| pubmed-article:7683643 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7683643 | lifeskim:mentions | umls-concept:C0010222 | lld:lifeskim |
| pubmed-article:7683643 | lifeskim:mentions | umls-concept:C0753114 | lld:lifeskim |
| pubmed-article:7683643 | lifeskim:mentions | umls-concept:C0164209 | lld:lifeskim |
| pubmed-article:7683643 | lifeskim:mentions | umls-concept:C1710236 | lld:lifeskim |
| pubmed-article:7683643 | pubmed:issue | 13 | lld:pubmed |
| pubmed-article:7683643 | pubmed:dateCreated | 1993-6-4 | lld:pubmed |
| pubmed-article:7683643 | pubmed:abstractText | The agonist-occupied forms of several G-protein-coupled receptors that modulate the activity of adenylycyclase via Gs (e.g. beta 2-adrenergic) or Gi (e.g. alpha 2-adrenergic and cardiac muscarinic) are phosphorylated by beta-adrenergic receptor kinases (beta ARK 1 and beta ARK 2). beta ARK-catalyzed phosphorylation of these receptors appears to correlate with their agonist-induced desensitization. The possibility that beta ARK isozymes may also be involved in the desensitization of other G-protein-coupled receptors such as those mediating phosphoinositide (PI) hydrolysis was tested by determining the phosphorylation of the substance P receptor (SPR), which is coupled to PI hydrolysis in numerous tissues. Rat SPR was expressed in Sf9 cells, partially purified, and reconstituted in phospholipid vesicles. The reconstituted SPR bound the SPR agonist substance P, 125I-labeled with Bolton-Hunter reagent, with low affinity. However, addition of purified Gq/11 to the reconstituted SPR resulted in the conversion of all the receptors to a high affinity state, suggesting that SPR couples to Gq/11. Phosphorylation of the reconstituted SPR with purified beta ARK 1 or 2 in the absence and presence of substance P (SP) was then studied. In the presence of 100 microM SP, both kinases promoted phosphorylation of the receptor to a stoichiometry of 9 +/- 2 mol of phosphate/mol of receptor. However, no phosphorylation of the receptor could be detected in the absence of agonist. Agonist-induced phosphorylation of the receptor was blocked by coincubation with the SPR antagonist spantide. These results show that beta ARK isozymes may regulate the function of both adenylylcyclase as well as PI-coupled receptors, and suggest a role for beta ARK isozymes in SPR signal transduction. | lld:pubmed |
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| pubmed-article:7683643 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:7683643 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:7683643 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7683643 | pubmed:month | May | lld:pubmed |
| pubmed-article:7683643 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:7683643 | pubmed:author | pubmed-author:LefkowitzR... | lld:pubmed |
| pubmed-article:7683643 | pubmed:author | pubmed-author:CaronM GMG | lld:pubmed |
| pubmed-article:7683643 | pubmed:author | pubmed-author:KimC MCM | lld:pubmed |
| pubmed-article:7683643 | pubmed:author | pubmed-author:BenovicJ LJL | lld:pubmed |
| pubmed-article:7683643 | pubmed:author | pubmed-author:BlandJ EJE | lld:pubmed |
| pubmed-article:7683643 | pubmed:author | pubmed-author:KwatraM MMM | lld:pubmed |
| pubmed-article:7683643 | pubmed:author | pubmed-author:KrauseJ EJE | lld:pubmed |
| pubmed-article:7683643 | pubmed:author | pubmed-author:SchreursJJ | lld:pubmed |
| pubmed-article:7683643 | pubmed:author | pubmed-author:SchwinnD ADA | lld:pubmed |
| pubmed-article:7683643 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7683643 | pubmed:day | 5 | lld:pubmed |
| pubmed-article:7683643 | pubmed:volume | 268 | lld:pubmed |
| pubmed-article:7683643 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7683643 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7683643 | pubmed:pagination | 9161-4 | lld:pubmed |
| pubmed-article:7683643 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:7683643 | pubmed:year | 1993 | lld:pubmed |
| pubmed-article:7683643 | pubmed:articleTitle | The substance P receptor, which couples to Gq/11, is a substrate of beta-adrenergic receptor kinase 1 and 2. | lld:pubmed |
| pubmed-article:7683643 | pubmed:affiliation | Department of Anesthesiology, Duke University Medical Center, Durham, North Carolina 27710. | lld:pubmed |
| pubmed-article:7683643 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7683643 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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