[74] Hormone-sensitive lipase from adipose tissue of rat

Fredrikson, Gudrun; Strålfors, Peter; Nilsson, Nils Östen; Belfrage, Per

doi:10.1016/0076-6879(81)71076-0

Cited by 120 publications

(149 citation statements)

References 14 publications

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“…It has been demonstrated previously that HSL has cholesterol ester hydrolase activity [5] and that, in addition to its role in lipolysis [6], HSL is responsi-ble for the cholesterol ester hydrolase activity in steroidogenic tissues [7,8]; furthermore, its cholesterol ester hydrolase activity can be activated by cyclic AMP-dependent protein kinase-mediated phosphorylation [9]. In this report we present direct evidence that HSL is responsible for the neutral cholesterol ester hydrolase activity in macrophages, providing a possible mechanism for hormonal or therapeutic control of intracellular levels of cholesterol esters.…”

Section: Introductionmentioning

confidence: 97%

Hormone‐sensitive lipase is responsible for the neutral cholesterol ester hydrolase activity in macrophages

1989

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Anti-hormone-sensitive lipase (HSL) immunoglobulin selectively immunoprecipitates a single 84 kDa 32P-phosphoprotein from macrophage homogenates previously phosphorylated by cyclic AMP-dependent protein kinase in the presence of [y-32P]ATP-Mg. This immunoglobulin also completely removes the neutral cholesterol ester hydrolase activity from macrophage homogenates. These data demonstrate that HSL is responsible for the neutral cholesterol ester hydrolase activity in macrophages and hence plays a key role in cholesterol metabolism in these cells.Hormone-sensitive lipase; Cholesterol ester hydrolase; Macrophage; Atherosclerosis

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Section: Introductionmentioning

confidence: 97%

Hormone‐sensitive lipase is responsible for the neutral cholesterol ester hydrolase activity in macrophages

1989

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“…A key feature of HSL is its ability to be activated by phosphorylation by cyclic AMPdependent protein kinase [5][6][7]. Consistent ~ith this, Goldberg cell-free extracts of P388D~ macrophages by cyclic AMP-dependent protein kinase, and in intact cells by elevation of intracellular cyclic AMP levels [81.…”

Section: Introductionmentioning

confidence: 99%

Phosphorylation and activation of hormone‐sensitive lipase in isolated macrophages

et al. 1991

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Hormone‐sensitive lipase (HSL) is responsible for the neutral cholesterol ester hydrolase activity in macrophages. Incubation of intact WEHI macrophages or mouse peritoneal macrophages leads to phosphorylation of HSL, which is increased by incubation with either dibutyryl cyclic AMP and 3‐isobutyl‐1‐methylxanthine or okadaic acid. Correspondingly, these agents also activate neutral cholesterol ester hydrolase activity in intact WEHI cells. Regulation of mobilisation of esterified cholesterol in macrophages may be of antiatherogenic value, which this model system now allows us to investigate further.

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“…This regulatory module is found within the C-terminal domain of HSL, which also contains the catalytic triad [50]. Phosphorylation results in increased hydrolytic activity [51], translocation of HSL from the cytosol to the lipid-droplet surface and enhanced TAG breakdown in the cell [49]. HSL can also be regulated by other kinases [49,52], including AMP-activated protein kinase [53].…”

Section: Hydrolysis Of Triacylglycerolmentioning

confidence: 99%

“…In vitro, HSL is 10-20-fold more active against DAG than TAG, and it may be the only, or at least the major, neutral cholesteryl ester (CE) hydrolase in vivo [51,66,67]. Until recently, HSL was believed to be the major regulatory enzyme in TAG hydrolysis.…”

Section: Hydrolysis Of Triacylglycerolmentioning

confidence: 99%

“…In times of energy need, such as fasting and exercise, adipocyte lipolysis is markedly increased by catecholamines that activate Gs-coupled receptors. HSL has broad substrate specificity, with hydrolytic activity against TAG, diacylglycerol [DAG] and monoacylglycerol, as well as cholesteryl and retinyl esters [51]. In vitro, HSL is 10-20-fold more active against DAG than TAG, and it may be the only, or at least the major, neutral cholesteryl ester (CE) hydrolase in vivo [51,66,67].…”

Section: Hydrolysis Of Triacylglycerolmentioning

confidence: 99%

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Triacylglycerol Metabolism In Adipose Tissue

et al. 2007

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Triacylglycerol (TAG) in adipose tissue serves as the major energy storage form in higher eukaryotes. Obesity, resulting from excess white adipose tissue, has increased dramatically in recent years resulting in a serious public health problem. Understanding of adipocyte-specific TAG synthesis and hydrolysis is critical to the development of strategies to treat and prevent obesity and its closely associated diseases, for example, Type 2 diabetes, hypertension and atherosclerosis. In this review, we present an overview of the major enzymes in TAG synthesis and lipolysis, including the recent discovery of a novel adipocyte TAG hydrolase. Keywords1-acylglycerol-3-phosphate acyltransferase; desnutrin/adipose triglyceride lipase; diacylglycerol acyltransferase; glycerol-3-phosphate acyltransferase; hormone-sensitive lipase; lipolysis; phosphatidic acid phosphatase; triacylglycerol White adipose tissue (WAT) is the major energy reserve in higher eukaryotes. The primary purposes of WAT are synthesis and storage of triacylglycerol (TAG) in periods of energy excess, and hydrolysis of TAG to generate fatty acids for use by other organs during periods of energy deprivation [1]. Adipose tissue also secretes adipokines that regulate energy intake and metabolism.The prevalence of obesity resulting from excess WAT has increased dramatically in recent years resulting in a serious public health problem, since obesity is closely associated with a number of disorders including Type 2 diabetes, hypertension and atherosclerosis [2]. While † Author for correspondence, University of California, Department of Nutritional Sciences & Toxicology, Berkeley, CA 94720, USA, adipocyte number has been shown to increase (hyperplasia) in morbid obesity, obesity is primarily attributed to adipocyte hypertrophy that occurs when TAG synthesis (esterification) exceeds TAG breakdown (lipolysis), resulting in elevated TAG storage [1]. Although it has been postulated that large adipocyte size may contribute to insulin resistance, the molecular mechanism is not clear.Paradoxically, the metabolic abnormalities typically found in obesity are also associated with lipodystrophies that are characterized by selective loss of adipose tissue from particular regions of the body [3][4][5][6]. Although the underlying molecular mechanisms are not clear, metabolic complications may result from ectopic storage of TAG in tissues such as the liver and muscle [7][8][9]. A proper capacity for TAG storage in adipocytes is clearly important for normal metabolic regulation. In view of the wide range of health problems associated with improper fat storage and release, it is critical to understand adipocyte-specific regulation of TAG synthesis and hydrolysis. Biosynthesis of triacylglycerolThe synthesis of phosphatidic acid and its subsequent conversion to TAG was described more than 40 years ago by Kennedy and coworkers [10], and is summarized in Figure 1. The initial committal step in this pathway is the formation of lysophosphatidic acid (1-acylglycerol-3-phosphate)...

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[74] Hormone-sensitive lipase from adipose tissue of rat

Cited by 120 publications

References 14 publications

Hormone‐sensitive lipase is responsible for the neutral cholesterol ester hydrolase activity in macrophages

Hormone‐sensitive lipase is responsible for the neutral cholesterol ester hydrolase activity in macrophages

Phosphorylation and activation of hormone‐sensitive lipase in isolated macrophages

Triacylglycerol Metabolism In Adipose Tissue

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