The anti-apoptotic activity associated with phosphatidylinositol transfer protein alpha activates the MAPK and Akt/PKB pathway
| Autor: | Gerry T. Snoek, Martijn Schenning, Diana Avram, Karel W. A. Wirtz, Joachim Goedhart, Theodorus W. J. Gadella |
|---|---|
| Přispěvatelé: | Molecular Cytology (SILS, FNWI) |
| Rok vydání: | 2007 |
| Předmět: |
MAPK/ERK pathway
Cannabinoid receptor MAP Kinase Signaling System Apoptosis Biology NF-κB Mice Receptor Cannabinoid CB1 Phospholipase C Animals p42/p44 MAPK Phospholipid Transfer Proteins Phosphorylation Molecular Biology Protein kinase B Protein kinase C Phosphatidylinositol transfer protein PI-TPβ PI-TPα Mitogen-Activated Protein Kinase 1 Mitogen-Activated Protein Kinase 3 Akt/PKB signaling pathway Cell Membrane NF-kappa B Cell Biology Molecular biology Cell biology Enzyme Activation Type C Phospholipases NIH 3T3 Cells Proto-Oncogene Proteins c-akt Phosphatidylinositol transfer protein alpha |
| Zdroj: | Biochimica et Biophysica Acta-Molecular Cell Research, 1783(10), 1700-1706. Elsevier |
| ISSN: | 0006-3002 0167-4889 |
| Popis: | The conditioned medium (CM) from mouse NIH3T3 fibroblast cells overexpressing phosphatidylinositol transfer protein alpha (PI-TPalpha; SPIalpha cells) demonstrates an increased anti-apoptotic activity compared with CM from wild type NIH3T3 (wtNIH3T3) cells. As previously shown, the anti-apoptotic activity acts by activating a G protein-coupled receptor, most probably a cannabinoid 1 (CB1)-like receptor as the activity was blocked by both pertussis toxin and rimonabant [M. Schenning, C.M. van Tiel, D. Van Manen, J.C. Stam, B.M. Gadella, K.W. Wirtz and G.T. Snoek, Phosphatidylinositol transfer protein alpha regulates growth and apoptosis of NIH3T3 cells: involvement of a cannabinoid 1-like receptor, J. Lipid Res. 45 (2004) 1555-1564]. The CB1 receptor appears to be expressed in mouse fibroblast cells, at levels in the order SPIalphawtNIH3T3SPIbeta cells (i.e. wild type cells overexpressing PI-TPbeta). Upon incubation of SPIbeta cells with the PI-TPalpha-dependent anti-apoptotic factors, both the ERK/MAP kinase and the Akt/PKB pathway are activated in a CB1 receptor dependent manner as shown by Western blotting. In addition, activation of ERK2 was also shown by EYFP-ERK2 translocation to the nucleus, as visualized by confocal laser scanning microscopy. The subsequent activation of the anti-apoptotic transcription factor NF-kappaB is in line with the increased resistance towards UV-induced apoptosis. On the other hand, receptor activation by CM from SPIalpha cells was not linked to phospholipase C activation as the YFP-labelled C2-domain of protein kinase C was not translocated to the plasma membrane of SPIbeta cells as visualized by confocal laser scanning microscopy. |
| Databáze: | OpenAIRE |
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