| pubmed-article:9814969 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9814969 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
| pubmed-article:9814969 | lifeskim:mentions | umls-concept:C1334291 | lld:lifeskim |
| pubmed-article:9814969 | lifeskim:mentions | umls-concept:C0003018 | lld:lifeskim |
| pubmed-article:9814969 | lifeskim:mentions | umls-concept:C1335280 | lld:lifeskim |
| pubmed-article:9814969 | lifeskim:mentions | umls-concept:C1706044 | lld:lifeskim |
| pubmed-article:9814969 | lifeskim:mentions | umls-concept:C1519726 | lld:lifeskim |
| pubmed-article:9814969 | lifeskim:mentions | umls-concept:C1335283 | lld:lifeskim |
| pubmed-article:9814969 | lifeskim:mentions | umls-concept:C1705637 | lld:lifeskim |
| pubmed-article:9814969 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:9814969 | pubmed:issue | 5 Pt 1 | lld:pubmed |
| pubmed-article:9814969 | pubmed:dateCreated | 1998-12-14 | lld:pubmed |
| pubmed-article:9814969 | pubmed:abstractText | Angiotensin II (ANG II) exerts its effects on vascular smooth muscle cells through G protein-coupled AT1 receptors. ANG II stimulation activates the Janus kinase/signal transducers and activators of transcription (JAK/STAT) pathway by inducing tyrosine phosphorylation, activation, and association of JAK2 with the receptor. Association appears to be required for JAK2 phosphorylation. In the present study, electroporation experiments with neutralizing anti-Src homology phosphatase-1 (SHP-1) and anti-SHP-2 antibodies and time course determinations of SHP-1 and SHP-2 activation and complexation with JAK2 suggest that the tyrosine phosphatases, SHP-1 and SHP-2, have opposite roles in ANG II-induced JAK2 phosphorylation. SHP-1 appears responsible for JAK2 dephosphorylation and termination of the ANG II-induced JAK/STAT cascade. SHP-2 appears to have an essential role in JAK2 phosphorylation and initiation of the ANG II-induced JAK/STAT cascade leading to cell proliferation. The motif in the AT1 receptor that is required for association with JAK2 is also required for association with SHP-2. Furthermore, SHP-2 is required for JAK2-receptor association. SHP-2 may thus play a role as an adaptor protein for JAK2 association with the receptor, thereby facilitating JAK2 phosphorylation and activation. | lld:pubmed |
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| pubmed-article:9814969 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:9814969 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:9814969 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9814969 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:9814969 | pubmed:issn | 0002-9513 | lld:pubmed |
| pubmed-article:9814969 | pubmed:author | pubmed-author:EatonD CDC | lld:pubmed |
| pubmed-article:9814969 | pubmed:author | pubmed-author:VenemaV JVJ | lld:pubmed |
| pubmed-article:9814969 | pubmed:author | pubmed-author:JuHH | lld:pubmed |
| pubmed-article:9814969 | pubmed:author | pubmed-author:VenemaR CRC | lld:pubmed |
| pubmed-article:9814969 | pubmed:author | pubmed-author:MarreroM BMB | lld:pubmed |
| pubmed-article:9814969 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9814969 | pubmed:volume | 275 | lld:pubmed |
| pubmed-article:9814969 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9814969 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9814969 | pubmed:pagination | C1216-23 | lld:pubmed |
| pubmed-article:9814969 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:9814969 | pubmed:year | 1998 | lld:pubmed |
| pubmed-article:9814969 | pubmed:articleTitle | Regulation of angiotensin II-induced JAK2 tyrosine phosphorylation: roles of SHP-1 and SHP-2. | lld:pubmed |
| pubmed-article:9814969 | pubmed:affiliation | Vascular Biology Center, Medical College of Georgia, Augusta 30912, Georgia, USA. | lld:pubmed |
| pubmed-article:9814969 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9814969 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:9814969 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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