| pubmed-article:8226908 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8226908 | lifeskim:mentions | umls-concept:C0008356 | lld:lifeskim |
| pubmed-article:8226908 | lifeskim:mentions | umls-concept:C0034785 | lld:lifeskim |
| pubmed-article:8226908 | lifeskim:mentions | umls-concept:C0887847 | lld:lifeskim |
| pubmed-article:8226908 | lifeskim:mentions | umls-concept:C0205217 | lld:lifeskim |
| pubmed-article:8226908 | lifeskim:mentions | umls-concept:C0598435 | lld:lifeskim |
| pubmed-article:8226908 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:8226908 | pubmed:issue | 32 | lld:pubmed |
| pubmed-article:8226908 | pubmed:dateCreated | 1993-12-13 | lld:pubmed |
| pubmed-article:8226908 | pubmed:abstractText | The alpha subunit of the heterotrimeric Gs protein that couples the beta-adrenergic receptor to adenylyl cyclase undergoes post-translational palmitoylation. We examined the dynamics of this modification of alpha s by metabolic labeling of COS and S49 lymphoma cells under different conditions. The endogenous alpha s proteins were immunoprecipitated with a peptide-specific antibody, separated by SDS-polyacrylamide gel electrophoresis, and analyzed by fluorography and densitometry. A pulse-chase study of COS cells incubated with [3H]palmitate or [35S]methionine showed that for alpha s the palmitate turnover (t1/2 approximately 50 min) was significantly faster than the protein degradation. Treatment of cells with 10 microM isoproterenol, a beta-adrenergic receptor agonist, in the presence of [3H]palmitate led to a rapid 4-10-fold increase in the palmitoylation of alpha s. This increase in palmitoylation was concentration-dependent (EC50 approximately 0.9 microM) and blocked by the antagonist propranolol. The mutant alpha s proteins in the unc and H21a S49 cell lines did not show an increase in [3H]palmitate incorporation with isoproterenol treatment. Cholera toxin treatment of COS cells increased the [3H]palmitate incorporation into the alpha s subunits. These data indicate that palmitoylation of the alpha s subunit is dynamic and regulated by activation of the alpha s subunit. | lld:pubmed |
| pubmed-article:8226908 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8226908 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8226908 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:8226908 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8226908 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:8226908 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:8226908 | pubmed:author | pubmed-author:SpiegelA MAM | lld:pubmed |
| pubmed-article:8226908 | pubmed:author | pubmed-author:JonesT LTL | lld:pubmed |
| pubmed-article:8226908 | pubmed:author | pubmed-author:DegtyarevM... | lld:pubmed |
| pubmed-article:8226908 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8226908 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:8226908 | pubmed:volume | 268 | lld:pubmed |
| pubmed-article:8226908 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8226908 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8226908 | pubmed:pagination | 23769-72 | lld:pubmed |
| pubmed-article:8226908 | pubmed:dateRevised | 2003-11-14 | lld:pubmed |
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| pubmed-article:8226908 | pubmed:year | 1993 | lld:pubmed |
| pubmed-article:8226908 | pubmed:articleTitle | Increased palmitoylation of the Gs protein alpha subunit after activation by the beta-adrenergic receptor or cholera toxin. | lld:pubmed |
| pubmed-article:8226908 | pubmed:affiliation | Molecular Pathophysiology Branch, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892. | lld:pubmed |
| pubmed-article:8226908 | pubmed:publicationType | Journal Article | lld:pubmed |
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