Aging and acyl-CoA binding protein alter mitochondrial glycerol-3-phosphate acyltransferase activity

Kannan, Latha; Knudsen, Jens; Jolly, Christopher A.

doi:10.1016/s1388-1981(02)00367-0

Cited by 36 publications

(30 citation statements)

References 21 publications

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“…Our findings suggest that this preference may not be reflected in the intact cell. Indeed, it has recently been shown that mtGPAT substrate preference depends partially on fatty acid binding protein availability (34). In that study, mtGPAT substrate preference depended on the availability of albumin or acyl-CoA binding protein in the assay media.…”

Section: Figmentioning

confidence: 76%

Overexpression of mitochondrial GPAT in rat hepatocytes leads to decreased fatty acid oxidation and increased glycerolipid biosynthesis

Lindén

William-Olsson

Rhedin

et al. 2004

Journal of Lipid Research

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Glycerol-3-phosphate acyltransferase (GPAT) catalyses the first committed step in glycerolipid biosynthesis. The mitochondrial isoform (mtGPAT) is mainly expressed in liver, where it is highly regulated, indicating that mtGPAT may have a unique role in hepatic fatty acid metabolism. Because both mtGPAT and carnitine palmitoyl transferase-1 are located on the outer mitochondrial membrane, we hypothesized that mtGPAT directs fatty acyl-CoA away from ␤ -oxidation and toward glycerolipid synthesis. Adenoviralmediated overexpression of murine mtGPAT in primary cultures of rat hepatocytes increased mtGPAT activity 2.7-fold with no compensatory effect on microsomal GPAT activity. MtGPAT overexpression resulted in a dramatic 80% reduction in fatty acid oxidation and a significant increase in hepatic diacylglycerol and phospholipid biosynthesis. Following lipid loading of the cells, intracellular triacylglycerol biosynthesis was also induced by mtGPAT overexpression. Changing an invariant aspartic acid residue to a glycine [D235G] in mtGPAT resulted in an inactive enzyme, which helps define the active site required for mammalian mtGPAT function. To determine if obesity increases hepatic mtGPAT activity, two models of rodent obesity were examined and shown to have Ͼ 2-fold increased enzyme activity.Overall, these results support the concept that increased hepatic mtGPAT activity associated with obesity positively contributes to lipid disorders by reducing oxidative processes and promoting de novo glycerolipid synthesis. -Lindén, D., L. William-Olsson, M. Rhedin, A-K. Asztély, J. C. Clapham, and S. Schreyer. Overexpression of mitochondrial GPAT in rat hepatocytes leads to decreased fatty acid oxidation and increased glycerolipid biosynthesis.

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Section: Figmentioning

confidence: 76%

Overexpression of mitochondrial GPAT in rat hepatocytes leads to decreased fatty acid oxidation and increased glycerolipid biosynthesis

Lindén

William-Olsson

Rhedin

et al. 2004

Journal of Lipid Research

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“…Paraffi n sections were mounted on SuperFrostPlus ® microscopic slides, dried over night at room temperature, and stored at (11)(12)(13), glycerolipid ( 14 ), and cholesteryl ester synthesis ( 15 ). In addition, by sequestration of acyl-CoA esters, a number of acyl-CoA feedback-inhibited proteins, including FA synthetase ( 3 ), acetyl CoA carboxylase, and long chain acyl-CoA synthetase ( 16 ), are relieved of acyl-CoA inhibition in vitro.…”

Section: Immunostaining Of Paraffi N-embedded Tissuesmentioning

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%

“…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%

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

Bloksgaard

Bek

Marcher

et al. 2012

Journal of Lipid Research

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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

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“…Subsequently, similar small cytosolic ACBPs were isolated from many eukaryotes and some prokaryotes (Burton et al 2005;Xiao and Chye 2011a). These 10-kDa ACBPs were found to participate in acyl-CoA transport (Rasmussen et al 1994;Schjerling et al 1996) and in the maintenance of intracellular acyl-CoA pools Gaigg et al 2001;Huang et al 2005), in membrane biosynthesis (Gaigg et al 2001;Faergeman et al 2004) and in the regulation of gene expression and enzyme activities related to lipid metabolism (Rasmussen et al 1993;Mandrup et al 1998;Kannan et al 2003;Feddersen et al 2007;Oikari et al 2008).…”

Section: Introductionmentioning

confidence: 99%

Interactions between Arabidopsis acyl-CoA-binding proteins and their protein partners

Chye

2013

Planta

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Protein-protein interactions are at the core of cellular interactomics and are essential for various biological functions. Since proteins commonly function as macromolecular complexes, it is important to identify their interacting partners to better understand their function and the significance in these interactions. The acyl-CoA-binding proteins (ACBPs) of eukaryotes show conservation in the presence of a lipid-binding acyl-CoA-binding domain. In Arabidopsis thaliana, four of six members from the AtACBP family possess ankyrin repeats (AtACBP1 and AtACBP2) or kelch motifs (AtACBP4 and AtACBP5), which can potentially mediate protein-protein interactions. Through yeast twohybrid screens, a dozen putative protein partners interacting with AtACBPs have been isolated from an Arabidopsis cDNA library. Investigations in the past decade on the interaction between AtACBPs and their protein partners have revealed novel roles for AtACBPs, including functions in mediating oxidative stress responses, heavy metal tolerance and oxygen sensing. Recent progress and current questions on AtACBPs and their interactors are discussed in this review.

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Aging and acyl-CoA binding protein alter mitochondrial glycerol-3-phosphate acyltransferase activity

Cited by 36 publications

References 21 publications

Overexpression of mitochondrial GPAT in rat hepatocytes leads to decreased fatty acid oxidation and increased glycerolipid biosynthesis

Overexpression of mitochondrial GPAT in rat hepatocytes leads to decreased fatty acid oxidation and increased glycerolipid biosynthesis

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

Interactions between Arabidopsis acyl-CoA-binding proteins and their protein partners

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