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Substituent‐dependent, positive and negative modulation of Bombyx mori adenylate cyclase by synthetic octopamine/tyramine analogues
Author(s) -
Aoyama Masato,
Nakane Toshiya,
Ono Takako,
Khan Md. Anwar Arfien,
Ohta Hiroto,
Ozoe Yoshihisa
Publication year - 2001
Publication title -
archives of insect biochemistry and physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.576
H-Index - 66
eISSN - 1520-6327
pISSN - 0739-4462
DOI - 10.1002/arch.1029
Subject(s) - tyramine , octopamine (neurotransmitter) , adenylate kinase , cyclase , bombyx mori , biology , second messenger system , stimulation , receptor , biogenic amine , biochemistry , medicine , endocrinology , neurotransmitter , gene , serotonin
Octopamine (OCT)/tyramine (TYR) analogues, mainly including p ‐ and β‐substituted phenylethylamines, were prepared as probes for the ligand‐binding site(s) of adenylate cyclase‐coupled OCT or TYR receptors, and were examined for their effects on cAMP production in the head membranes of Bombyx mori larvae. Small structural changes in OCT and TYR proved to lead to three types of OCT/TYR analogues: (1) compounds that increase the cAMP level by themselves and also depress OCT‐stimulated cAMP production, (2) compounds that do not stimulate cAMP production by themselves but inhibit OCT‐stimulated cAMP production, and (3) compounds that are not active in either the stimulation of cAMP production or the inhibition of OCT‐stimulated cAMP production. Tyramine, which belongs to the second group, also inhibited the basal level of cAMP production at high concentrations. The data indicate that two biogenic amine systems that positively and negatively regulate the level of the second messenger cAMP are present in the head part of B. mori larvae. This finding points to the necessity of separately evaluating the positive and negative regulatory effects in order to quantitatively understand the structure‐activity relationships of OCT receptor ligands. Arch. Insect Biochem. Physiol. 47:1–7, 2001. © 2001 Wiley‐Liss, Inc.