Zinc deficiency impairs the metabolism of polyunsaturates, but the degree to which its effects are independent of food intake are still in question. Identical amounts of a semiliquid control diet (26.4 mg zinc/kg) or moderately zinc deficient diet (3.2 mg zinc/kg) were tube fed to rats for 11 days during the second half of pregnancy to evaluate the specific effects of zinc deficiency on maternal utilization and fetal accumulation of polyunsaturates. The whole body fatty acid balance method was used to determine net accumulation of polyunsaturates and their whole-body disappearance. Incorporation of 14C from [1-14C]linoleate into maternal and fetal lipid classes was also studied on days 20-21. At term, zinc-deficient rats had significantly higher whole-body disappearance of linoleate and alpha-linolenate and lower accumulation of n-6 and n-3 long-chain polyunsaturates. Zinc-deficient rats had higher 14C activity in free cholesterol, saturates, and monounsaturates in several maternal organs but not in the fetuses. We conclude that during pregnancy, moderate zinc deficiency not affecting food intake or weight gain still alters whole-body metabolism of linoleate and alpha-linolenate towards increased beta-oxidation and also increases the utilization of carbon from linoleate for de novo lipid synthesis.
Dietary zinc deficiency impairs desaturation and elongation of linoleic acid, but nothing is so far known about its effects on net whole-body utilization of linoleic or alpha-linolenic acids. By measuring intake, whole-body accumulation, and excretion of linoleic and alpha-linolenic acids, together with accumulation of their long-chain products, we hypothesized that a quantitative estimate could be obtained of their whole-body disappearance (apparent oxidation). This was evaluated in pregnant and non-pregnant rats given a low-zinc diet (3.4 vs. 34 mg zinc/kg diet in zinc-adequate controls). In the nonpregnant controls, low zinc intake did not significantly affect food intake or weight gain but did reduce whole-body accumulation of desaturated and (or) elongated products of linoleic and alpha-linolenic acids. In pregnant rats, low zinc intake reduced food intake and weight gain and doubled whole-body disappearance of linoleic and alpha-linolenic acids relative to that in the zinc-adequate controls. In contrast to the maternal fatty acid changes, low zinc intake had no significant effect on linoleic acid accumulation in the fetuses. We conclude that low zinc intake during pregnancy prevents the normal accumulation of long-chain fatty acids and differentially depletes maternal whole-body stores of linoleic and alpha-linolenic acids.
CTP-phosphocholine cytidylyltransferase (CT) is a key regulatory enzyme in the biosynthesis of phosphatidylcholine (PC) in many cells. Enzyme-membrane interactions appear to play an important role in CT activation. A putative membrane-binding domain appears to be located between residues 236 and 293 from the N-terminus. To map the membrane-binding domain more precisely, glutathione S-transferase fusion proteins were prepared that contained deletions of various domains in this putative lipid-binding region. The fusion proteins were assessed for their binding of [3H]PC/oleic acid vesicles. Fusion proteins encompassing residues 267-277 bound to PC/oleic acid vesicles, whereas fragments lacking this region exhibited no specific binding to the lipid vesicles. The membrane-binding characteristics of the CT fusion proteins were also examined using intact lung microsomes. Only fragments encompassing residues 267-277 competed with full-length 125I-labelled CT, expressed in recombinant Sf9 insect cells, for microsomal membrane binding. To investigate the role of this region in PC biosynthesis, A549 and L2 cells were transfected with cDNA for CT mutants under the control of a glucocorticoid-inducible long terminal repeat (LTR) promoter. Induction of CT mutants containing residues 267-277 in transfectants resulted in reduced PC synthesis. The decrease in PC synthesis was accompanied by a shift in endogenous CT activity from the particulate to the soluble fraction. Expression of CT mutants lacking this region in A549 and L2 cells did not affect PC formation and subcellular distribution of CT activity. These results suggest that the CT region located between residues 267 and 277 from the N-terminus is required for the interaction of CT with membranes.
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