https://scholars.lib.ntu.edu.tw/handle/123456789/193256
DC 欄位 | 值 | 語言 |
---|---|---|
dc.contributor | 外科 | en |
dc.contributor.author | CHEN, CHIA-HUEI | en |
dc.contributor.author | TUNG, PO-YUAN | en |
dc.contributor.author | HUANG, SHIH-HORNG | en |
dc.contributor.author | WANG, SEU-MEI | en |
dc.creator | 陳佳徽;董伯元;黃實宏;王淑美 | zh-tw |
dc.creator | CHEN, CHIA-HUEI;TUNG, PO-YUAN;HUANG, SHIH-HORNG;WANG, SEU-MEI | en |
dc.date | 2009 | en |
dc.date.accessioned | 2010-06-23T06:03:38Z | - |
dc.date.accessioned | 2018-07-11T10:03:14Z | - |
dc.date.available | 2010-06-23T06:03:38Z | - |
dc.date.available | 2018-07-11T10:03:14Z | - |
dc.date.issued | 2009 | - |
dc.identifier.uri | http://ntur.lib.ntu.edu.tw//handle/246246/185892 | - |
dc.description.abstract | We have previously shown that culturing HepG2 cells in pH 6. 6 culture medium increases the c-Src-dependent tyrosine phosphorylation of beta- catenin and induces disassembly of adherens junctions (AJs). Here, we investigated the upstream mechanism leading to this pH 6.6-induced modification of E- cadherin. In control cells cultured at pH 7.4, E- cadherin staining was linear and continuous at cell-cell contact sites. Culturing cells at pH 6.6 was not cytotoxic, and resulted in weak and discontinuous junctional E-cadherin staining, consistent with the decreased levels of E-cadherin in membrane fractions. pH 6.6 treatment activated c-Src and Fyn kinase and induced tyrosine phosphorylation of p 120 catenin (p120ctn) and E-cadherin. Inhibition of Src family kinases by PP2 attenuated the pH 6.6-induced tyrosine phosphorylation of E-cadherin and p120ctn, and prevented the loss of these proteins from AJs. In addition, E-cadherin was bound to Hakai and ubiquitinated. Furthermore, pH 6.6- induced detachment of E-cadherin from AJs was blocked by pretreatment with MG132 or NH4Cl, indicating the involvement : of ubiquitin-proteasomal/lysosomal degradation of E- cadherin. An early loss of p120ctn prior to E-cadherin detachment from AJs was noted, concomitant with a decreased association between p120ctn and E-cadherin at pH 6.6. PP2 pretreatment prevented the dissociation of these two proteins. In conclusion, pH 6.6 activated Src kinases, resulting in tyrosine phosphorylation of E-cadherin and p120 ctn and a weakening of the association of E-cadherin with p 120ctn and contributing to the instability of E-cadherin at AJs. | en |
dc.language | en-us | en |
dc.language.iso | en_US | - |
dc.relation | JOURNAL OF CELLULAR BIOCHEMISTRY v.108 n.4 pp.851-859 | en |
dc.relation.ispartof | Journal of Cellular Biochemistry | en_US |
dc.subject | EXTRACELLULAR ACIDIC PH | en |
dc.subject | ADHERENS JUNCTION | en |
dc.subject | E-CADHERIN | en |
dc.subject | p120 CATENIN | en |
dc.subject | c-Src | en |
dc.subject | FYN KINASE | en |
dc.subject.classification | [SDGs]SDG3 | - |
dc.subject.other | 4 amino 7 tert butyl 5 (4 chlorophenyl)pyrazolo[3,4 d]pyrimidine; ammonium chloride; benzyloxycarbonylleucylleucylleucinal; catenin; protein kinase Fyn; protein tyrosine kinase; uvomorulin; article; cancer cell culture; cell contact; cell interaction; cell junction; down regulation; enzyme modification; human; human cell; oncogene src; pH measurement; priority journal; protein phosphorylation; Adherens Junctions; Cadherins; Catenins; Cell Membrane; Enzyme Inhibitors; Gene Expression Regulation; Hep G2 Cells; Humans; Hydrogen-Ion Concentration; Lysosomes; Phosphorylation; Proteasome Endopeptidase Complex; Proto-Oncogene Proteins c-fyn; src-Family Kinases; Ubiquitin | - |
dc.title | An Acidic Extracellular Ph Disrupts Adherens Junctions in Hepg2 Cells by Src Kinases-Dependent Modification of E-Cadherin | en |
dc.type | journal article | en |
dc.identifier.doi | 10.1002/jcb.22313 | - |
dc.relation.pages | 851-859 | - |
item.languageiso639-1 | en_US | - |
item.cerifentitytype | Publications | - |
item.fulltext | no fulltext | - |
item.openairecristype | http://purl.org/coar/resource_type/c_6501 | - |
item.openairetype | journal article | - |
item.grantfulltext | none | - |
顯示於: | 醫學系 |
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