Abstract
Rat kidney cortex microsomal preparations were unable to catalyze Δ9, Δ6, and Δ5 desaturation of stearoylcoenzyme A (CoA), linoleoyl-CoA and dihomo-γ-linolenoyl-CoA, respectively. The kidney cortex microsomal fraction, however, did catalyze the malonyl-CoA dependent fatty acyl-CoA elongation. The biochemical properties of palmitoyl-CoA elongation were studied as a function of protein concentration, time, reduced nicotinamide adenine dinucleotide phosphate (NADPH), malonyl-CoA and substrate concentrations; of the substrates investigated, Δ6.9.12–18∶3 was the most active. Unlike what was observed in the hepatic system, a high-carbohydrate, fat-free diet did not induced kidney fatty acid chain elongation. All intermediate kidney cortex microsomal reactions,i.e., β-ketoacyl-CoA reductase, β-hydroxyacyl-CoA dehydrase andtrans-2-enoyl-CoA reductase activities, were significantly higher (greater than one order of magnitude) than the condensing enzyme activity, suggesting that the rate-limiting step in total elongation is the initial condensation reaction. Contrary to other reports, the results suggest that the kidney cannot synthesize arachidonic acid needed for eicosanoid production.
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Abbreviations
- ATP:
-
adenosine triphosphate
- BHT:
-
butylated hydroxytoluene
- BSA:
-
bevine serum albumin
- CoA:
-
coenzyme A
- FACES:
-
fatty acid chain elongation system
- NADH:
-
reduced nicotinamide adenine dinucleotide
- NADPH:
-
reduced nicotinamide adenine dinucleotide phosphate
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Suneja, S.K., Nagi, M.N., Cook, L. et al. Do rat kidney cortex microsomes possess the enzymatic machinery to desaturate and chain elongate fatty acyl-CoA derivatives?. Lipids 26, 359–363 (1991). https://doi.org/10.1007/BF02537199
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DOI: https://doi.org/10.1007/BF02537199