AgeingOkadaic acid modulates the cytoskeleton changes induced by amyloid peptide (25-35) in cultured astrocytesSalinero, O1; Moreno-Flores, M T.1; Wandosell, F1,2Author Information 1Centro de Biología Molecular ‘Serero Ochoa’, CSIC-Universidad Autonoma de Madrid, Cantoblanco-Madrid 28049, Spain 2Corresponding Author: F. Wandosell ACKNOWLEDGEMENTS: We are grateful to Dr J. Avila (UAM-CBM, Spain) for providing polyclonal antibody against Vimentin. We thank Dr Mar Perez for the electron microscopy experiments. We also thank Dr Filip Lim and Dr J. Diaz-Nido for manuscript corrections and advice. This work was supported by grants DGYT (PB93–0155), the European Sandoz Foundation for Gerontological Research), and an institutional grant from Fundación Ramón Areces. Website publication 3 October 1997 Received 6 August 1997; accepted 20 August 1997 NeuroReport: October 20th, 1997 - Volume 8 - Issue 15 - p 3333-3338 Buy Abstract AMYLOID β-protein (25–35) (βA) induced a marked morphological change in astrocytes, changing their flat polygonal shape into a stellate process-bearing morphology. The changes induced by βA were concentration and time-dependent, whereas the addition of a scrambled peptide did not alter astrocyte morphology. We discard the possibility of βA-astrocytes being type II-like astrocytes. We also analysed the influence of the presence of kinase and phosphate inhibitors on this morphological change. Our data indicate that the βA-induced phenotype was not affected by the inhibition of protein tyrosine kinase or tyrosine phosphatases. Only the addition of okadaic acid to astrocytes prevented the morphological transformation from flat to stellate shape, induced by βA (25–35). Inhibition of the stellate phenotype by okadaic acid was initiated at a concentration of 10 nM which suggested that either phosphatase 2A or 1 plays an important role in the βA astrocytic transformation. © Lippincott-Raven Publishers.