Sea urchin deciliation induces thermoresistance and activates the p38 mitogen-activated protein kinase pathway

• Published in: Cell stress & chaperones 2003-01, Vol.8 (1), p.70-75
• Main Authors: Casano, Caterina, Roccheri, Maria Carmela, Maenza, Luisa, Migliore, Silvia, Gianguzza, Fabrizio
• Format: Article
• Language: English
• Subjects: Animals; Antibodies; Antibodies, Monoclonal; Apoptosis; Cilia - physiology; Electrophoresis, Polyacrylamide Gel; Embryos; Enzyme Activation; Gastrula - enzymology; Gastrula - physiology; Heat shock proteins; Heat shock response; Heat tolerance; Hot Temperature; Imidazoles - pharmacology; Mitogen-Activated Protein Kinases - antagonists & inhibitors; Mitogen-Activated Protein Kinases - metabolism; Original; Original s; p38 Mitogen-Activated Protein Kinases; Phosphorylation; Pyridines - pharmacology; Sea urchins; Sea Urchins - embryology; Shock heating; Signal Transduction - physiology; Stress response; Stress, Physiological
• ISSN: 1355-8145; 1466-1268
• DOI: 10.1379/1466-1268(2003)8<70:SUDITA>2.0.CO;2

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.