Octopamine in invertebrates and vertebrates. A review

David, Jean‐Claude; Coulon, J.F.

doi:10.1016/0301-0082(85)90009-7

Cited by 199 publications

(88 citation statements)

References 222 publications

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“…Interestingly, we observed that HEK293 cells stably expressing Lym oa 1 showed the same current response to octopamine as cells expressing Lym oa 2 (Fig. 7B).…”

Section: Resultsmentioning

confidence: 68%

“…Octopamine is often referred to as the invertebrate counterpart of norepinephrine because of the structural similarity between these neurotransmitters (they differ only in the presence of a single catecholic hydroxyl group) as well as their functional similarity (both serve an important role in stress adaptation) (2). Consequently, the adrenergic and octopaminergic receptors share pharmacological as well as structural properties (3,4).…”

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confidence: 99%

“…In these species, the interactions of octopamine with its receptors have been described mainly at the electrophysiological level (7,8,(11)(12)(13)(14)(15). In general, application of octopamine induces a hyperpolarization of susceptible snail neurons, a process that is thought to be mediated by an increase in cAMP (2,11,12), leading to an increased potassium (12)(13)(14) or calcium (15) conductance. In addition, a pharmacological characterization of octopamine receptors has been described for Lymnaea.…”

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confidence: 99%

“…In addition, a pharmacological characterization of octopamine receptors has been described for Lymnaea. 2 We have recently cloned and characterized a cDNA encoding an octopamine receptor expressed in the brain of Lymnaea stagnalis (16). This receptor (Lym oa 1 ) shows moderate homology to the Drosophila tyramine/octopamine receptor (17,18), to the Locusta tyramine receptor (19) and to the vertebrate ␣-adrenergic receptors.…”

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confidence: 99%

“…1). The total coding region was cloned into pcDNA3 (Invitrogen), yielding a construct designated pcDNA-Lym oa 2 .…”

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confidence: 99%

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Cloning and Expression of a Complementary DNA Encoding a Molluscan Octopamine Receptor That Couples to Chloride Channels in HEK293 Cells

Gerhardt

Lodder

Vincent

et al. 1997

Journal of Biological Chemistry

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A cDNA encoding a G-protein-coupled receptor was cloned from the central nervous system of the pond snail Lymnaea stagnalis. The predicted amino acid sequence of this cDNA most closely resembles the Drosophila tyramine/octopamine receptor, the Locusta tyramine receptor, and an octopamine receptor (Lym oa 1 ) that we recently cloned from Lymnaea. After stable expression of the cDNA in HEK293 cells, we found that [ 3 H]rauwolscine binds with high affinity to the receptor (K D ‫؍‬ 6.2⅐10 ؊9 M). Octopamine appears to be the most potent naturally occurring agonist to displace the [ 3 H]rauwolscine binding (K i ‫؍‬ 3.0⅐10 ؊7 M). Therefore, the receptor is considered to be an octopamine receptor and is consequently designated Lym oa 2 . The novel receptor shares little pharmacological resemblance with Lym oa 1 , indicating that the two receptors represent different octopamine receptor subfamilies. Octopaminergic stimulation of Lym oa 2 does not induce changes in intracellular concentrations of cAMP or inositol phosphates. However, electrophysiological experiments indicate that octopamine is able to activate a voltage-independent Cl ؊ current in HEK293 cells stably expressing Lym oa 2 . Although opening of this chloride channel most probably does not require the activation of either protein kinase A or C, it can be blocked by inhibition of protein phosphorylation.

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“…Interestingly, we observed that HEK293 cells stably expressing Lym oa 1 showed the same current response to octopamine as cells expressing Lym oa 2 (Fig. 7B).…”

Section: Resultsmentioning

confidence: 68%

mentioning

confidence: 99%