6533b853fe1ef96bd12ac38a
RESEARCH PRODUCT
Sea urchin deciliation induces thermoresistance and activates the p38 mitogen-activated protein kinase pathway.
Luisa MaenzaMaria Carmela RoccheriCaterina CasanoFabrizio GianguzzaSilvia Miglioresubject
animal structuresHot TemperaturePyridinesp38 mitogen-activated protein kinasesSEA URCHIN DECILIATION p38MAP KINASEBiochemistryp38 Mitogen-Activated Protein KinasesEnzyme activatorStress Physiologicalbiology.animalAnimalsCiliaSettore BIO/06 - Anatomia Comparata E CitologiaPhosphorylationProtein kinase ASea urchinbiologyEffectorImidazolesAntibodies MonoclonalCell BiologyGastrulaOriginal ArticlesMolecular biologyBlotEnzyme ActivationSea Urchinsembryonic structuresPhosphorylationElectrophoresis Polyacrylamide GelSignal transductionMitogen-Activated Protein KinasesSignal Transductiondescription
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.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2003-06-25 | Cell stresschaperones |