Solubilization of a long chain fatty acyl-CoA synthetase from chicken adipose tissue microsomes

Banis, R. J.; Tove, S. B.

doi:10.1016/0005-2760(74)90232-x

Cited by 60 publications

(18 citation statements)

References 15 publications

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“…Acyl-CoA synthetase activity was measured in the presence of 175 mM Tris, pH 7.4, 8 mM MgCl 2 , 5 mM dithiothreitol, 10 mM ATP, 250 M CoA, and 50 (22). Only initial rates were measured.…”

Section: Cell Homogenate Preparations For Acsl Activity and Protein Amentioning

confidence: 99%

Rat Long Chain Acyl-CoA Synthetase 5 Increases Fatty Acid Uptake and Partitioning to Cellular Triacylglycerol in McArdle-RH7777 Cells

Mashek

McKenzie

Horn

et al. 2006

Journal of Biological Chemistry

110

105

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Long chain acyl-CoA synthetase (ACSL) catalyzes the initial step in long chain fatty acid metabolism. Of the five mammalian ACSL isoforms cloned and characterized, ACSL5 is the only isoform found to be located, in part, on mitochondria and thus was hypothesized to be involved in fatty acid oxidation. To elucidate the specific roles of ACSL5 in fatty acid metabolism, we used adenoviralmediated overexpression of ACSL5 (Ad-ACSL5) in rat hepatoma McArdle-RH7777 cells. Confocal microscopy revealed that Ad-ACSL5 colocalized to both mitochondria and endoplasmic reticulum. When compared with cells infected with Ad-GFP, Ad-ACSL5-infected cells at 24 h after infection had 2-fold higher acyl-CoA synthetase activities and 30% higher rates of fatty acid uptake when incubated with 500 Acyl-CoA synthetase catalyzes the initial step in mammalian fatty acid metabolism. In this reaction, fatty acid, CoA, and ATP are used to form acyl-CoA and AMP. Acyl-CoAs have diverse metabolic fates within the cell and can be used to acylate proteins or be metabolized through catabolic pathways such as ␤-oxidation or anabolic pathways such as de novo synthesis and reacylation of triacylglycerol (TAG), 2 phospholipids, and cholesterol esters.To date, five isoforms of long chain acyl-CoA synthetase have been cloned and shown to possess activity toward long chain fatty acids. The unique pattern of tissue expression, subcellular localization, and differences in substrate preference among the isoforms suggests that individual isoforms have distinct functions. ACSL1, ACSL4, and ACSL5 appear to be the predominant isoforms in rat liver (1-5). ACSL1 and ACSL4 are located in liver endoplasmic reticulum and mitochondrial-associated membrane (6), an endoplasmic reticulum fraction possibly involved in lipoprotein synthesis (7). In addition, ACSL4 is also present on peroxisomes and has a marked preference for C20:4 and C20:5 (2). ACSL5 is the only isoform found in both mitochondrial membranes and endoplasmic reticulum (6) and, similar to ACSL1, has its highest preference for saturated and unsaturated fatty acids of 16 -20 carbons (1). Because ACSL5 is the only ACSL isoform known to be located on mitochondria, it is logical to speculate that it has a role in the ␤-oxidation of fatty acids. In support of this hypothesis, rat liver mitochondrial protein content of ACSL5 increases following a 48-h fast but declines when rats are refed a high sucrose diet for 24 h (6). To date, the most direct studies that focus on ACSL used triacsin C, an inhibitor of ACSL1, ACSL3, and ACSL4 but not ACSL5 or ACSL6 (8, 9). In hepatocytes obtained from fed rats, triacsin C decreases [1-14 C]oleic acid incorporation into TAG by 70% (10). In contrast, triacsin C decreases the metabolism of [1-14 C]oleic acid to phospholipids by 34% and to ASM by 33%. Therefore, inhibiting ACSL1, ACSL3, and ACSL4 decreases fatty acid incorporation into TAG more than into phospholipids or into pathways of fatty acid oxidation. Because hepatocytes express little ACSL6 (4), ACSL5 could account for the t...

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“…Acyl-CoA synthetase activity was measured in the presence of 175 mM Tris, pH 7.4, 8 mM MgCl 2 , 5 mM dithiothreitol, 10 mM ATP, 250 M CoA, and 50 (22). Only initial rates were measured.…”

Section: Cell Homogenate Preparations For Acsl Activity and Protein Amentioning

confidence: 99%

Rat Long Chain Acyl-CoA Synthetase 5 Increases Fatty Acid Uptake and Partitioning to Cellular Triacylglycerol in McArdle-RH7777 Cells

Mashek

McKenzie

Horn

et al. 2006

Journal of Biological Chemistry

110

105

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show abstract

“…The second assay method for acyl-CoA synthetase was based on the property of long-chain acyl-CoA to be acid precipitable (1,31). The Millipore filter assay described by Polokoff and Bell (26) reaction was terminated, the free fatty acids were extracted, and the radioactivity was determined as described below for the assay of the acyl-CoA thioesterase activity.…”

Section: Chemicalsmentioning

confidence: 99%

Synthesis of Long-Chain Acyl-CoA in Chloroplast Envelope Membranes

Joyard¹,

Stumpf²

1981

Plant Physiol.

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“…[3H]palmitate and 5 mm ATP as previously described (24). Glycerol-P acyltransferase activity was assayed using 75 AM palmitoyl CoA and 300 MM [3H]glycerol 3-P (25).…”

Section: Introductionmentioning

confidence: 99%