Domain-structure analysis of recombinant rat hormone-sensitive lipase

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Domain-structure analysis of recombinant rat hormone-sensitive lipase.

Hormone-sensitive lipase (HSL) plays a key role in lipid metabolism and overall energy homoeostasis, by controlling the release of fatty acids from stored triglycerides in adipose tissue. Lipases and esterases form a protein superfamily with a common structural fold, called the alpha/beta-hydrolase fold, and a catalytic triad of serine, aspartic or glutamic acid and histidine. Previous alignmen...

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Hormone-Sensitive Lipase Knockouts

All treatments for obesity, including dietary restriction of carbohydrates, have a goal of reducing the storage of fat in adipocytes. The chief enzyme responsible for the mobilization of FFA from adipose tissue, i.e., lipolysis, is thought to be hormone-sensitive lipase (HSL). Studies of HSL knockouts have provided important insights into the functional significance of HSL and into adipose meta...

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Positional specificity of hormone-sensitive lipase from rat adipose tissue.

Hormone-sensitive lipase, purified from rat adipose tissue (Fredrikson, G., Strålfors, P., Nilsson, N. O., and Belfrage, P. (1981) J. Biol. Chem. 256, 6311-6320), has been incubated with tri-, di-, and monooleoyl[3H]glycerol, and the acylglycerol reaction products were isolated by thin layer chromatography on silicic acid, impregnated with boric acid. Trioleoylglycerol was hydrolyzed with the i...

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The reciprocal regulation of lipoprotein lipase activity and hormone-sensitive lipase activity in rat adipocytes.

The regulation of lipoprotein lipase activity was studied in rat adipocytes. Incubation of fat cells for 60 mm in buffer without glucose and insulin resulted in a 50% decrease in lipoprotein lipase activity. This decrease was prevented by glucose and insulin. Inhibition of fat cell protein synthesis by cycloheximide abolished the effect of glucose and insulin and caused a rapid decay of lipopro...

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ژورنال

عنوان ژورنال: Biochemical Journal

سال: 1996

ISSN: 0264-6021,1470-8728

DOI: 10.1042/bj3190411