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Mode of action of neuropeptides from the adipokinetic hormone family
Authors:Gäde Gerd  Auerswald Lutz
Affiliation:Department of Zoology, University of Cape Town, ZA-7701, Rondebosch, South Africa. ggade@botzoo.uct.ac.za
Abstract:Neuropeptides of the adipokinetic hormone (AKH) family regulate inter alia mobilisation of various substrates from stores in the fat body of insects during episodes of flight. How is this achieved? In insects which exclusively oxidise carbohydrates for flight (cockroaches), or which oxidise carbohydrates in conjunction with lipids (locusts) or proline (a number of beetles), the endogenous AKHs bind to a G(q)-protein-coupled receptor, activate a phospholipase C and the resulting inositol trisphosphate releases Ca(2+) from internal stores. In addition, influx of extracellular Ca(2+) is increased and, via a kinase cascade, glycogen phosphorylase is activated, glucose-1-phosphate produced, and transformed to trehalose, which is released into the haemolymph. In locusts, additionally, adenylate cyclase is activated and cyclic AMP is synthesised. In insects which use lipids for sustained flight (locust, tobacco hornworm moth) or proline for flight (certain beetles), adenylate cyclase is activated after the AKHs bind to their respective G(s)-protein-coupled receptor. The resulting cyclic AMP, together with the messengers intra- and extracellular Ca(2+), activate a triacylglycerol lipase, which results in the production of 1,2 diacylglycerols (in locusts, moths) or (hypothetically) free fatty acids (fruit beetle).
Keywords:Adipokinetic neuropeptides   Insects   Signal transduction   Receptors   G-proteins   Phospholipase C   Inositol phosphate   Diacylglycerol   Calcium   Cyclic AMP   Glycogen phosphorylase   Triacylglycerol lipase
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