publications

References 28 publications

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

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

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

Compromised epidermal barrier stimulates Harderian gland activity and hypertrophy in ACBP−/− mice

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