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Lipid metabolism in Trichuris globulosa (Nematoda)
Published online by Cambridge University Press: 05 June 2009
Abstract
Adult males and females of Trichuris globulosa, an intestinal nematode parasite of goats, were studied for their lipid composition, capability of incorporation of (Na)-1-14C-acetate into different lipid classes and the activity of certain key enzymes of lipid metabolism. The parasite possesses a large variety of lipids including certain complex lipids. These are phosphatidylcholine (PC), diphosphatidylglycerol (cardiolipin), lysophosphatidylcholine (LPC), lysophosphatidylethanolamine (LPE), phosphatidylserine (PS), phosphatidylinositol (PI), plasmalogens (choline+ethanolamine), mono-, di- and triacylglycerols, free and esterified cholesterol, non-esterified fatty acids (NEFA), gangliosides, cerebrosides (glycosyl ceramide) and sulphuric acid esters of cerebrosides (sulphatides). The females contain more lipids than males, particularly the acylglycerols and phospholipids, possibly to meet the energy requirement and structural entities for the daily production of large numbers of eggs. Incorporation studies of labelled substrate, sodium-1-14C acetate demonstrate that the adult female has extremely active mechanisms for biosynthesizing these lipids. Most of the labels are found in PC, PE, SM, acylglycerols, NEFA, gangliosides, cerebrosides and sulphatides. Cholesterol, although a minor component of the parasitic lipids, incorporates large amount of label and also undergoes fast turnover. Kinetic analysis of the incorporation by measuring the rate constant (k) and half life (t½) reveals that gangliosides are the fastest biosynthesizing and turning over lipids, although they constitute only 0·1% of the total lipids. The presence of important enzymes of lipid biosynthesis, glucose-6-phosphate dehydrogenase, malate dehydrogenase and hydroxymethyl glutaryl-CoA reductase and an enzyme of lipid ester hydrolysis, triacylglycerol lipase, is also established in T. globulosa. Michaelis-Menten kinetic characteristics of the parasitic enzymes (Km, Vmax, v and the first order rate constant, k) are comparable with those of rat liver homogenates.
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- Copyright © Cambridge University Press 1989
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