Isolation and primary structure of neuropeptides from the mosquito,Aedes aegypti,immunoreactive to FMRFamide antiserum |
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| Institution: | 1. Institute of Physical and Chemical Research (RIKEN), Hirosawa 2-1, Wako-Shi, Saitama, 350-01 Japan;2. Department of Entomology, University of Georgia, Athens, GA 30602, USA;3. Department of Zoology, University of Georgia, Athens, GA 30602 USA;4. Department of Physiology, Duke University Medical Center, Durham, NC 27710, U.S.A.;1. Diabetes, Endocrinology, and Obesity Branch, National Institute of Diabetes and Digestive and Kidney Diseases, NIH, Bethesda, MD 20892, USA;1. School of Informatics, University of Edinburgh, Edinburgh, EH8 9AB, UK;2. HHMI-Janelia Research Campus, Ashburn, VA 20147, USA;3. School of Natural Sciences, Bangor University, Bangor LL57 2UW, Bangor, UK;4. Biological Sciences, Florida Atlantic University, Boca Raton, FL 33431, USA;5. Virtual Fly Brain, University of Cambridge, Cambridge, CB2 3EJ, UK;6. Department of Physiology & Biophysics, University of Washington, Seattle, WA 98195, USA;7. iDN, Johannes Gutenberg University Mainz, 55128 Mainz, Germany;8. Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10027, USA;9. School of Biological Sciences, The University of Queensland, Brisbane, QLD 4072, Australia;10. Division of Biology and Biological Engineering, The California Institute of Technology, Pasadena, CA 91125, USA;11. Centre for Developmental Neurobiology, King’s College London, London WC2R 2LS, UK;12. Department of Biology, Villanova University, Villanova, PA 19085, USA;13. Institute of Neurobiology, University of Puerto Rico Medical Sciences Campus, San Juan, Puerto Rico;14. Molecular, Cellular and Developmental Biology, University of California, Santa Barbara, Santa Barbara, CA 93106, USA;15. Friday Harbor Laboratories, University of Washington, Friday Harbor, WA 98250, USA;16. RCAST, University of Tokyo, Tokyo 153-8904, Japan;1. Department of Molecular Biophysics & Biochemistry, Yale University, New Haven, Connecticut;2. Quantitative Biology Institute, Yale University, New Haven, Connecticut;1. Department of Chemistry, University of Wisconsin-Madison, Madison, WI, USA;2. School of Pharmacy, University of Wisconsin-Madison, Madison, WI, USA |
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| Abstract: | Two novel neuropeptides, Aea-HP-I and II, have been isolated from a head extract of the mosquito, Aedes aegypti; they were detected by a FMRFamide radioimmunoassay. The peptides were purified by gel filtration, ion exchange chromatography, and reversed-phase high performance liquid chromatography. Amino acid composition and sequence analysis, combined with enzymatic digestion, established the primary structure of Aea-HP-I as pGlu-Arg-Pro-Hyp-Ser-Leu-Lys-Thr-Arg-Phe-NH2 and Aea-HP-II as Thr-Arg-Phe-NH2. Aea-HP-I was synthesized, and chromatographic properties of the synthetic peptide were the same as those of the native peptide, thus confirming the structural analysis. The peptide has three unusual residues: an amino-terminal pGlu, a Hyp in the fourth position, and a carboxyl-terminal amide. The Pro-Hyp sequence occurs in toxin peptides from the venoms of cone snails and wasps and in bradykinin analogues. Although the functions of Aea-HP-I and II have not been determined, the peptides have the same RFa sequence at the carboxyl-terminal as Lem-SK-I and II (leucosulfakinins) and Lem-MS (leucomyosuppressin) in cockroaches and FMRFamide-related peptides in molluscs. |
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