Artículo
Enhancement by GOSPEL protein of GAPDH aggregation induced by nitric oxide donor and its inhibition by NAD+
Gonzalez, María C.; Romero, Jorge Miguel
; Ingaramo, María Clara
; Muñoz Sosa, Christian Javier
; Curtino, Juan Agustin
; Carrizo Garcia, Maria Elena
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![Icon](/themes/CONICETDigital/images/conicet.png)
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Fecha de publicación:
07/2016
Editorial:
Elsevier Science
Revista:
FEBS Letters
ISSN:
0014-5793
e-ISSN:
1873-3468
Idioma:
Inglés
Tipo de recurso:
Artículo publicado
Clasificación temática:
Resumen
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 undescribed effect of the coenzyme against the consequences of oxidative stress.
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Articulos(CIQUIBIC)
Articulos de CENTRO DE INVEST.EN QCA.BIOL.DE CORDOBA (P)
Articulos de CENTRO DE INVEST.EN QCA.BIOL.DE CORDOBA (P)
Citación
Gonzalez, María C.; Romero, Jorge Miguel; Ingaramo, María Clara; Muñoz Sosa, Christian Javier; Curtino, Juan Agustin; et al.; Enhancement by GOSPEL protein of GAPDH aggregation induced by nitric oxide donor and its inhibition by NAD+; Elsevier Science; FEBS Letters; 590; 14; 7-2016; 2210-2220
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