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DC Field | Value | Language |
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dc.citation.endPage | 800 | - |
dc.citation.number | 7 | - |
dc.citation.startPage | 791 | - |
dc.citation.title | CELLULAR SIGNALLING | - |
dc.citation.volume | 16 | - |
dc.contributor.author | Kang, YJ | - |
dc.contributor.author | Jeon, ES | - |
dc.contributor.author | Lee, HJ | - |
dc.contributor.author | Oh, YS | - |
dc.contributor.author | Suh, Pann-Ghill | - |
dc.contributor.author | Jung, JS | - |
dc.contributor.author | Donowitz, M | - |
dc.contributor.author | Kim, JH | - |
dc.date.accessioned | 2023-12-22T10:45:54Z | - |
dc.date.available | 2023-12-22T10:45:54Z | - |
dc.date.created | 2014-09-02 | - |
dc.date.issued | 2004-07 | - |
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 Rat1 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 NHERF2-dependent 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 up-regulates 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. | - |
dc.identifier.bibliographicCitation | CELLULAR SIGNALLING, v.16, no.7, pp.791 - 800 | - |
dc.identifier.doi | 10.1016/j.cellsig.2003.12.003 | - |
dc.identifier.issn | 0898-6568 | - |
dc.identifier.scopusid | 2-s2.0-2042444455 | - |
dc.identifier.uri | https://scholarworks.unist.ac.kr/handle/201301/5677 | - |
dc.identifier.url | http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=2042444455 | - |
dc.identifier.wosid | 000221386100004 | - |
dc.language | 영어 | - |
dc.publisher | ELSEVIER SCIENCE INC | - |
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.description.journalRegisteredClass | scopus | - |
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