Journal article
HSP90 modulates actin dynamics: Inhibition of HSP90 leads to decreased cell motility and impairs invasion
Abstract
HSP90, a major molecular chaperone, plays an essential role in the maintenance of several signaling molecules. Inhibition of HSP90 by inhibitors such as 17-allylamino-demethoxy-geldanamycin (17AAG) is known to induce apoptosis in various cancer cells by decreasing the activation or expression of pro-survival molecules such as protein kinase B (Akt). While we did not observe either decrease in expression or activation of pro-survival signaling …
Authors
Taiyab A; Rao CM
Journal
Biochimica et Biophysica Acta, Vol. 1813, No. 1, pp. 213–221
Publisher
Elsevier
Publication Date
January 2011
DOI
10.1016/j.bbamcr.2010.09.012
ISSN
0006-3002
Associated Experts
Fields of Research (FoR)
Medical Subject Headings (MeSH)
ActinsBenzoquinonesBlotting, WesternBreast NeoplasmsCell Line, TumorCell MovementCollagenDrug CombinationsFemaleFluorescent Antibody TechniqueHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsHumansImmunoenzyme TechniquesImmunoprecipitationLactams, MacrocyclicLamininProteoglycansSignal TransductionWound Healing