title: Activation of triacylglycerol lipase in the fat body of a beetle by adipokinetic hormone.
abstract: The activation of triacylglycerol lipase and the stimulation of proline synthesis in the fat body of the fruit beetle Pachnoda sinuata by the endogenous octapeptide hormone Melme-CC (pQLNYSPDWa), which belongs to the family of insect adipokinetic hormones, were studied, and the correlation of both events investigated. At rest, the activity of triacylglycerol lipase in the fat body of the beetle was higher than in the fat body of the American cockroach, Periplaneta americana, but lower than in the migratory locust, Locusta migratoria. Triacylglycerol lipase of the beetle is activated by: (a) injection of synthetic Melme-CC and (b) the stimulus of flight. Activation of lipase by Melme-CC is time-dependent. Injection of cpt-cAMP activates triacylglycerol lipase in the fat body and causes an increase in the concentration of proline in the haemolymph at the expense of alanine. In contrast, injection of F-inositol-1,4,5-phosphate does not affect the activation state of lipase, nor the levels of amino acids in the haemolymph. High doses of octopamine do not activate lipase. Furthermore, activity of fat body lipase and proline concentration in the haemolymph both follow a circadian rhythm: both parameters are high in the morning, whereas they are low in the evening. When transfer of Melme-CC, released from the corpora cardiaca, to the thorax/abdomen is prevented by neck-ligation, the activity of lipase, as well as the circulating proline levels are low. Regression analysis revealed that activity of triacylglycerol lipase is positively correlated to proline concentration in the haemolymph, whereas there is a negative correlation of the enzyme activity and alanine level in the haemolymph. From these results we conclude that the activation of fat body triacylglycerol lipase by Melme-CC in P. sinuata stimulates proline synthesis. Proline is one of the major substrates to power flight activity in the beetle.
authors.affiliation: Zoology Department, University of Cape Town, Rondebosch 7701, South Africa. lauerswa@botzoo.uct.ac.za
authors.forename: Lutz
authors.initials: L
authors.lastname: Auerswald
authors.forename: Karl J
authors.initials: KJ
authors.lastname: Siegert
authors.forename: Gerd
authors.initials: G
authors.lastname: Gäde
mesh_terms: D000818:Animals; D001517:Coleoptera / Q000502:physiology*; D004789:Enzyme Activation / Q000502:physiology*; D005216:Fat Body / Q000502:physiology*; D007301:Insect Hormones / Q000502:physiology*; D008049:Lipase / Q000378:metabolism*; D008053:Lipid Mobilization / Q000502:physiology; D009842:Oligopeptides / Q000502:physiology*; D011761:Pyrrolidonecarboxylic Acid / Q000031:analogs & derivatives*
chemical_list: D007301:Insect Hormones; D009842:Oligopeptides; C044833:adipokinetic hormone; D008049:Lipase; D011761:Pyrrolidonecarboxylic Acid