Inhibition of H-Ras and MAPK is compensated by PKC-dependent pathways in annexin A6 expressing cells
| Autor: | Carlos Enrich, William E. Hughes, Francesc Tebar, Laia Cubells, Iñaki de Diego, Rachael Evans, Peta Wood, Thomas Grewal, Toni E. Hayes, Albert Pol, Sandra Vilà de Muga, Carles Rentero, Kerry-Anne Rye |
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| Rok vydání: | 2006 |
| Předmět: |
MAPK/ERK pathway
MAP Kinase Kinase 2 PDZ domain MAP Kinase Kinase 1 CHO Cells Biology Phosphatidylinositol 3-Kinases Cricetulus Annexin Cricetinae Anti-apoptotic Ras signalling cascade Animals Humans Annexin A6 Phosphorylation Scavenger receptor Extracellular Signal-Regulated MAP Kinases Protein Kinase C PI3K/AKT/mTOR pathway Protein kinase C Chinese hamster ovary cell Cell Membrane Lipoproteins HDL3 Cell Biology Cell biology Enzyme Activation Cholesterol ras Proteins Calcium Lipoproteins HDL Signal Transduction |
| Zdroj: | Cellular Signalling. 18:1006-1016 |
| ISSN: | 0898-6568 |
| Popis: | High-density lipoprotein (HDL)-induced activation of the Ras/MAPK pathway can be mediated by protein kinase C (PKC)-dependent and independent pathways. Although both pathways co-exist in cells, we showed that binding of HDL to scavenger receptor BI (SR-BI) in CHO cells activates Ras and MAPK in a PKC-independent manner. We have recently identified that HDL-induced activation of Ras and Raf-1 is reduced in annexin A6 expressing CHO cells (CHOanx6). In the present study we demonstrate that despite the loss of Ras and Raf-1 activity, HDL induces MAPK phosphorylation in CHOanx6 cells. Since annexin A6 is a PKCalpha-binding protein we therefore investigated the possible involvement of PKC in HDL-induced Ras and MAPK activation in CHOanx6 cells. Taken together our findings demonstrate that HDL-induced H-Ras and MAPK activation is PKC-dependent in cells expressing annexin A6 to compensate for the loss of PKC-independent activation of H-Ras and MAPK. |
| Databáze: | OpenAIRE |
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