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Termination of second messenger signaling in olfaction.
Author(s) -
Ingrid Boekhoff,
Heinz Breer
Publication year - 1992
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.89.2.471
Subject(s) - second messenger system , phosphorylation , kinase , signal transduction , olfaction , microbiology and biotechnology , chemistry , transduction (biophysics) , biology , biochemistry , neuroscience
By using isolated rat olfactory cilia and a fast kinetics methodology, it has been demonstrated that odorant-induced second messenger signaling in the millisecond time range is terminated via phosphorylation reactions catalyzed by specific protein kinases. The cyclic adenosine nucleotide pathway is turned off by kinase A activity, whereas the inositol trisphosphate cascade is terminated by kinase C. The data support the concept that desensitization of odorant responses involves phosphorylation of key elements in the transduction cascade.

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