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The isolated digestive juice of Aeshna cyanea larvae hydrolysed trioleoylglycerol preferentially at the terminal 1 and 3 positions, yielding 1, 2-dioleoylglycerol as first intermediate. Hydrolysis continued to 1- and 2-monooleoylglycerol as second intermediate. Separate incubation of monooleoylglycerol revealed that hydrolysis could proceed to completion. Inadequate inhibition of mono[1-14C]oleoylglycerol hydrolysis in the cold and in the presence of the lipase inhibitor tetrahydrolipstatin provided no information on whether monooleoylglycerol was absorbed in addition to free oleic acid. On the other hand, the analogue oleylglyceryl ethers were resistant towards hydrolysis by the digestive juice. Both monoethers and both diethers were esterified with [1-14C]palmitic acid by the homogenate of the midgut wall, whereas esterification in vivo occurred only with the monoethers. These were recovered from the haemolymph after saponification of the joint diacylglycerol and acyl-0-alkylglycerol fraction, indicating that the monoethers had been absorbed and transported into the haemolymph. Ingestion of mono-1-0-[3H]octadecylglycerol showed that the ether was absorbed unchanged by the midgut epithelium, where the major part of the alkyl moiety was oxidized to free fatty acid and incorporated into phospholipids, acylglycerols and acyl-0-alkylglycerols. It is concluded from the absorption of the analogous monoalkylglyceryl ethers that monoacylglyceryl esters are also absorbed by Aeshna larvae.
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Am J Physiol. 1996 Oct;271(4 Pt 1):C1194-202.
Diacylglycerols derived from membrane phospholipids are metabolized by lipases in A10 smooth muscle cells.
Migas I, Severson DL.
Smooth Muscle Research Group, Faculty of Medicine, University of Calgary, Alberta, Canada.
The metabolic fate of endogenous diacylglycerol (DAG) in cultured A10 smooth muscle cells was determined. Preincubation of A10 cells with [3H]myristic acid or [3H]arachidonic acid resulted in preferential labeling of phosphatidylcholine (PC) or phosphatidylinositol (PI), respectively. Addition of PC-specific phospholipase C (PC-PLC) to [3H]myristate-labeled A10 cells resulted in a 10-fold increase in radiolabeled DAG, which was converted to monoacylglycerol (MG) and fatty acid (FA). DAG degradation and MG formation was inhibited by tetrahydrolipstatin, a DAG lipase inhibitor. PC-derived DAG was not converted to phosphatidic acid; in addition, PC resynthesis or triacylglycerol synthesis was not observed. Addition of PI-specific PLC (PI-PLC) to [3H]arachidonate-labeled A10 cells resulted in a modest increase in radiolabeled DAG that was also hydrolyzed to MG and FA. Therefore, the principal metabolic fate of endogenous DAG generated from membrane phospholipids by treatment of A10 cells with PC-PLC and PI-PLC was hydrolysis by a DAG lipase pathway.
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FEBS Lett. 1996 Oct 28;396(1):90-4.
Evidence for a multi-domain structure for hormone-sensitive lipase.
Smith GM, Garton AJ, Aitken A, Yeaman SJ.
Department of Biochemistry and Genetics, Medical School, University of Newcastle, Newcastle upon Tyne, UK.
Hormone-sensitive lipase (HSL) is a multi-functional enzyme involved in several aspects of lipid metabolism. Limited tryptic digestion of HSL led to selective loss of activity against lipid substrates but not against the water-soluble substrate, p-nitrophenyl butyrate. Following labelling of the active site of HSL with either [3H]di-isopropylfluorophosphate or [14C]orlistat, tryptic digestion of HSL generated a stable radiolabelled domain of molecular mass approx. 17.6 kDa, consistent with this representing a catalytic domain of HSL capable of hydrolysing water-soluble but not lipid substrates. Following phosphorylation of HSL by cyclic AMP-dependent protein kinase, limited tryptic digestion produced a stable phosphorylated domain of molecular mass 11.5 kDa. Based on these experimental data a model for a domain structure of HSL is proposed.
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