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Volume 272, Number 16, Issue of April 18, 1997 pp. 10402-10407
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

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A Single cDNA Encodes All Three Aedes Leucokinins, Which Stimulate Both Fluid Secretion by the Malpighian Tubules and Hindgut Contractions

(Received for publication, October 21, 1996, and in revised form, February 3, 1997)

Jan A. Veenstra , John M. Pattillo ^¶ and David H. Petzel ^**

From the  Department of Entomology and Center for Insect Science, The University of Arizona, Tucson, Arizona 85721, the ^¶ Department of Entomology, The University of Georgia, Athens, Georgia 30602, and the ^** Department of Biomedical Sciences, Creighton University, Omaha, Nebraska 68178

A cDNA encoding preproleucokinin was isolated from a cDNA library of the mosquito Aedes aegypti. The deduced amino acid sequence of Aedes preproleucokinin contains a putative signal peptide of 18 amino acid residues and a 210-amino acid residue proleucokinin. Within the proleucokinin are encoded one copy each of the Aedes leucokinins 1, 2, and 3 isolated previously from this species (Veenstra, J. A. (1994) Biochem. Biophys. Res. Commun. 202, 715-719). All three Aedes leucokinins depolarize the transepithelial voltage of the malpighian tubule in concentrations of less than 10⁹ M and increase the frequency of hindgut contractions at concentrations above 10⁸ M. At higher concentrations the Aedes leucokinins 1 and 3 but not Aedes leucokinin 2 are also able to increase the rate of fluid secretion by the malpighian tubules. The differences of the three Aedes leucokinins in their potencies to induce fluid secretion or depolarizations in the malpighian tubules suggest that there may be more than one type of leucokinin receptor in this tissue.

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