Functional and pharmacological characterization of a β-adrenergic-like octopamine receptor from the silkworm Bombyx mori

Chen, Xi; Ohta, Hiroto; Ozoe, Fumiyo; Miyazawa, Keisuke; Huang, Jia; Ozoe, Yoshihisa

doi:10.1016/j.ibmb.2010.04.007

Cited by 43 publications

(63 citation statements)

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“…AB470228) encoding a b -adrenergic-like OAR (BmOAR2) from the nerve tissues of silkworm (Bombyx mori) larvae. 8) We generated a human embryonic kidney (HEK)-293 cell line that stably expressed BmOAR2. Upon activation with OA, BmOAR2 elicited a concentration-dependent increase in intracellular cAMP levels ([cAMP] i ), but not Ca 2+ levels.…”

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confidence: 99%

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Amino acid residues involved in the interaction with the intrinsic agonist (R)-octopamine in the .BETA.-adrenergic-like octopamine receptor from the silkworm Bombyx mori

et al. 2011

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“…The pcDNA3-FLAG vector was constructed to add a FLAG tag (DYKDDDDK) to the N-terminus of BmOAR2 by introducing a Kozak sequence 9) and a FLAG tag sequence into the HindIII/KpnI site of the mammalian expression vector pcDNA3 (Invitrogen). 8) Each pcDNA3-FLAG/mutant_BmOAR2 construct was verified by DNA sequencing.…”

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confidence: 99%

Amino acid residues involved in the interaction with the intrinsic agonist (R)-octopamine in the .BETA.-adrenergic-like octopamine receptor from the silkworm Bombyx mori

et al. 2011

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“…However, current knowledge regarding the octopamine receptor subtype(s) in mediating the effects of octopamine is limited. To date, only OctRs from Drosophila melanogaster (three subtypes) and Bombyx mori (two subtypes but only one have function) have been cloned and characterized (Chen et al, 2010;Maqueira et al, 2005). A partial sequence of putative OctR in the desert locust Schistocerca gregaria (SgOctR) was also cloned (Verlinden et al, 2010b).…”

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confidence: 99%

Characterization of a β-adrenergic-like octopamine receptor from the rice stem borer (Chilo suppressalis)

Yao

Huang

et al. 2012

Journal of Experimental Biology

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SUMMARYOctopamine, the invertebrate counterpart of adrenaline and noradrenaline, plays a key role in regulation of many physiological and behavioral processes in insects. It modulates these functions through binding to specific octopamine receptors, which are typical rhodopsin-like G-protein coupled receptors. A cDNA encoding a seven-transmembrane receptor was cloned from the nerve cord of the rice stem borer, Chilo suppressalis, viz. CsOA2B2, which shares high sequence similarity to CG6989, a Drosophila -adrenergic-like octopamine receptor (DmOct2R). We generated an HEK-293 cell line that stably expresses CsOA2B2 in order to examine the functional and pharmacological properties of this receptor. Activation of CsOA2B2 by octopamine increased the production of cAMP in a dose-dependent manner (EC 50 2.33nmoll Supplementary material available online at

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“…150,151 Furthermore, the author has created a phylogenetic tree based on the comparison of 25 complete nucleotide sequences of insect octopaminergic and tyraminergic receptor genes by using the "Muscle" sequence alignment program. [153][154][155] Based on nucleotide sequence homology in the phylogenetic tree, insect octopaminergic receptor sequences from the moth M. sexta (MsOA), 146 D. melanogaster (OAMB) 137 and splice variants (DmOA1A, and DmOA1B), 143 A. mellifera (AmOA1), 138 P. americana (PaOA1), 142 B. mori (BmOAR1), 145 and locust Schistocerca gregaria (SgOctαR) 26 cluster together in the Octα-R class, whereas S. gregaria (SgOctβR), 26 B. mori (BmOAR2), 152 and D. melanogaster (DmOctβ1-R, DmOctβ2-R, DmOctβ3-R) 144 fall into the Octβ-R class ( Figure 5). Tyraminergic receptor sequences from A. mellifera (Amtyr1), 148 B. mori (BmTAR1), 140 (HvTA), 134 Agrotis ipsilon (Aityr/OCT), 141 Locusta migratoria (Lmtyr1), 139 and the cattle tick Boophilus microplus (BmiTA) 147 fall into the Tyr1-R subclass.…”

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Review of octopamine in insect nervous systems

Farooqui¹

2012

OAIP

145

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Octopamine (OCT) belongs to a group of compounds known as biogenic amines. OCT, a monohydroxylic analog of norepinephrine, is found in both vertebrate and invertebrate nervous systems. OCT is present in relatively high concentrations in the neuronal and nonneuronal tissues of most invertebrate species studied. However, OCT occurs as a trace amine in vertebrates where its physiological significance remains uncertain. OCT acts as a neurotransmitter, neuromodulator, and neurohormone in insect nervous systems where it prominently influences multiple physiological events. In the peripheral nervous system, OCT modulates the activity of flight muscles, peripheral organs, and most sense organs. In the central nervous system, OCT is essential for the regulation of motivation, desensitization of sensory inputs, arousal, initiation, and maintenance of various rhythmic behaviors, hygiene behavior, and complex social behaviors, including establishment of labor, as well as learning and memory. As a neurotransmitter, OCT regulates endocrine gland activity and controls the emission of light in the firefly lantern. As a neurohormone, OCT is released into hemolymph, transported to target tissues, and induces mobilization of lipids and carbohydrates, preparing insects for a period of extended activity or assisting recovery from a period of increased energy demand. OCT modulates hemocytic nodulation in nonimmune larvae and enhances phagocytosis as a neurohormone. OCT exerts its effects by binding to specific receptors belonging to the superfamily of G protein-coupled receptors and shares the structural motif of seven transmembrane domains. Activation of octopaminergic receptor types is coupled with different second messenger pathways depending on the species, tissue source, receptor type, and cell line used for expression of the cloned receptor. OCT-mediated generation of second messengers is associated with changes in cellular response, affecting insect behaviors. This review describes the roles of OCT in insect nervous systems at the behavioral and molecular levels.

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Functional and pharmacological characterization of a β-adrenergic-like octopamine receptor from the silkworm Bombyx mori

Cited by 43 publications

References 47 publications

Amino acid residues involved in the interaction with the intrinsic agonist (R)-octopamine in the .BETA.-adrenergic-like octopamine receptor from the silkworm Bombyx mori

Amino acid residues involved in the interaction with the intrinsic agonist (R)-octopamine in the .BETA.-adrenergic-like octopamine receptor from the silkworm Bombyx mori

Characterization of a β-adrenergic-like octopamine receptor from the rice stem borer (Chilo suppressalis)

Review of octopamine in insect nervous systems

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