A beta-adrenergic receptor kinase-like enzyme is involved in olfactory signal termination.

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1993-02-15

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Abstract

We have previously shown that second-messenger-dependent kinases (cAMP-dependent kinase, protein kinase C) in the olfactory system are essential in terminating second-messenger signaling in response to odorants. We now document that subtype 2 of the beta-adrenergic receptor kinase (beta ARK) is also involved in this process. By using subtype-specific antibodies to beta ARK-1 and beta ARK-2, we show that beta ARK-2 is preferentially expressed in the olfactory epithelium in contrast to findings in most other tissues. Heparin, an inhibitor of beta ARK, as well as anti-beta ARK-2 antibodies, (i) completely prevents the rapid decline of second-messenger signals (desensitization) that follows odorant stimulation and (ii) strongly inhibits odorant-induced phosphorylation of olfactory ciliary proteins. In contrast, beta ARK-1 antibodies are without effect. Inhibitors of protein kinase A and protein kinase C also block odorant-induced desensitization and phosphorylation. These data suggest that a sequential interplay of second-messenger-dependent and receptor-specific kinases is functionally involved in olfactory desensitization.

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Animals, Antibodies, Cerebral Cortex, Chemoreceptor Cells, Cilia, Cyclic AMP-Dependent Protein Kinases, Epithelium, Heparin, Immune Sera, Kinetics, Odorants, Olfactory Pathways, Organ Specificity, Phosphorylation, Protein Kinase Inhibitors, Protein Kinases, Rats, Rats, Sprague-Dawley, Receptors, Adrenergic, beta, Signal Transduction, Smell, Time Factors, beta-Adrenergic Receptor Kinases

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