| dc.creator | INOSTROZA,JUAN | |
| dc.creator | SÁENZ,LEONARDO | |
| dc.creator | CALAF,GLORIA | |
| dc.creator | CABELLO,GERTRUDIS | |
| dc.creator | PARRA,EDUARDO | |
| dc.date | 2005-01-01 | |
| dc.date.accessioned | 2019-05-02T21:21:25Z | |
| dc.date.available | 2019-05-02T21:21:25Z | |
| dc.identifier | https://scielo.conicyt.cl/scielo.php?script=sci_arttext&pid=S0716-97602005000200006 | |
| dc.identifier.uri | http://revistaschilenas.uchile.cl/handle/2250/81587 | |
| dc.description | The specific signaling connections between the mitogen-activated protein kinases (MAPK) such as c-Jun N-terminal kinase (JNK-1) and phosphatases PP4 and M3/6, affecting the family of early nuclear factors, is complex and remains poorly understood. JNK-1 regulates cellular differentiation, apoptosis and stress responsiveness by up-regulating early nuclear factors such as c-Jun, a member of the activating protein (AP-1) family, and the Early Growth Factor (EGR-1). C-Jun, when phosphorylated by c-Jun N-terminal kinase (JNK-1) associates with c-Fos to form the AP-1 transcription factor that activates gene expression. We have investigated the regulation of the JNK-1 kinase by co-transfecting phosphatases PP4 and M3/6 in prostate cancer cell lines PC-3 and LNCaP, which have been previously stimulated with human EGF or cisplatin. Co-transfections of plasmids expressing the JNK-1 and the serine/threonine phosphatases PP4 resulted in a significant increase in JNK-1 activity in both PC3 and LNCaP cells. In contrast, co-transfection of JNK-1 with the dual specific phosphatase serine/threonine M3/6 showed only a marginal effect in JNK-1 activity. The phosphatase M3/6 also failed in blocking the induction of JNK-1 activity observed in presence of PP4. The higher activity of JNK-1 was associated with increased activities of the factors c-Jun/AP-1 and EGR-1. This suggests that JNK-1 activity in PC-3 and LNCaP cells requires not only active PP4 for stable maintenance but also suggests that the relative degree of phosphorylation of multiple cellular components is the determinant of JNK-1 stability. | |
| dc.format | text/html | |
| dc.language | en | |
| dc.publisher | Sociedad de Biología de Chile | |
| dc.relation | 10.4067/S0716-97602005000200006 | |
| dc.rights | info:eu-repo/semantics/openAccess | |
| dc.source | Biological Research v.38 n.2-3 2005 | |
| dc.subject | prostate cancer | |
| dc.subject | phosphatase PP4 | |
| dc.subject | kinase JNK-1 | |
| dc.title | Role of the phosphatase PP4 in the activation of JNK-1 in prostate carcinoma cell lines PC-3 and LNCaP resulting in increased AP-1 and EGR-1 activity | |
