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Enhancement by GOSPEL protein of GAPDH aggregation induced by nitric oxide donor and its inhibition by NAD +
Author(s) -
González María C.,
Romero Jorge M.,
Ingaramo María C.,
Muñoz Sosa Christian J.,
Curtino Juan A.,
Carrizo María E.
Publication year - 2016
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.12242
Subject(s) - glyceraldehyde 3 phosphate dehydrogenase , nad+ kinase , chemistry , dehydrogenase , in vitro , gospel , apoptosis , biochemistry , microbiology and biotechnology , enzyme , biology , art , literature
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.