title: Evidence that free fatty acids in trophocytes of Periplaneta americana fat body may be regulated by the activity of phospholipase A2 and cyclooxygenase.
abstract: Previous studies have shown that palmitic, stearic, oleic and linoleic acid levels in trophocytes prepared from the fat body of male Periplaneta americana are increased following treatment of the cells with hypertrehalosemic hormone (HTH). Melittin, an activator of phospholipase A2, mimicked the action of HTH by increasing the free fatty acid content in a concentration-dependent manner. The increase caused by HTH could be eliminated by pretreatment of the trophocytes with 1 mM 4'-bromophenacyl bromide (BPB), an inhibitor of phospholipase A2. BPB also decreases the concentration of free fatty acids in trophocytes not treated with HTH but by a smaller margin. Nordihydroguaiaretic acid (NDGA) and indomethacin, inhibitors of lipoxygenase and cyclooxygenase, respectively, eliminated the increase in free fatty acids evoked by HTH. In the absence of HTH both inhibitors increased the free fatty acid content of the trophocytes, an effect consistent with the known mode of action of these agents. None of the inhibitors tested, all of which blocked HTH activated trehalose synthesis, prevented activation of phosphorylase by HTH. This is taken as evidence that other downstream sites are also important in the regulation of trehalose production by the fat body. It is suggested that the increase in free fatty acids evoked by HTH, or metabolites of those fatty acids, may regulate the synthesis and release of trehalose from the trophocytes because of potential effects on trehalose phosphate synthase, trehalose 6-phosphate phosphatase, and the trehalose transport mechanism in the trophocyte membrane.
authors.affiliation: Department of Zoology, University of Western Ontario, London, Canada.
authors.forename: I
authors.initials: I
authors.lastname: Ali
authors.forename: J E
authors.initials: JE
authors.lastname: Steele
mesh_terms: D000098:Acetophenones / Q000494:pharmacology; D000818:Animals; D016861:Cyclooxygenase Inhibitors / Q000494:pharmacology; D004789:Enzyme Activation; D004791:Enzyme Inhibitors / Q000494:pharmacology; D005216:Fat Body / Q000378:metabolism; D005227:Fatty Acids / Q000378:metabolism*; D007213:Indomethacin / Q000494:pharmacology; D007301:Insect Hormones / Q000494:pharmacology; D019787:Linoleic Acid / Q000378:metabolism; D008297:Male; D009637:Masoprocol / Q000494:pharmacology; D008555:Melitten / Q000494:pharmacology; D009479:Neuropeptides / Q000494:pharmacology; D019301:Oleic Acid / Q000378:metabolism; D019308:Palmitic Acid / Q000378:metabolism; D010526:Periplaneta / Q000378:metabolism*; D010741:Phospholipases A / Q000378:metabolism*; D054467:Phospholipases A2; D011451:Prostaglandin-Endoperoxide Synthases / Q000378:metabolism*; D013229:Stearic Acids / Q000378:metabolism; D014199:Trehalose / Q000378:metabolism
chemical_list: D000098:Acetophenones; D016861:Cyclooxygenase Inhibitors; D004791:Enzyme Inhibitors; D005227:Fatty Acids; D007301:Insect Hormones; D009479:Neuropeptides; D013229:Stearic Acids; D008555:Melitten; D019301:Oleic Acid; D019308:Palmitic Acid; C031183:stearic acid; D009637:Masoprocol; C043192:glutamyl-valyl-asparaginyl-phenylalanyl-seryl-prolyl-asparaginyl-tryptophanamide; C043191:glutamyl-leucyl-threonyl-phenylalanyl-threonyl-prolyl-asparaginyl-tryptophanamide; D019787:Linoleic Acid; D014199:Trehalose; D011451:Prostaglandin-Endoperoxide Synthases; D010741:Phospholipases A; D054467:Phospholipases A2; C006821:4-bromophenacyl bromide; D007213:Indomethacin