| pubmed-article:11085942 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11085942 | lifeskim:mentions | umls-concept:C0007634 | lld:lifeskim |
| pubmed-article:11085942 | lifeskim:mentions | umls-concept:C0007452 | lld:lifeskim |
| pubmed-article:11085942 | lifeskim:mentions | umls-concept:C0001655 | lld:lifeskim |
| pubmed-article:11085942 | lifeskim:mentions | umls-concept:C0031715 | lld:lifeskim |
| pubmed-article:11085942 | lifeskim:mentions | umls-concept:C0010531 | lld:lifeskim |
| pubmed-article:11085942 | lifeskim:mentions | umls-concept:C0085536 | lld:lifeskim |
| pubmed-article:11085942 | lifeskim:mentions | umls-concept:C1335280 | lld:lifeskim |
| pubmed-article:11085942 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:11085942 | pubmed:dateCreated | 2001-1-2 | lld:pubmed |
| pubmed-article:11085942 | pubmed:abstractText | During activation of adrenocortical cells by adrenocorticotrophic hormone (ACTH), tyrosine dephosphorylation of paxillin is stimulated and this correlates with protrusion of filopodial structures and a decreased number of focal adhesions. These effects are inhibited by Na(3)VO(4), a phosphotyrosine phosphatase inhibitor [Vilgrain, Chinn, Gaillard, Chambaz and Feige (1998) Biochem. J. 332, 533-540]. However, the tyrosine phosphatases involved in these processes remain to be identified. In this study, we provide evidence that the Src homology domain (SH)2-containing phosphotyrosine phosphatase (SHP)2, but not SHP1, is expressed in adrenocortical cells and is phosphorylated upon ACTH challenge. ACTH (10(-8) M) treatment of (32)P-labelled adrenocortical cells resulted in an increase in phosphorylated SHP2. By probing SHP2-containing immunoprecipitates with an antibody to phosphoserine we found that SHP2 was phosphorylated on serine in ACTH-treated cells in a dose- and time-dependent manner. Furthermore, using an in vitro kinase assay, we showed that SHP2 was a target for cAMP-dependent protein kinase (PKA). Serine was identified as the only target amino acid phosphorylated in SHP2. Phosphorylation of SHP2 by PKA resulted in a dramatic stimulation of phosphatase activity measured either with insulin receptor substrate-1 or with the synthetic peptide [(32)P]poly(Glu/Tyr) as substrate. In an in-gel assay of SHP2-containing immunoprecipitates, phosphorylated in vitro by PKA or isolated from adrenocortical cells treated with 10 nM ACTH, a pronounced activation of SHP2 activity was shown. These observations clearly support the idea that a PKA-mediated signal transduction pathway contributes to SHP2 regulation in adrenocortical cells and point to SHP2 as a possible mediator of the effects of ACTH. | lld:pubmed |
| pubmed-article:11085942 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11085942 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11085942 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11085942 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11085942 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11085942 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11085942 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11085942 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11085942 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11085942 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11085942 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11085942 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11085942 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11085942 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11085942 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11085942 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11085942 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11085942 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11085942 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11085942 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11085942 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11085942 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11085942 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11085942 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11085942 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11085942 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11085942 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11085942 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11085942 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11085942 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11085942 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11085942 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11085942 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11085942 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11085942 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11085942 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11085942 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11085942 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11085942 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11085942 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11085942 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11085942 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11085942 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11085942 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11085942 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11085942 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11085942 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11085942 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11085942 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11085942 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11085942 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11085942 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:11085942 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:11085942 | pubmed:author | pubmed-author:ChambazE MEM | lld:pubmed |
| pubmed-article:11085942 | pubmed:author | pubmed-author:van... | lld:pubmed |
| pubmed-article:11085942 | pubmed:author | pubmed-author:VilgrainII | lld:pubmed |
| pubmed-article:11085942 | pubmed:author | pubmed-author:RocchiSS | lld:pubmed |
| pubmed-article:11085942 | pubmed:author | pubmed-author:GaillardII | lld:pubmed |
| pubmed-article:11085942 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11085942 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:11085942 | pubmed:volume | 352 Pt 2 | lld:pubmed |
| pubmed-article:11085942 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11085942 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11085942 | pubmed:pagination | 483-90 | lld:pubmed |
| pubmed-article:11085942 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:11085942 | pubmed:meshHeading | pubmed-meshheading:11085942... | lld:pubmed |
| pubmed-article:11085942 | pubmed:meshHeading | pubmed-meshheading:11085942... | lld:pubmed |
| pubmed-article:11085942 | pubmed:meshHeading | pubmed-meshheading:11085942... | lld:pubmed |
| pubmed-article:11085942 | pubmed:meshHeading | pubmed-meshheading:11085942... | lld:pubmed |
| pubmed-article:11085942 | pubmed:meshHeading | pubmed-meshheading:11085942... | lld:pubmed |
| pubmed-article:11085942 | pubmed:meshHeading | pubmed-meshheading:11085942... | lld:pubmed |
| pubmed-article:11085942 | pubmed:meshHeading | pubmed-meshheading:11085942... | lld:pubmed |
| pubmed-article:11085942 | pubmed:meshHeading | pubmed-meshheading:11085942... | lld:pubmed |
| pubmed-article:11085942 | pubmed:meshHeading | pubmed-meshheading:11085942... | lld:pubmed |
| pubmed-article:11085942 | pubmed:meshHeading | pubmed-meshheading:11085942... | lld:pubmed |
| pubmed-article:11085942 | pubmed:meshHeading | pubmed-meshheading:11085942... | lld:pubmed |
| pubmed-article:11085942 | pubmed:meshHeading | pubmed-meshheading:11085942... | lld:pubmed |
| pubmed-article:11085942 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:11085942 | pubmed:articleTitle | Adrenocorticotrophic hormone stimulates phosphotyrosine phosphatase SHP2 in bovine adrenocortical cells: phosphorylation and activation by cAMP-dependent protein kinase. | lld:pubmed |
| pubmed-article:11085942 | pubmed:affiliation | Unité INSERM 145, Faculté de Médecine, Avenue de Valombrose, 06107 Nice cedex 2, France. | lld:pubmed |
| pubmed-article:11085942 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11085942 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:11085942 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:11085942 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:11085942 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:11085942 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:11085942 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:11085942 | lld:pubmed |
