RT info:eu-repo/semantics/article
T1 A new procedure for amyloid   oligomers preparation enables the unambiguous testing of their effects on cytosolic and mitochondrial Ca2+ entry and cell death in primary neurons
A1 Caballero, Erica
A1 Calvo Rodríguez, María
A1 Gonzalo Ruiz, Alicia
A1 Villalobos Jorge, Carlos
A1 Núñez Llorente, Lucía
K1 Alzheimer, Enfermedad de
AB Oligomers of the amyloid   peptide (A o) are becoming the most likely neurotoxin in Alzheimer’s disease.Controversy remains on the mechanisms involved in neurotoxicity induced by A o and the targetsinvolved. We have reported that A o promote Ca2+ entry, mitochondrial Ca2+ overload and apoptosisin cultured cerebellar neurons. However, recent evidence suggests that some of these effects could beinduced by glutamate receptor agonists solved in F12, the media in which A o are prepared. Here wehave tested the effects of different media on A o formation and on cytosolic Ca2+ concentration ([Ca2+]cyt)in rat cerebellar and hippocampal cell cultures. We found that A o prepared according to previous protocolsbut solved in alternative media including saline, MEM and DMEM do not allow oligomer formationand fail to increase [Ca2+]cyt. Changes in the oligomerization protocol and supplementation of media withselected salts reported to favor oligomer formation enable A o formation. A o prepared by the new procedureand containing small molecular weight oligomers increased [Ca2+]cyt, promoted mitochondrialCa2+ overload and cell death in cerebellar granule cells and hippocampal neurons. These results foster arole for Ca2+ entry in neurotoxicity induced by A o and provide a reliable procedure for investigating theCa2+ entry pathway promoted by A o.
PB Elsevier
SN 0304-3940
YR 2016
FD 2016
LK http://uvadoc.uva.es/handle/10324/21812
UL http://uvadoc.uva.es/handle/10324/21812
LA eng
NO Neuroscience Letters  Volume 612, 26 January 2016, Pages 66–73
NO Producción Científica
DS UVaDOC
RD 22-nov-2024