Full metadata record
DC Field | Value | Language |
---|---|---|
dc.contributor.author | 한중수 | - |
dc.date.accessioned | 2018-04-16T03:34:45Z | - |
dc.date.available | 2018-04-16T03:34:45Z | - |
dc.date.issued | 2012-03 | - |
dc.identifier.citation | Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, Vol.1823, No.6 [2012], p1082-1091 | en_US |
dc.identifier.issn | 0006-3002 | - |
dc.identifier.uri | http://www.sciencedirect.com/science/article/pii/S016748891200081X?via%3Dihub | - |
dc.identifier.uri | http://hdl.handle.net/20.500.11754/67682 | - |
dc.description.abstract | The purpose of this study was to identify the role of phospholipase D (PLD) isozymes in Bcl-2 expression. Overexpression of PLD1 or PLD2 increased Bcl-2 expression and phosphatidic acid (PA), the product of PLDs, also upregulated Bcl-2 expression. Treatment with PA activated the phospholipase A2 (PLA2)/Gi/ERK1/2, RhoA/Rho-associated kinase (ROCK)/p38 MAPK, and Rac1/p38 MAPK pathways. PA-induced phosphorylation of ERK1/2 was attenuated by a PLA2 inhibitor (mepacrine) and, a Gi protein inhibitor (pertussis toxin, PTX). On the other hand, p38 MAPK phosphorylation was attenuated by a dominant negative Rac1 and a specific Rho-kinase inhibitor (Y-27632). These results suggest that PLA2/Gi acts at the upstream of ERK1/2, while Rac1 and RhoA/ROCK act upstream of p38 MAPK. We next, tried to determine which transcription factor is involved in PLD-related Bcl-2 expression. When signal transducer and activator of transcription 3 (STAT3) activity was blocked by a STAT3 specific siRNA, PA-induced Bcl-2 expression was remarkably decreased, suggesting that STAT3 is an essential transcription factor linking PLD to Bcl-2 upregulation. Taken together, these findings indicate that PLD acts as an important regulator in Bcl-2 expression by activating STAT3 involving the phosphorylation of Ser727 through the PLA2/Gi/ERK1/2, RhoA/ROCK/p38 MAPK, and Rac1/p38 MAPK pathways. | en_US |
dc.description.sponsorship | This study was supported by a Korea Research Foundation Grant funded by the Korean Government (KRF-2008-313-C00751) and by a National Research Foundation of Korea (NRF) grant funded by the Korean Government (MEST) (2010–0029503). | en_US |
dc.language.iso | en | en_US |
dc.publisher | Elsevier Science B.V., Amsterdam. | en_US |
dc.subject | Phospholipase D (PLD) | en_US |
dc.subject | Phosphatidic acid (PA) | en_US |
dc.subject | Bcl-2 | en_US |
dc.subject | MAPK | en_US |
dc.subject | RhoA | en_US |
dc.subject | STAT3 (ser727) | en_US |
dc.title | Overexpression of phospholipase D enhances Bcl-2 expression by activating STAT3 through independent activation of ERK and p38MAPK in HeLa cells | en_US |
dc.type | Article | en_US |
dc.relation.no | 6 | - |
dc.relation.volume | 1823 | - |
dc.identifier.doi | 10.1016/j.bbamcr.2012.03.015 | - |
dc.relation.page | 1082-1091 | - |
dc.relation.journal | BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH | - |
dc.contributor.googleauthor | Choi, H. J. | - |
dc.contributor.googleauthor | Han, J. S. | - |
dc.relation.code | 2012201255 | - |
dc.sector.campus | S | - |
dc.sector.daehak | COLLEGE OF MEDICINE[S] | - |
dc.sector.department | DEPARTMENT OF MEDICINE | - |
dc.identifier.pid | jshan | - |
dc.identifier.researcherID | 23974393200 | - |
dc.identifier.orcid | 0000-0002-0875-6158 | - |
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