title: Endocrine control of TAG lipase in the fat body of the migratory locust, Locusta migratoria.
abstract: Aspects of the role and activation of the enzyme triacylglycerol lipase (TAG lipase) in the fat body of the migratory locust Locusta migratoria were investigated. TAG lipase is under the hormonal control of the three endogenous adipokinetic peptides of the migratory locust, Locmi-AKH-I, Locmi-AKH-II and Locmi-AKH-III. Injection of low doses (5-10 pmol) of each peptide causes an increase in lipase activity. The activation of lipase is time dependent: an elevated activity was recorded 15 min after injection of 10 pmol Locmi-AKH-I and maximum activation was reached after 45-60 min. The activation of TAG lipase is also dose-dependent. Doses of 2 pmol of each Locmi-AKH had no effect, whereas 5 pmol caused a significant activation. Maximum activation is reached with a dose of 10 pmol. Analogues of the second messengers cAMP (cpt-cAMP) and IP(3) (F-IP(3)) both activate the enzyme glycogen phosphorylase whereas only cpt-cAMP, but not F-IP(3), activates TAG lipase; cpt-cAMP elevates the lipid levels in the haemolymph. Activation of lipase is specific to the three endogenous AKH peptides: 5 pmol of the endogenous peptide Locmi-HrTH and 10 pmol of corazonin failed to activate lipase. High doses of octopamine did not activate lipase nor did they elevate the lipid concentration in the haemolymph. TAG lipase is stimulated by flight activity but activation is slower than that of glycogen phosphorylase: after 30 min of flight or after 5 min of flight plus 1h of subsequent rest, activity of TAG lipase is increased, but not immediately after 5 min of flight. In contrast, glycogen phosphorylase is activated significantly after 5 min of flight. These activation patterns of the two enzymes mirror-image the concentration of their substrates in the haemolymph: there is a significant decrease in the concentration of carbohydrates after 5 min of flight, whereas no change of the concentration of lipids can be measured after such short time of flight activity; however, a subsequent rest period of 1h is sufficient to increase the lipid concentration.
authors.affiliation: Zoology Department, University of Cape Town, Rondebosch 7701, South Africa. lauerswa@botzoo.uct.ac.za <lauerswa@botzoo.uct.ac.za>
authors.forename: Lutz
authors.initials: L
authors.lastname: Auerswald
authors.forename: Gerd
authors.initials: G
authors.lastname: Gäde
mesh_terms: D000316:Adrenergic alpha-Agonists / Q000494:pharmacology; D000818:Animals; D004789:Enzyme Activation / Q000187:drug effects; D005216:Fat Body / Q000201:enzymology*; D005426:Flight, Animal; D006458:Hemolymph / Q000201:enzymology; D007301:Insect Hormones / Q000494:pharmacology / Q000502:physiology*; D019476:Insect Proteins / Q000378:metabolism* / Q000502:physiology; D008049:Lipase / Q000097:blood / Q000378:metabolism* / Q000502:physiology; D008055:Lipids / Q000097:blood; D048188:Locusta migratoria / Q000201:enzymology*; D009655:Octopamine / Q000494:pharmacology; D009842:Oligopeptides / Q000494:pharmacology / Q000502:physiology*; D011761:Pyrrolidonecarboxylic Acid / Q000031:analogs & derivatives* / Q000494:pharmacology
chemical_list: D000316:Adrenergic alpha-Agonists; D007301:Insect Hormones; D019476:Insect Proteins; D008055:Lipids; D009842:Oligopeptides; C044833:adipokinetic hormone; D009655:Octopamine; D008049:Lipase; D011761:Pyrrolidonecarboxylic Acid