| pubmed-article:6146982 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:6146982 | lifeskim:mentions | umls-concept:C0085262 | lld:lifeskim |
| pubmed-article:6146982 | lifeskim:mentions | umls-concept:C0001443 | lld:lifeskim |
| pubmed-article:6146982 | lifeskim:mentions | umls-concept:C0041491 | lld:lifeskim |
| pubmed-article:6146982 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:6146982 | pubmed:issue | 15 | lld:pubmed |
| pubmed-article:6146982 | pubmed:dateCreated | 1984-9-19 | lld:pubmed |
| pubmed-article:6146982 | pubmed:abstractText | (R)-N6-Phenylisopropyladenosine (PIA) stimulates dopa production 3- to 5-fold in PC12 cells, with a half-maximal effective concentration (EC50) of 50 nM. This increase can be explained by a stable activation of tyrosine hydroxylase [TyrOHase; L-tyrosine, tetrahydropteridine:oxygen oxidoreductase (3-hydroxylating), EC 1.14.16.2] when it is phosphorylated by a cAMP-dependent protein kinase. The activation of TyrOHase is mediated by the adenosine-dependent activation of adenylate cyclase (EC50 = 600 nM). PIA (10 microM) is as effective as cholera toxin or dibutyryl cAMP in activating TyrOHase in wild-type cells. Adenosine kinase-deficient mutants of PC12 were found to be resistant to PIA-dependent activation of TyrOHase (EC50 = 100-1000 nM). This phenomenon was explored in detail in one adenosine kinase-deficient mutant and was shown to occur because the mutant was resistant to the adenosine-dependent activation of adenylate cyclase. In this mutant, TyrOHase was activated 14-fold by cholera toxin, suggesting that activated TyrOHase is about 14 times as active as unactivated TyrOHase. These studies with kinase-deficient PC12 cells provide genetic evidence that adenosine-dependent activation of TyrOHase is mediated by acute increases in cAMP. When the adenosine receptor found on PC12 cells is expressed in vivo, it might function as either a presynaptic (i.e., localized on the nerve terminal) or a postsynaptic (i.e., localized on the cell body or dendrite) receptor that regulates rates of transmitter synthesis in response to cell activity. | lld:pubmed |
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| pubmed-article:6146982 | pubmed:language | eng | lld:pubmed |
| pubmed-article:6146982 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6146982 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:6146982 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:6146982 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:6146982 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:6146982 | pubmed:author | pubmed-author:WagnerJ AJA | lld:pubmed |
| pubmed-article:6146982 | pubmed:author | pubmed-author:ErnyRR | lld:pubmed |
| pubmed-article:6146982 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:6146982 | pubmed:volume | 81 | lld:pubmed |
| pubmed-article:6146982 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:6146982 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:6146982 | pubmed:pagination | 4974-8 | lld:pubmed |
| pubmed-article:6146982 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:6146982 | pubmed:year | 1984 | lld:pubmed |
| pubmed-article:6146982 | pubmed:articleTitle | Adenosine-dependent activation of tyrosine hydroxylase is defective in adenosine kinase-deficient PC12 cells. | lld:pubmed |
| pubmed-article:6146982 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:6146982 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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