pubmed-article:2540203 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:2540203 | lifeskim:mentions | umls-concept:C0682538 | lld:lifeskim |
pubmed-article:2540203 | lifeskim:mentions | umls-concept:C0006104 | lld:lifeskim |
pubmed-article:2540203 | lifeskim:mentions | umls-concept:C0205147 | lld:lifeskim |
pubmed-article:2540203 | lifeskim:mentions | umls-concept:C0205145 | lld:lifeskim |
pubmed-article:2540203 | lifeskim:mentions | umls-concept:C0031715 | lld:lifeskim |
pubmed-article:2540203 | lifeskim:mentions | umls-concept:C0001455 | lld:lifeskim |
pubmed-article:2540203 | lifeskim:mentions | umls-concept:C0031689 | lld:lifeskim |
pubmed-article:2540203 | lifeskim:mentions | umls-concept:C0056694 | lld:lifeskim |
pubmed-article:2540203 | lifeskim:mentions | umls-concept:C0002518 | lld:lifeskim |
pubmed-article:2540203 | lifeskim:mentions | umls-concept:C1533691 | lld:lifeskim |
pubmed-article:2540203 | lifeskim:mentions | umls-concept:C2603343 | lld:lifeskim |
pubmed-article:2540203 | lifeskim:mentions | umls-concept:C0439596 | lld:lifeskim |
pubmed-article:2540203 | pubmed:issue | 13 | lld:pubmed |
pubmed-article:2540203 | pubmed:dateCreated | 1989-6-2 | lld:pubmed |
pubmed-article:2540203 | pubmed:abstractText | ARPP-21 (cyclic AMP-regulated phosphoprotein, Mr = 21,000) is a cytosolic neuronal phosphoprotein that is highly enriched in regions of mammalian brain that receive dopaminergic innervation, in particular the striatum. The state of phosphorylation of ARPP-21 in brain slices prepared from rat striatum was shown to be regulated by 8-bromo-cyclic AMP. Phosphorylation occurred exclusively on seryl residues contained within a single tryptic phosphopeptide as analyzed by two-dimensional thin layer electrophoresis/chromatography. The tryptic phosphopeptide derived from ARPP-21 phosphorylated in intact cells comigrated with the tryptic phosphopeptide derived from purified ARPP-21 phosphorylated by the catalytic subunit of cyclic AMP-dependent protein kinase in vitro. Purified cyclic AMP-dependent protein kinase catalyzed the incorporation of 1.1 mol of [32P]phosphate/mol of ARPP-21 exclusively on seryl residues. The amino acid sequence surrounding the site in purified ARPP-21 phosphorylated by cyclic AMP-dependent protein kinase in vitro was determined by analyzing two overlapping chymotryptic peptides isolated from [32P]phospho-ARPP-21 by reverse phase high performance liquid chromatography. A combination of gas phase and solid phase amino acid sequencing yielded a phosphorylation site sequence of -Glu-Arg-Arg-Lys-Ser(P)-Lys-Ser-Gly-Ala-Gly-. Initial rate studies of the phosphorylation of purified ARPP-21 by the catalytic subunit of cyclic AMP-dependent protein kinase yielded an apparent Km of 0.78 microM and a kcat of 2.2 s-1. A synthetic peptide based on the phosphorylation site of ARPP-21 was phosphorylated on the corresponding seryl residue with an apparent Km of 40 microM and a kcat of 4.0 s-1. These results are compatible with a physiological role for the phosphorylation of ARPP-21 by cyclic AMP-dependent protein kinase in vivo, regulated by first messengers acting via cyclic AMP, e.g. dopamine and vasoactive intestinal peptide. | lld:pubmed |
pubmed-article:2540203 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2540203 | pubmed:language | eng | lld:pubmed |
pubmed-article:2540203 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2540203 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:2540203 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:2540203 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2540203 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:2540203 | pubmed:month | May | lld:pubmed |
pubmed-article:2540203 | pubmed:issn | 0021-9258 | lld:pubmed |
pubmed-article:2540203 | pubmed:author | pubmed-author:GreengardPP | lld:pubmed |
pubmed-article:2540203 | pubmed:author | pubmed-author:WilliamsK RKR | lld:pubmed |
pubmed-article:2540203 | pubmed:author | pubmed-author:HemmingsH... | lld:pubmed |
pubmed-article:2540203 | pubmed:author | pubmed-author:GiraultJ AJA | lld:pubmed |
pubmed-article:2540203 | pubmed:author | pubmed-author:LoPrestiM BMB | lld:pubmed |
pubmed-article:2540203 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:2540203 | pubmed:day | 5 | lld:pubmed |
pubmed-article:2540203 | pubmed:volume | 264 | lld:pubmed |
pubmed-article:2540203 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:2540203 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:2540203 | pubmed:pagination | 7726-33 | lld:pubmed |
pubmed-article:2540203 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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pubmed-article:2540203 | pubmed:meshHeading | pubmed-meshheading:2540203-... | lld:pubmed |
pubmed-article:2540203 | pubmed:year | 1989 | lld:pubmed |
pubmed-article:2540203 | pubmed:articleTitle | ARPP-21, a cyclic AMP-regulated phosphoprotein (Mr = 21,000) enriched in dopamine-innervated brain regions. Amino acid sequence of the site phosphorylated by cyclic AMP in intact cells and kinetic studies of its phosphorylation in vitro. | lld:pubmed |
pubmed-article:2540203 | pubmed:affiliation | Laboratory of Molecular and Cellular Neuroscience, Rockefeller University, New York, New York 10021. | lld:pubmed |
pubmed-article:2540203 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:2540203 | pubmed:publicationType | In Vitro | lld:pubmed |
pubmed-article:2540203 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
entrez-gene:363153 | entrezgene:pubmed | pubmed-article:2540203 | lld:entrezgene |
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