DC Field | Value | Language |
---|---|---|
dc.contributor.author | Kang, YJ | - |
dc.contributor.author | Jeon, ES | - |
dc.contributor.author | Lee, HJ | - |
dc.contributor.author | Oh, YS | - |
dc.contributor.author | Suh, PG | - |
dc.contributor.author | Jung, JS | - |
dc.contributor.author | Donowitz, M | - |
dc.contributor.author | Kim, JH | - |
dc.date.accessioned | 2016-03-31T12:27:57Z | - |
dc.date.available | 2016-03-31T12:27:57Z | - |
dc.date.created | 2009-02-28 | - |
dc.date.issued | 2004-07 | - |
dc.identifier.issn | 0898-6568 | - |
dc.identifier.other | 2004-OAK-0000004238 | - |
dc.identifier.uri | https://oasis.postech.ac.kr/handle/2014.oak/17940 | - |
dc.description.abstract | Platelet-derived growth factor (PDGF) has multiple functions including inhibition of apoptosis and promotion of cell proliferation. In this study. we show that Na+/H+ exchanger regulatory factor 2 (NHERF2) binds to the carboxyl-terminal PDZ domain-binding motif of the PDGF receptor through a PDZ domain-mediated interaction, and evaluate the consequence on PDGF-induced proliferation. Stable transfection with NHERF2 increased the PDGF-induced phosphorylation of ERK and Akt in Ratl embryonic fibroblasts. The phosphorylation of Akt was blocked by pretreatment with LY294002, a PI-3-kinase inhibitor, in both Rat1/NHERF2 and Rat1/vector cells. In Rat1/vector cells, PDGF-induced phosphorylation of ERK was completely inhibited by pretreatment with PD98059, a MEK inhibitor. In contrast, the NHERF2-dependent increase of ERK phosphorylation was not affected by pretreatment with PD98059 in Rat1/NHERF2 cells. Thus, the NHERF2dependent increase of ERK phosphorylation occurs in a MEK-independent fashion. Pretreatment with PP2, a specific inhibitor of Src family tyrosine kinase, completely blocked the NHERF2-dependent increase of the phosphorylation of ERK and Akt, suggesting that NHERF2 upregulates Erk phosphorylation through a Src family kinase-dependent pathway. Consistent with these results, the PDGF-induced thymidine incorporation was increased in Rat1/NHERF2 cells, and the NHERF2-dependent increase of thymidine incorporation was prevented by treatment with LY294002 and PP2 but not with PD98059. These results suggest that NHERF2 stimulates PDGF-induced proliferation by increasing PI-3-kinase/Akt, MEKindependent ERK, and Src family kinase-mediated signaling pathways. (C) 2004 Elsevier Inc. All rights reserved. | - |
dc.description.statementofresponsibility | X | - |
dc.language | English | - |
dc.publisher | ELSEVIER SCIENCE INC | - |
dc.relation.isPartOf | CELLULAR SIGNALLING | - |
dc.subject | PDGF | - |
dc.subject | NHERF2 | - |
dc.subject | PDZ | - |
dc.subject | proliferation | - |
dc.subject | MEK | - |
dc.subject | Src | - |
dc.subject | EXCHANGER REGULATORY FACTOR | - |
dc.subject | PDZ-CONTAINING PROTEINS | - |
dc.subject | NA+/H+ EXCHANGER-3 | - |
dc.subject | SIGNAL-TRANSDUCTION | - |
dc.subject | ACTIN CYTOSKELETON | - |
dc.subject | NHE3 KINASE | - |
dc.subject | ACTIVATION | - |
dc.subject | RECEPTOR | - |
dc.subject | PDGF | - |
dc.subject | REQUIRES | - |
dc.title | NHERF2 increases platelet-derived growth factor-induced proliferation through PI-3-kinase/Akt-, ERK-, and Src family kinase-dependent pathway | - |
dc.type | Article | - |
dc.contributor.college | 생명과학과 | - |
dc.identifier.doi | 10.1016/j.cellsig.2003.12.003 | - |
dc.author.google | Kang, YJ | - |
dc.author.google | Jeon, ES | - |
dc.author.google | Lee, HJ | - |
dc.author.google | Oh, YS | - |
dc.author.google | Suh, PG | - |
dc.author.google | Jung, JS | - |
dc.author.google | Donowitz, M | - |
dc.author.google | Kim, JH | - |
dc.relation.volume | 16 | - |
dc.relation.issue | 7 | - |
dc.relation.startpage | 791 | - |
dc.relation.lastpage | 800 | - |
dc.contributor.id | 10052640 | - |
dc.relation.journal | CELLULAR SIGNALLING | - |
dc.relation.index | SCI급, SCOPUS 등재논문 | - |
dc.relation.sci | SCI | - |
dc.collections.name | Journal Papers | - |
dc.type.rims | ART | - |
dc.identifier.bibliographicCitation | CELLULAR SIGNALLING, v.16, no.7, pp.791 - 800 | - |
dc.identifier.wosid | 000221386100004 | - |
dc.date.tcdate | 2019-01-01 | - |
dc.citation.endPage | 800 | - |
dc.citation.number | 7 | - |
dc.citation.startPage | 791 | - |
dc.citation.title | CELLULAR SIGNALLING | - |
dc.citation.volume | 16 | - |
dc.contributor.affiliatedAuthor | Suh, PG | - |
dc.identifier.scopusid | 2-s2.0-2042444455 | - |
dc.description.journalClass | 1 | - |
dc.description.journalClass | 1 | - |
dc.description.wostc | 11 | - |
dc.type.docType | Article | - |
dc.subject.keywordPlus | EXCHANGER REGULATORY FACTOR | - |
dc.subject.keywordPlus | PDZ-CONTAINING PROTEINS | - |
dc.subject.keywordPlus | NA+/H+ EXCHANGER-3 | - |
dc.subject.keywordPlus | SIGNAL-TRANSDUCTION | - |
dc.subject.keywordPlus | ACTIN CYTOSKELETON | - |
dc.subject.keywordPlus | NHE3 KINASE | - |
dc.subject.keywordPlus | ACTIVATION | - |
dc.subject.keywordPlus | RECEPTOR | - |
dc.subject.keywordPlus | PDGF | - |
dc.subject.keywordPlus | REQUIRES | - |
dc.subject.keywordAuthor | PDGF | - |
dc.subject.keywordAuthor | NHERF2 | - |
dc.subject.keywordAuthor | PDZ | - |
dc.subject.keywordAuthor | proliferation | - |
dc.subject.keywordAuthor | MEK | - |
dc.subject.keywordAuthor | Src | - |
dc.relation.journalWebOfScienceCategory | Cell Biology | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Cell Biology | - |
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