In this study, we demonstrate by a variety of approaches (ie, morphological analysis, Western blots, immunolocalization, and the use of specific antibodies) that hyperosmotic deciliation stress of sea urchin embryos induces a thermotolerant response. Deciliation is also able to activate a phosphorylation signaling cascade the effector of which might be the p38 stress-activated protein kinase because we found that the administration of the p38 inhibitor SB203580 to sea urchin deciliated gastrula embryos makes the hyperosmotic deciliation stress lethal.
Casano, C., Roccheri, M., Maenza, L., Migliore, S., Gianguzza, F. (2003). SEA URCHIN DECILIATION INDUCES THERMORESISTANCE AND ACTIVATES THE p38MAP MITOGEN-ACTIVATED PROTEIN KINASE PATHWAY. CELL STRESS & CHAPERONES, 8(1), 70-75.
SEA URCHIN DECILIATION INDUCES THERMORESISTANCE AND ACTIVATES THE p38MAP MITOGEN-ACTIVATED PROTEIN KINASE PATHWAY
CASANO, Caterina;ROCCHERI, Maria Carmela;GIANGUZZA, Fabrizio
2003-01-01
Abstract
In this study, we demonstrate by a variety of approaches (ie, morphological analysis, Western blots, immunolocalization, and the use of specific antibodies) that hyperosmotic deciliation stress of sea urchin embryos induces a thermotolerant response. Deciliation is also able to activate a phosphorylation signaling cascade the effector of which might be the p38 stress-activated protein kinase because we found that the administration of the p38 inhibitor SB203580 to sea urchin deciliated gastrula embryos makes the hyperosmotic deciliation stress lethal.File | Dimensione | Formato | |
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