Please use this identifier to cite or link to this item: http://hdl.handle.net/11455/38516
DC FieldValueLanguage
dc.contributor.authorChen, C.H.en_US
dc.contributor.author赫, 林zh_TW
dc.contributor.authorLin, H.en_US
dc.contributor.authorChuang, S.M.en_US
dc.contributor.authorLin, S.Y.en_US
dc.contributor.authorChen, J.J.W.en_US
dc.contributor.author陳健尉zh_TW
dc.date2010zh_TW
dc.date.accessioned2014-06-06T08:00:53Z-
dc.date.available2014-06-06T08:00:53Z-
dc.identifier.issn0014-4827zh_TW
dc.identifier.urihttp://hdl.handle.net/11455/38516-
dc.description.abstractAcidosis is a common stress in solid tumours and is also a major determinant of tumour growth, metabolism, and metastasis. During cellular stress, heat shock proteins play an important role in actin cytoskeleton stability. HLJ1, a member of the DnaJ-like heat shock protein 40, has been characterised as a tumour suppressor gene; however, the effect of acidic stress on HLJ1 is unknown. In this study, we found that the migration ability of human lung adenocarcinoma cells was significantly impaired following the increased protein level of HLJ1 under acidic culture conditions. However, HLJ1 transcriptional activity was no different in the normal and acidic culture medium. Incubation of the cells in an acidic extracellular pH (pHe 6.4) caused up-regulated tyrosine phosphorylation of HLJ1 within 2 h. We further identified the sub-cellular distribution of tyrosine phospho-HLJ1 and its tyrosine-phosphorylated sites. Most importantly, acidic stress was observed to remarkably enhance the interaction between HLJ1 and beta-actin, which was a tyrosine phosphorylation-dependent association. In conclusion, our results not only validate that HLJ1 is a tyrosine phosphoprotein, but also suggest that the increased level of tyrosine phospho-HLJ1 is crucial for binding with the actin cytoskeleton, especially in acidic pHe. We propose that acidic stress increases the association between HLJ1 and beta-actin to modulate migration of human lung cancer cells. (C) 2010 Elsevier Inc. All rights reserved.en_US
dc.language.isoen_USzh_TW
dc.relationExperimental Cell Researchen_US
dc.relation.ispartofseriesExperimental Cell Research, Volume 316, Issue 17, Page(s) 2910-2921.en_US
dc.relation.urihttp://dx.doi.org/10.1016/j.yexcr.2010.06.027en_US
dc.subjectAcidic stressen_US
dc.subjectHLJ1en_US
dc.subjectTyrosine phosphorylationen_US
dc.subjectbeta-actinen_US
dc.subjectLung canceren_US
dc.subjectcellsen_US
dc.subjectheat-shock protein-27en_US
dc.subjecthuman-melanoma cellsen_US
dc.subjectextracellular phen_US
dc.subjectsignalingen_US
dc.subjectpathwayen_US
dc.subjecttumor-suppressoren_US
dc.subjectexpressionen_US
dc.subjectmicroenvironmenten_US
dc.subjectkinaseen_US
dc.subjecttranscriptionen_US
dc.subjectmetastasisen_US
dc.titleAcidic stress facilitates tyrosine phosphorylation of HLJ1 to associate with actin cytoskeleton in lung cancer cellsen_US
dc.typeJournal Articlezh_TW
dc.identifier.doi10.1016/j.yexcr.2010.06.027zh_TW
item.cerifentitytypePublications-
item.grantfulltextnone-
item.languageiso639-1en_US-
item.fulltextno fulltext-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.openairetypeJournal Article-
Appears in Collections:生命科學系所
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