A single cDNA encodes all three Aedes leucokinins, which stimulate both fluid secretion by the malpighian tubules and hindgut contractions
Journal of Biological Chemistry. 1997-04-01; 272(16): 10402-10407
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1. J Biol Chem. 1997 Apr 18;272(16):10402-7.
A single cDNA encodes all three Aedes leucokinins, which stimulate both fluid
secretion by the malpighian tubules and hindgut contractions.
Veenstra JA(1), Pattillo JM, Petzel DH.
(1)Department of Entomology and Center for Insect Science, The University of
Arizona, Tucson, Arizona 85721, USA.
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 10(-9) M and increase the frequency of hindgut contractions at
concentrations above 10(-8) 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.
PMID: 9099680 [Indexed for MEDLINE]