ACBP and cholesterol differentially alter fatty acyl CoA utilization by microsomal ACAT

Chao, Hsu; Zhou, Minglong; McIntosh, Avery L.; Schroeder, Friedhelm; Kier, Ann B.

doi:10.1194/jlr.m200191-jlr200

Cited by 59 publications

(51 citation statements)

References 51 publications

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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 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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Section: Immunostaining Of Paraffi N-embedded Tissuesmentioning

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

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“…in [8,15,31]. Based on in vitro studies, the primordial role of ACBP has been thought to maintain a cytosolic pool of acyl-CoAs protected from acyl-CoA hydrolases, thus making acyl-CoAs available to several cytoplasmic membrane-bound organelles involved in lipid metabolism, such as to: endoplasmic reticulum (ER) for transacylation to cholesteryl esters, triacylglycerides, or glycerophospholipids [4,5,15,21]; mitochondria for transacylation to acylcarnitines for oxidation [1,3,34]; and the Golgi complex for regulating vesicle budding to form transport vesicles [32,33]. At the nuclear membrane and in the nuclear matrix, ACBP may modulate gene expression, as indicated by ACBP-specific transactivation and proximity to nuclear receptors such as hepatocyte nuclear factor-4 α (HNF-4α) in fixed cells [31].…”

Section: Introductionmentioning

confidence: 99%

Structural and functional characterization of a new recombinant histidine-tagged acyl coenzyme A binding protein (ACBP) from mouse

Petrescu

Huang

Hostetler

et al. 2008

Protein Expression and Purification

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Acyl-coenzyme A binding protein (ACBP) has been proposed to transport fatty acyl-CoAs intracellularly, facilitating their metabolism. In this study, a new mouse recombinant ACBP was produced by insertion of a histidine (his) tag at the C-terminus to allow efficient purification by Niaffinity chromatography. The his-tag was inserted at the C-terminus since ACBP is a small molecular size (10 kDa) protein whose structure and activity are sensitive to amino acid substitutions in the Nterminus. The his tag had no or little effect on ACBP structure or ligand binding affinity and specificity. His-ACBP bound the naturally-occurring fluorescent cis-parinaroyl-CoA with very high affinity (K d =2.15 nM), but exhibited no affinity for non-esterified cis-parinaric acid. To determine if the presence of the C-terminal his tag altered ACBP interactions with other proteins, direct binding to hepatocyte nuclear factor 4α (HNF-4α), a nuclear receptor regulating transcription of genes involved in lipid metabolism, was examined. His-ACBP and HNF-4α were labeled with Cy5 and Cy3, respectively, and direct interaction was determined by a novel fluorescence resonance energy transfer (FRET) binding assay. FRET analysis showed that his-ACBP directly interacted with HNF-4α (intermolecular distance of 73 Å) at high affinity (K d =64-111 nM) similar to native ACBP. The his-tag also had no effect on ACBPs ability to interact with and stimulate microsomal enzymes utilizing or forming fatty acyl CoA. Thus, C-terminal his-tagged-ACBP maintained very similar structural and functional features of the untagged native protein and can be used in further in vitro experiments that require pure recombinant ACBP.

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“…Long-chain acyl-CoA esters can be inhibitory for the activity of acyl-CoA-producing enzymes (3,5), and binding to ACBPs opposes product feedback inhibition. Conversely, acyl-CoAs bound to acylCoA binding proteins appear to represent the preferred form of the substrate for acyl-CoA-utilizing enzymes (5,6). It has also been suggested that the acyl-CoA/ACBP complex interacts with utilizing enzymes (7).…”

mentioning

confidence: 99%

Characterization of an acyl-coenzyme A binding protein predominantly expressed in human primitive progenitor cells

Soupène¹,

Serikov²,

Kuypers³

2008

Journal of Lipid Research

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Human acyl-coenzyme A binding domain-containing member 6 (ACBD6) is a modular protein that carries an acyl-CoA binding domain at its N terminus and two ankyrin motifs at its C terminus. ACBD6 binds long-chain acyl-CoAs with a strong preference for unsaturated, C18: 1-CoA and C20:4-CoA, over saturated, C16:0-CoA, acyl species. Deletion of the C terminus, which is not conserved among the members of this family, did not affect the binding capacity or the substrate specificity of the protein.

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ACBP and cholesterol differentially alter fatty acyl CoA utilization by microsomal ACAT

Cited by 59 publications

References 51 publications

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

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

Structural and functional characterization of a new recombinant histidine-tagged acyl coenzyme A binding protein (ACBP) from mouse

Characterization of an acyl-coenzyme A binding protein predominantly expressed in human primitive progenitor cells

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