Cellular prion protein mediates early apoptotic proteome alternation and phospho-modification in human neuroblastoma cells.

ABSTRACT: Anti-apoptotic properties of physiological and elevated levels of the cellular prion protein (PrP^c) under stress conditions are well documented. Yet, detrimental effects of elevated PrP^c levels under stress conditions, such as exposure to staurosporine (STS) have also been described. In the present study, we focused on discerning early apoptotic STS-induced proteome and phospho-proteome changes in SH-SY5Y human neuroblastoma cells stably transfected either with an empty or PRNP-containing vector, expressing physiological or supraphysiological levels of PrP^c, respectively. PrP^c-overexpression per se appears to stress the cells under STS-free conditions as indicated by diminished cell viability of PrP^c-overexpressing versus control cells

SUBMITTER: Zafar S 

PROVIDER: S-EPMC5386350 | biostudies-literature | 2017 Jan

REPOSITORIES: biostudies-literature