| pubmed-article:8622888 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8622888 | lifeskim:mentions | umls-concept:C1512505 | lld:lifeskim |
| pubmed-article:8622888 | lifeskim:mentions | umls-concept:C0597718 | lld:lifeskim |
| pubmed-article:8622888 | lifeskim:mentions | umls-concept:C0086982 | lld:lifeskim |
| pubmed-article:8622888 | lifeskim:mentions | umls-concept:C0205263 | lld:lifeskim |
| pubmed-article:8622888 | pubmed:issue | 8 | lld:pubmed |
| pubmed-article:8622888 | pubmed:dateCreated | 1996-6-18 | lld:pubmed |
| pubmed-article:8622888 | pubmed:abstractText | Heregulins (HRGs) induce tyrosine phosphorylation of several members of the erb-B family of receptors. Although originally isolated as the ligands for p185c-erb-2, recent evidence suggests that other receptors of the erbB family, including p180erbB-3 and p180erbB-4, are their true cognate receptors. Stimulation of MDA MB-453 cells with HRG beta 2 resulted in the tyrosine phosphorylation of p185c-erbB-2 and p180erbB-4 in a time- and dose-dependent fashion. This event was accompanied by the formation of multimeric complexes between the activated receptors and SH2-containing proteins. Ligand caused p120-rasGTPase activating protein (GAP), SHC and the p85 subunit of phosphatidylinositol-3'-kinase (PI3K) to be associated with both p185c-erbB-2 and p180erbB-4. In addition, tyrosine phosphorylation of p85-PI3K and SHC, but not of GAP or of its associated p62 and p190 proteins, was also detected. HRG also induced the association of GRB2 with tyrosine phosphorylated p185c-erbB-2, p180erbB-4 and SHC. Activation of mitogen-activated protein kinase (MAPK) ( > 30-fold over untreated controls) was observed upon receptor(s) activation, as it was the induction of the immediate early gene c-fos ( > 200-fold). These observations suggest that p21ras activation plays a role in the HRG pathway. Furthermore, comparative analysis of the binding of p85-PI3K to 185c-erbB-2 and p180erbB-4, revealed a preferential association with activated p180erbB-4. These findings might suggest a model of HRG action in which the relative expression of the various erb-B family members and the partitioning of signal transduction molecules between each type of receptor might determine the nature of the signal elicited by the ligand and the biological response attained. | lld:pubmed |
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| pubmed-article:8622888 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:8622888 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:8622888 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8622888 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:8622888 | pubmed:issn | 0950-9232 | lld:pubmed |
| pubmed-article:8622888 | pubmed:author | pubmed-author:LisHH | lld:pubmed |
| pubmed-article:8622888 | pubmed:author | pubmed-author:ChoCC | lld:pubmed |
| pubmed-article:8622888 | pubmed:author | pubmed-author:RosenNN | lld:pubmed |
| pubmed-article:8622888 | pubmed:author | pubmed-author:LuGG | lld:pubmed |
| pubmed-article:8622888 | pubmed:author | pubmed-author:LupuRR | lld:pubmed |
| pubmed-article:8622888 | pubmed:author | pubmed-author:ServeHH | lld:pubmed |
| pubmed-article:8622888 | pubmed:author | pubmed-author:Sepp-Lorenzin... | lld:pubmed |
| pubmed-article:8622888 | pubmed:author | pubmed-author:EberhardII | lld:pubmed |
| pubmed-article:8622888 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8622888 | pubmed:day | 18 | lld:pubmed |
| pubmed-article:8622888 | pubmed:volume | 12 | lld:pubmed |
| pubmed-article:8622888 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8622888 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8622888 | pubmed:pagination | 1679-87 | lld:pubmed |
| pubmed-article:8622888 | pubmed:dateRevised | 2011-11-2 | lld:pubmed |
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| pubmed-article:8622888 | pubmed:year | 1996 | lld:pubmed |
| pubmed-article:8622888 | pubmed:articleTitle | Signal transduction pathways induced by heregulin in MDA-MB-453 breast cancer cells. | lld:pubmed |
| pubmed-article:8622888 | pubmed:affiliation | Department of Medicine, Memorial Sloan-Kettering Cancer Center, New York, NY 10021, USA. | lld:pubmed |
| pubmed-article:8622888 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8622888 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:8622888 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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