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Two splicing variants of a novel family of octopamine receptors with different signaling properties.

Authors
  • Wu, Shun-Fan
  • Xu, Gang
  • Qi, Yi-Xiang
  • Xia, Ren-Ying
  • Huang, Jia
  • Ye, Gong-Yin
Type
Published Article
Journal
Journal of Neurochemistry
Publisher
Wiley
Publication Date
Apr 01, 2014
Volume
129
Issue
1
Pages
37–47
Identifiers
DOI: 10.1111/jnc.12526
PMID: 24279508
Source
Medline
Keywords
License
Unknown

Abstract

The octopamine and tyramine, as the invertebrate counterparts of the vertebrate adrenergic transmitters, control and modulate many physiological and behavioral processes. Both molecules mediate their effects by binding to specific receptors belonging to the superfamily of G-protein-coupled receptors. So far, four families of octopamine and tyramine receptors have been reported. Here, we described the functional characterization of one putative octopamine/tyramine receptor gene from the rice stem borer, Chilo suppressalis. By a mechanism of alternative splicing, this receptor gene (CsOA3) encodes two molecularly distinct transcripts, CsOA3S and CsOA3L. CsOA3L differs from CsOA3S on account of the presence of an additional 30 amino acids within the third intracellular loop. When heterologously expressed, both receptors cause increases of intracellular Ca(2+) concentration. The short form, CsOA3S, was activated by both octopamine and tyramine, resulting in decreased intracellular cAMP levels ([cAMP]i ) in a dose-dependent manner, whereas dopamine and serotonin are not effective. However, CsOA3L did not show any impact on [cAMP]i . Studies with series of agonists and antagonists confirmed that CsOA3 has a different pharmacological profile from that of other octopamine receptor families. The CsOA3 is, to our knowledge, a novel family of insect octopamine receptors.

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