pubmed-article:11438667 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:11438667 | lifeskim:mentions | umls-concept:C0062534 | lld:lifeskim |
pubmed-article:11438667 | lifeskim:mentions | umls-concept:C1571580 | lld:lifeskim |
pubmed-article:11438667 | lifeskim:mentions | umls-concept:C0205307 | lld:lifeskim |
pubmed-article:11438667 | lifeskim:mentions | umls-concept:C0033414 | lld:lifeskim |
pubmed-article:11438667 | lifeskim:mentions | umls-concept:C1523347 | lld:lifeskim |
pubmed-article:11438667 | lifeskim:mentions | umls-concept:C1514829 | lld:lifeskim |
pubmed-article:11438667 | lifeskim:mentions | umls-concept:C2587213 | lld:lifeskim |
pubmed-article:11438667 | lifeskim:mentions | umls-concept:C2348042 | lld:lifeskim |
pubmed-article:11438667 | lifeskim:mentions | umls-concept:C2700387 | lld:lifeskim |
pubmed-article:11438667 | pubmed:issue | 15 | lld:pubmed |
pubmed-article:11438667 | pubmed:dateCreated | 2001-7-4 | lld:pubmed |
pubmed-article:11438667 | pubmed:abstractText | Smads serve as intracellular mediators of transforming growth factor beta (TGF-beta) signaling. After phosphorylation by activated type I TGF-beta receptors, Smad proteins translocate to the nucleus, where they serve as transcription factors and increase or decrease expression of TGF-beta target genes. Mice lacking one copy each of Smad2 and Smad3 suffered midgestation lethality due to liver hypoplasia and anemia, suggesting essential dosage requirements of TGF-beta signal components. This is likely due to abnormal adhesive properties of the mutant hepatocytes, which may result from a decrease in the level of the beta1-integrin and abnormal processing and localization of E-cadherin. Culture of mutant livers in vitro revealed the existence of a parallel developmental pathway mediated by hepatocyte growth factor (HGF), which could rescue the mutant phenotype independent of Smad activation. These pathways merge at the beta1-integrin, the level of which was increased by HGF in the cultured mutant livers. HGF treatment reversed the defects in cell proliferation and hepatic architecture in the Smad2(+/-); Smad3(+/-) livers. | lld:pubmed |
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pubmed-article:11438667 | pubmed:language | eng | lld:pubmed |
pubmed-article:11438667 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11438667 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:11438667 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:11438667 | pubmed:month | Aug | lld:pubmed |
pubmed-article:11438667 | pubmed:issn | 0270-7306 | lld:pubmed |
pubmed-article:11438667 | pubmed:author | pubmed-author:WeinsteinMM | lld:pubmed |
pubmed-article:11438667 | pubmed:author | pubmed-author:MAJJ | lld:pubmed |
pubmed-article:11438667 | pubmed:author | pubmed-author:MishraLL | lld:pubmed |
pubmed-article:11438667 | pubmed:author | pubmed-author:LieII | lld:pubmed |
pubmed-article:11438667 | pubmed:author | pubmed-author:TangYY | lld:pubmed |
pubmed-article:11438667 | pubmed:author | pubmed-author:BrodieS GSG | lld:pubmed |
pubmed-article:11438667 | pubmed:author | pubmed-author:DengC XCX | lld:pubmed |
pubmed-article:11438667 | pubmed:author | pubmed-author:MongaS PSP | lld:pubmed |
pubmed-article:11438667 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:11438667 | pubmed:volume | 21 | lld:pubmed |
pubmed-article:11438667 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:11438667 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:11438667 | pubmed:pagination | 5122-31 | lld:pubmed |
pubmed-article:11438667 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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