Fate of linoleic, arachidonic, and docosa-7,10,13,16-tetraenoic acids in rat testicles

A comparative study was made on the fate of linoleic, arachidonic, and docosa-7,10,13,16-tetraenoic acids in various subcellular fractions of liver and testis from rats of different ages. It was demonstrated that testicular microsomes can desaturate and elongate linoleic and arachidonic acids in a manner similar to liver microsomes, and that testicular mitochondria can convert docosa-7,10,13,16-tetraenoic acid to arachidonic acid. Testicular or liver microsomes actively desaturate linoleic acid to γ-linolenic acid and eicosa-8,11,14-trienoic acid to arachidonic acid. However, it was impossible to measure in vitro any direct conversion of adrenic acid (22:4 [n – 6]) to docosapentaenoic acid (22: 5 [n – 6]) by either liver or testicular microsomes. Docosa-7,10,13,16-tetraenoic acid is incorporated preferentially into the triglyceride fraction of total testis, mitochondria, and microsomes, while linoleic and arachidonic acids are incorporated more into phospholipids. The capacity of testicular microsomes, but not of liver microsomes, to synthesize polyunsaturated fatty acids declines with age. It is proposed that the synthesis of acids of the linoleic family proceeds in two stages, a rapid one in which arachidonic acid is made and a second, slower, one in which C22 and C24 acids are synthesized. In addition, there appears to be a cycle between microsomes and mitochondria that acts to conserve essential polyunsaturated C20 and C22 fatty acids by means of synthesis and partial degradation, respectively. This cycle would restrict the loss of essential fatty acids and might be of importance for the supply of arachidonic acid in testis under specific requirements and especially in older animals.Facultad de Ciencias Médica

Dietary and hormonal effects upon activity of "soluble" protein and particulate fraction of fatty acid desaturation system of rat liver microsomes

Rat liver microsomes were extracted with a buffered 0.15 M KCl and 0.25 M sucrose solution and fractionated by centrifugation into a particulate component and a supernatant containing a protein factor necessary for fatty acid desaturation. The delta 6 fatty acid desaturation activity of the extracted microsomes was reduced significantly, and the readdition of the supernatant restored the enzymatic activity to the original value of the whole microsomes. A protein diet or a fat-free diet increased the delta 6 desaturation activity of the whole microsomes. The activating effect was evoked upon the particulate components of the enzymatic desaturation system and not upon the protein factor present in the supernatant. Fasting, refeeding, and refeeding plus glucagon and theophylline treatments of rats also modified the delta 6 desaturation activity of whole liver microsomes. The effect also was evoked on the delta 6 desaturation system tightly bound to the microsomal membrane but not on the protein factor of the supernatant. Accordingly, the protein factor of the supernatant is considered to be different from the cyanide sensitive factor and the desaturase.Facultad de Ciencias Médica

Effect of ethanol administration on fatty acid desaturation

The effect of ethanol on the fatty acid desaturation by rat liver has been studied using liquid diets of different composition. Acute ethanol administration increased triacylglycerols of total liver lipids, but did not modify significantly the lipidic composition of microsomes. The Δ6 and Δ5 desaturases were inhibited by ethanol whereas the Δ9 desaturase and fatty acid synthetase were apparently modified only by diet composition. NADH-cytochrome (cyt.) c reductase was partially inhibited, whereas NADH-cyt. b5 reductase remained practically unaltered and NADPH-cyt. c reductase activity was enhanced. Decreased electrons supplied by the microsomal cyt. b5 electron transport chain would not be the reason for the inhibition of Δ6 and Δ5 desaturases by ethanol.Facultad de Ciencias Médica

The activating effect of dietary protein on linoleic acid desaturation

The desaturation of14C-1-linoleic acid to γ-linolenic acid and their incorporation into the microsomal lipids of rats fed on a balanced diet and a protein diet were measured in vitro. It was shown that a protein diet does not change significantly the distribution of the radioactivity among the different lipidic fractions compared to the animals fed on a balanced diet. However the microsomal desaturation of linoleic acid to γ-linolenic acid increased in the rats maintained on a protein diet. Besides, the amount and composition of the free fatty acids present in the microsomes of the animals fed on both diets were similar enough to discard the hypothesis that they may modify the desaturation of linoleic acid produced by the diet. The enzymic activity of the linoleyl desaturase of liver microsomes of animals fed on a protein diet, measured in substrate saturating conditions, is greater than in animals with balanced diet. Consequently the results support the hypothesis that a protein diet increases specifically the desaturating activity of the microsomes.Facultad de Ciencias Medica