| pubmed-article:2894032 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2894032 | lifeskim:mentions | umls-concept:C0007452 | lld:lifeskim |
| pubmed-article:2894032 | lifeskim:mentions | umls-concept:C0376604 | lld:lifeskim |
| pubmed-article:2894032 | lifeskim:mentions | umls-concept:C0521428 | lld:lifeskim |
| pubmed-article:2894032 | lifeskim:mentions | umls-concept:C0031715 | lld:lifeskim |
| pubmed-article:2894032 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:2894032 | lifeskim:mentions | umls-concept:C0599668 | lld:lifeskim |
| pubmed-article:2894032 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:2894032 | pubmed:dateCreated | 1988-4-1 | lld:pubmed |
| pubmed-article:2894032 | pubmed:abstractText | Chromaffin cells were isolated from bovine adrenal medullae and maintained in primary culture. After prelabeling with 32PO4, exposure of the chromaffin cells to acetylcholine increased the phosphorylation of a Mr approximately equal to 100,000 protein and a Mr approximately equal to 60,000 protein (tyrosine hydroxylase), visualized after separation of total cellular proteins in naDodSO4/polyacrylamide gels. Immunoprecipitation with antibodies to three known phosphoproteins ("100-kDa," "87-kDa," and protein III) revealed an acetylcholine-dependent phosphorylation of these proteins. These three proteins were also shown to be present in bovine adrenal chromaffin cells by immunolabeling techniques. "100-kDa" is a Mr approximately equal to 100,000 protein selectively phosphorylated by calcium/calmodulin-dependent protein kinase III, "87-kDa" is a Mr approximately equal to 87,000 protein selectively phosphorylated by protein kinase C, and protein III is a phosphoprotein doublet of Mr approximately equal to 74,000 (IIIa) and Mr approximately equal to 55,000 (IIIb) phosphorylated by cAMP-dependent protein kinase and calcium/calmodulin-dependent protein kinase I. Furthermore, 100-kDa was shown to be identical to the Mr approximately equal to 100,000 protein whose phosphorylation was increased by acetylcholine treatment. The acetylcholine-dependent increase in phosphorylation of tyrosine hydroxylase, 100-kDa, 87-kDa, and protein III required extracellular calcium and was mimicked by nicotine, veratridine, elevated K+, and calcium ionophore A23187, but not by muscarine. In addition, forskolin increased the phosphorylation of tyrosine hydroxylase, 100-kDa, and protein III, but not that of 87-kDa. Phorbol 12,13-dibutyrate increased the phosphorylation of tyrosine hydroxylase, 87-kDa, and protein III, but not that of 100-kDa. The data demonstrate that cholinergic activation of chromaffin cells increases the phosphorylation of several proteins and that several protein kinase systems may be involved in these effects. | lld:pubmed |
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| pubmed-article:2894032 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:2894032 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:2894032 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2894032 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:2894032 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:2894032 | pubmed:author | pubmed-author:GreengardPP | lld:pubmed |
| pubmed-article:2894032 | pubmed:author | pubmed-author:HaycockJ WJW | lld:pubmed |
| pubmed-article:2894032 | pubmed:author | pubmed-author:BrowningM DMD | lld:pubmed |
| pubmed-article:2894032 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2894032 | pubmed:volume | 85 | lld:pubmed |
| pubmed-article:2894032 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2894032 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2894032 | pubmed:pagination | 1677-81 | lld:pubmed |
| pubmed-article:2894032 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:2894032 | pubmed:meshHeading | pubmed-meshheading:2894032-... | lld:pubmed |
| pubmed-article:2894032 | pubmed:year | 1988 | lld:pubmed |
| pubmed-article:2894032 | pubmed:articleTitle | Cholinergic regulation of protein phosphorylation in bovine adrenal chromaffin cells. | lld:pubmed |
| pubmed-article:2894032 | pubmed:affiliation | Laboratory of Molecular and Cellular Neuroscience, Rockefeller University, New York, NY 10021-6399. | lld:pubmed |
| pubmed-article:2894032 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2894032 | pubmed:publicationType | In Vitro | lld:pubmed |
| pubmed-article:2894032 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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