Journal
FEBS LETTERS
Volume 590, Issue 14, Pages 2210-2220Publisher
WILEY-BLACKWELL
DOI: 10.1002/1873-3468.12242
Keywords
nicotinamide adenine dinucleotide; nitric oxide; nitrosative stress; oxidative stress; protein aggregation
Funding
- Consejo Nacional de Investigaciones Cientificas y Tecnicas (CONICET)
- Fondo para la Investigacion Cientifica y Tecnologica (FONCyT)
- Secretaria de Ciencia y Tecnica-Universidad Nacional de Cordoba (SECyT-UNC)
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Glyceraldehyde-3-phosphate dehydrogenase's (GAPDH's) competitor of Siah Protein Enhances Life (GOSPEL) is the protein that competes with Siah1 for binding to GAPDH under NO-induced stress conditions preventing Siah1-bound GAPDH nuclear translocation and subsequent apoptosis. Under these conditions, GAPDH may also form amyloid-like aggregates proposed to be involved in cell death. Here, we report the in vitro enhancement by GOSPEL of NO-induced GAPDH aggregation resulting in the formation GOSPEL-GAPDH co-aggregates with some amyloid-like properties. Our findings suggest a new function for GOSPEL, contrasting with its helpful role against the apoptotic nuclear translocation of GAPDH. NAD(+) inhibited both GAPDH aggregation and co-aggregation with GOSPEL, a hitherto un-described effect of the coenzyme against the consequences of oxidative stress.
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