Nuclear translocation and overexpression of GAPDH by the hyper-pressure in retinal ganglion cell

Proteomic characterization of differentially expressed proteins associated with no stress in retinal ganglion cells

“…Interestingly, GSNO treatment caused a concentration-dependent decrease in the cytosolic expression of GAPDH, whereas its nuclear expression increased significantly. In a previous study, hyper-pressure-induced apoptosis resulted in aberrant GAPDH protein expression and the nuclear accumulation of GAPDH in retinal ganglion cells (19).…”

“…We previously reported that GAPDH translocates to and accumulates within the nucleus of retinal ganglion cells (RGC-5) via hyper-pressure, and that its expression increases during hyper-pressure-induced cell death (19). Here, we used proteomic analysis to demonstrate that RGC-5 cells differentially express various proteins during s-nitrosoglutathione (GSNO)-induced cell death.…”

p53 is not necessary for nuclear translocation of GAPDH during NO-induced apoptosis

“…One of the most abundant endogenous nitrosothiols, S-nitrosoglutathione (GNSO), exhibits NO-like biological activities, and the release of NO from GSNO promotes NO-induced apoptosis (7). Moreover, glyceraldehyde-3-phosphate dehydrogenase (GAPDH) translocates to the nucleus during apoptotic cell death caused by several environmental stressors, including hyper-pressure, as we reported previously (8). We recently showed that GSNOinduced apoptosis in RGC-5 cells is accompanied by nuclear translocation and the accumulation of GAPDH (9,10).…”

“…The nuclear relocalization of GAPDH was recently reported as part of the cell death cascade (8,(16)(17)(18). To investigate the relocalization of GAPDH in HepG2 and Hep3B cells, the subcellular localization of GAPDH was compared by fluorescent immunostaining using specific antibodies against GAPDH.…”

“…Its role in apoptosis in various neuronal cell types has been shown to be related to its subcellular relocalization. However, the mechanisms underlying the translocation of GAPDH and its function in the nucleus remain unclear (8,(19)(20)(21)(22). A recent study showed that the nuclear translocation of GAPDH during cell death requires S-nitrosylation, which triggers binding to the E3 ubiquitin ligase Siah-1, a potential carrier/shuttle protein (7,22,23).…”