Literature DB >> 1356829

Inhibition of hormone-sensitive lipase by intermediary lipid metabolites.

C A Jepson1, S J Yeaman.   

Abstract

Hormone-sensitive lipase (HSL) is inhibited in a non-competitive manner by oleoyl CoA, oleic acid and 2-monopalmitoylglycerol, 50% inhibition being observed at concentrations of approx. 0.1 microM, 0.5 microM and 500 microM, respectively. HSL is a key enzyme in lipid metabolism, mobilising triacylglycerol and cholesterol ester stores in several tissues. Feedback inhibition of HSL by oleoyl CoA and oleic acid may therefore prevent accumulation of free fatty acids and cholesterol in the cell, whereas 2-monoacylglycerol may act as a feedback inhibitor if the capacity of monoacylglycerol lipase is exceeded.

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Year:  1992        PMID： 1356829     DOI： 10.1016/0014-5793(92)81328-j

Source DB:  PubMed          Journal:  FEBS Lett        ISSN： 0014-5793            Impact factor:   4.124


  21 in total

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5.  Metabolic characteristics of a human hepatoma cell line stably transfected with hormone-sensitive lipase.

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Review 6.  Chemical modulation of glycerolipid signaling and metabolic pathways.

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8.  Hydrogen peroxide-induced translocation of glycolipid-anchored (c)AMP-hydrolases to lipid droplets mediates inhibition of lipolysis in rat adipocytes.

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9.  Mice deficient in phosphofructokinase-M have greatly decreased fat stores.

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Review 10.  Hormone-sensitive lipase--new roles for an old enzyme.

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