Enhancement by GOSPEL protein of GAPDH aggregation induced by nitric oxide donor and its inhibition by NAD(.)
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Updated: Mar 19, 2026
Application of Genetically Encoded Fluorescent Nitric Oxide (NO•) Probes, the geNOps, for Real-time Imaging of NO• Signals in Single Cells
Published on: March 16, 2017
María C González1, Jorge M Romero1, María C Ingaramo1
1Departamento de Química Biológica, Facultad de Ciencias Químicas, Centro de Investigaciones en Química Biológica de Córdoba (CIQUIBIC), Universidad Nacional de Córdoba-Consejo Nacional de Investigaciones Científicas y Técnicas (UNC-CONICET), Universidad Nacional de Córdoba, Argentina.
Insights
GOSPEL protein enhances NO-induced GAPDH aggregation, forming amyloid-like co-aggregates. NAD+ inhibits this aggregation, revealing a new role for GOSPEL and NAD+ in oxidative stress response.
Area of Science:
- Biochemistry
- Molecular Biology
- Cellular Stress Response
Background:
- Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) plays a role in apoptosis under oxidative stress.
- Siah Protein Enhances Life (GOSPEL) protein competes with Siah1 for GAPDH binding, inhibiting nuclear translocation and apoptosis.
- GAPDH can form amyloid-like aggregates implicated in cell death during stress.
Discussion:
- This study investigates the in vitro effect of GOSPEL on NO-induced GAPDH aggregation.
- GOSPEL promotes the formation of GOSPEL-GAPDH co-aggregates with amyloid-like properties.
- This highlights a novel, potentially detrimental function of GOSPEL distinct from its anti-apoptotic role.
Key Insights:
- GOSPEL enhances NO-induced aggregation of GAPDH.
- Formation of GOSPEL-GAPDH co-aggregates with amyloid-like characteristics observed.
- NAD+ effectively inhibits both GAPDH aggregation and GOSPEL-GAPDH co-aggregation.
Outlook:
- Further research is needed to elucidate the precise mechanisms of GOSPEL-mediated aggregation.
- Investigating the physiological relevance of these co-aggregates in cellular processes.
- Exploring therapeutic strategies targeting GAPDH aggregation and NAD+ levels in oxidative stress conditions.
Abstract:
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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