Cloning of biogenic amine receptors from moths (Bombyx mori and Heliothis virescens)

Insect Biochem Mol Biol. 1996 Sep-Oct;26(8-9):817-27. doi: 10.1016/s0965-1748(96)00031-8.

Abstract

Based on the similarity of genes which code for guanine-nucleotide binding protein- (G-protein-) coupled receptors, cDNA clones encoding new members of the receptor family have been isolated from Bombyx mori and Heliothis virescens. The deduced protein structures exhibit highest similarity to tyramine/octopamine and serotonin receptors of Drosophila. One of the receptor clones (K50Hel) was permanently expressed in the mammalian cell line LLC-PK1. In stimulation experiments its responded to octopamine leading to an inhibition of adenylate cyclase activity in a dose-dependent manner. Pharmacological studies revealed a higher affinity for mianserin than for yohimbine suggesting, that the K50Hel clone encoded a neuronal type 3 octopamine receptor. As revealed by in situ hybridization, this receptor type is expressed in the central nervous system and antennae of moth.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Bombyx / genetics*
  • Bombyx / metabolism
  • Cloning, Molecular
  • DNA, Complementary
  • Gene Expression
  • LLC-PK1 Cells
  • Molecular Sequence Data
  • Moths / genetics*
  • Moths / metabolism
  • Octopamine / metabolism*
  • Receptors, Biogenic Amine / genetics*
  • Sequence Homology, Amino Acid
  • Swine

Substances

  • DNA, Complementary
  • Receptors, Biogenic Amine
  • norsynephrine receptor
  • tyramine receptor
  • Octopamine

Associated data

  • GENBANK/X95604
  • GENBANK/X95605
  • GENBANK/X95606
  • GENBANK/X95607