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J. Biol. Chem., Vol. 269, Issue 1, 9-12, 01, 1994
JD Reagan
Insect diuretic hormones and their receptors regulate fluid and ion
secretion and thus are attractive targets for the design of novel insect
control agents. A complementary DNA clone encoding a
corticotropin-releasing factor-related diuretic hormone receptor from the
tobacco hornworm Manduca sexta was isolated by expression cloning in COS-7
cells. The receptor consists of 395 amino acids and contains seven putative
transmembrane domains. The expressed receptor binds M. sexta diuretic
hormone, as well as several related insect diuretic peptides with high
affinity. Furthermore, each of these peptides stimulate adenylate cyclase
in COS-7 cells transfected with the receptor. The M. sexta diuretic hormone
receptor is homologous to the receptors for calcitonin, secretin,
vasoactive intestinal peptide, parathyroid hormone, glucagon-like peptide
1, growth hormone-releasing hormone, pituitary adenylate cyclase-activating
polypeptide, and glucagon. The M. sexta diuretic hormone receptor is the
first nonmammalian member of this family to be identified.
Expression cloning of an insect diuretic hormone receptor. A member of the calcitonin/secretin receptor family
Sandoz Agro, Inc., Research Division, Palo Alto, California 94304.
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