dc.creatorParis Pizarro, Irmgard
dc.creatorPérez Pastene, Carolina
dc.creatorCárdenas, Sergio
dc.creatorIturra, Patricio
dc.creatorMuñoz, Patricia
dc.creatorCouve, Eduardo
dc.creatorCaviedes Fernández, Pablo
dc.creatorSegura Aguilar, Juan
dc.date.accessioned2011-09-29T13:49:36Z
dc.date.available2011-09-29T13:49:36Z
dc.date.created2011-09-29T13:49:36Z
dc.date.issued2010-01-20
dc.identifierNEUROTOXICITY RESEARCH, Volume: 18, Issue: 1, Special Issue: SI, Pages: 82-92, 2010
dc.identifier1029-8428
dc.identifierhttps://repositorio.uchile.cl/handle/2250/119308
dc.description.abstractAbstract In previous studies, we observed that cells treated with aminochrome obtained by oxidizing dopamine with oxidizing agents dramatically changed cell morphology, thus posing the question if such morphological changes were dependent on aminochrome or the oxidizing agents used to produce aminochrome. Therefore, to answer this question, we have now purified aminochrome on a CM-Sepharose 50–100 column and, using NMR studies, we have confirmed that the resulting aminochrome was pure and that it retained its structure. Fluorescence microscopy with calcein-AM and transmission electron microscopy showed that RCSN-3 cells presented an elongated shape that did not change when the cells were incubated with 50 lMaminochrome or 100 lMdicoumarol, an inhibitor of DT-diaphorase. However, the cell were reduced in size and the elongated shape become spherical when the cells where incubated with 50 lM aminochrome in the presence of 100 lM dicoumarol. Under these conditions, actin, alpha-, and beta-tubulin cytoskeleton filament networks became condensed around the cell membrane. Actin aggregates were also observed in cells processes that connected the cells in culture. These results suggest that aminochrome one-electron metabolism induces the disruption of the normal morphology of actin, alpha-, and beta-tubulin in the cytoskeleton, and that DT-diaphorase prevents these effects.
dc.languageen
dc.publisherSPRINGER
dc.subjectActin
dc.titleAminochrome Induces Disruption of Actin, Alpha-, and Beta-Tubulin Cytoskeleton Networks in Substantia-Nigra-Derived Cell Line
dc.typeArtículo de revista


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