Adenylate cyclase mediates olfactory transduction for a wide variety of odorants.
Author(s) -
Graeme Lowe,
Tadashi Nakamura,
Geoffrey H. Gold
Publication year - 1989
Publication title -
proceedings of the national academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.86.14.5641
Subject(s) - cyclase , adenylate kinase , forskolin , odor , olfactory epithelium , transduction (biophysics) , stimulation , biology , second messenger system , signal transduction , olfaction , biochemistry , endocrinology , microbiology and biotechnology , chemistry , olfactory system , medicine , neuroscience , enzyme
An odor-stimulated adenylate cyclase [ATP pyrophosphate-lyase (cyclizing), EC 4.6.1.1] is thought to mediate olfactory transduction in vertebrates. However, it is not known whether the adenylate cyclase serves this function for all odorants or for only certain classes of odorants. To investigate this question, we have compared the abilities of 35 odorants to stimulate the adenylate cyclase and to elicit an electrophysiological response. We report a strong positive correlation between the magnitude of adenylate cyclase stimulation and the summated electrical response of the olfactory epithelium (electro-olfactogram) evoked by individual odorants. We also show that the adenylate cyclase stimulator forskolin equally attenuates the electro-olfactogram response for all odorants tested. These data provide evidence that the adenylate cyclase mediates transduction for a wide variety of odorants.
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