A beta-adrenergic receptor kinase-like enzyme is involved in olfactory signal termination.
Data(s) |
15/02/1993
|
---|---|
Formato |
1420 - 1424 |
Identificador |
http://www.ncbi.nlm.nih.gov/pubmed/8381966 Proc Natl Acad Sci U S A, 1993, 90 (4), pp. 1420 - 1424 0027-8424 |
Relação |
Proc Natl Acad Sci U S A 10.1073/pnas.90.4.1420 |
Palavras-Chave | #Animals #Antibodies #Cerebral Cortex #Chemoreceptor Cells #Cilia #Cyclic AMP-Dependent Protein Kinases #Epithelium #Heparin #Immune Sera #Kinetics #Odors #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 |
Tipo |
Journal Article |
Cobertura |
United States |
Resumo |
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. |
Idioma(s) |
ENG |