Enhancement by GOSPEL protein of GAPDH aggregation induced by nitric oxide donor and its inhibition by NAD+

GONZÁLEZ, MARÍA C; ROMERO JORGE M; INGARAMO, MARÍA C; MUÑOZ SOSA, CHRISTIAN J; CURTINO JUAN A; CARRIZO, MARÍA E

FEBS LETTERS

ELSEVIER SCIENCE BV

Lugar: Amsterdam; Año: 2016

0014-5793

lyceraldehyde-3-phosphate dehydrogenase?s (GAPDH?s) competitor of SiahProtein Enhances Life (GOSPEL) is the protein that competes with Siah1for binding to GAPDH under NO-induced stress conditions preventing Siah1-bound GAPDH nuclear translocation and subsequent apoptosis. Under theseconditions, GAPDH may also form amyloid-like aggregates proposed to beinvolved in cell death. Here, we report the in vitro enhancement by GOSPELof NO-induced GAPDH aggregation resulting in the formation GOSPELGAPDHco-aggregates with some amyloid-like properties. Our findings suggesta new function for GOSPEL, contrasting with its helpful role againstthe apoptotic nuclear translocation of GAPDH. NAD+ inhibited bothGAPDH aggregation and co-aggregation with GOSPEL, a hitherto undescribedeffect of the coenzyme against the consequences of oxidative stress.