GAPDH: Biological Properties and Diversity

Seidler, Norbert W.

doi:10.1007/978-94-007-4716-6

Cited by 41 publications

(41 citation statements)

References 461 publications

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“…GAPDH catalyzes the reversible oxidative phosphorylation of G3P to 1,3-bisphosphoglycerate (1,3-BPG) using NAD + and inorganic phosphate. 1,3-BPG is a strong product inhibitor of GAPDH [ 74 ]. Mechanistically, GAPDH employs a conserved active site cysteine (Cys152 in humans) for a nucleophilic attack on the aldehyde moiety of G3P forming a thiohemiacetal that rearranges to an acyl-enzyme intermediate with a hydride transfer to NAD + .…”

Section: Glyceraldehyde 3-phosphate Dehydrogenase Inhibitionmentioning

confidence: 99%

“…Mechanistically, GAPDH employs a conserved active site cysteine (Cys152 in humans) for a nucleophilic attack on the aldehyde moiety of G3P forming a thiohemiacetal that rearranges to an acyl-enzyme intermediate with a hydride transfer to NAD + . The acyl-enzyme intermediate is resolved by an inorganic phosphate attack [ 74 ]. The same active site cysteine involved in catalysis functions as a thiol switch, as discussed below.…”

Section: Glyceraldehyde 3-phosphate Dehydrogenase Inhibitionmentioning

confidence: 99%

“…The same active site cysteine involved in catalysis functions as a thiol switch, as discussed below. Interestingly, GAPDH has other enzymatic activities including S-nitrolase, ADP-ribosylase, kinase, and peroxidase [ 74 ].…”

Section: Glyceraldehyde 3-phosphate Dehydrogenase Inhibitionmentioning

confidence: 99%

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Diverting Glycolysis to Combat Oxidative Stress

Mullarky

Cantley

2015

Innovative Medicine

140

157

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Reactive oxygen species (ROS) are an intricate part of normal cellular physiology. In excess, however, ROS can damage all three major classes of macromolecules and compromise cell viability. We briefl y discuss the physiology of ROS but focus on the mechanisms cells use to preserve redox homeostasis upon oxidative stress, with particular emphasis on glycolysis. ROS inhibits multiple glycolytic enzymes, including glyceraldehyde 3-phosphate dehydrogenase, pyruvate kinase M2, and phosphofructokinase-1. Consistently, glycolytic inhibition promotes fl ux into the oxidative arm of the pentose phosphate pathway to generate NADPH. NADPH is critically important, as it provides the reducing power that fuels the protein-based antioxidant systems and recycles oxidized glutathione. The unique ability of pyruvate kinase M2 inhibition to promote serine synthesis in the context of oxidative stress is also discussed.

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Section: Glyceraldehyde 3-phosphate Dehydrogenase Inhibitionmentioning

confidence: 99%

Section: Glyceraldehyde 3-phosphate Dehydrogenase Inhibitionmentioning

confidence: 99%

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Diverting Glycolysis to Combat Oxidative Stress

Mullarky

Cantley

2015

Innovative Medicine

140

157

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“…Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a ubiquitous intracellular oxidoreductase enzyme best known for its role in glycolysis (1). Beyond this metabolic function, GAPDH participates in many other diverse cellular processes, including microtubule bundling (2), apoptosis (3)(4)(5), and transcriptional (6) and post-transcriptional gene regulation (7).…”

mentioning

confidence: 99%

“…Under basal conditions, GAPDH resides in the cytosol as an abundant (ϳ1-15 g/liter) and highly soluble homotetramer (1,8). In addition, GAPDH shuttles from the cytosol into other subcellular compartments in a regulated fashion.…”

mentioning

confidence: 99%

Oxidation of an Exposed Methionine Instigates the Aggregation of Glyceraldehyde-3-phosphate Dehydrogenase

Samson

Knaupp

Kass

et al. 2014

Journal of Biological Chemistry

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Background: GAPDH is a glycolytic enzyme that aggregates during disease. Cysteine oxidation is the putative cause of aggregation. Whether GAPDH aggregation influences disease is unknown. Results: Mutating Met-46 renders GAPDH resistant to free radical-induced aggregation. Conclusion: Methionine oxidation, rather than cysteine oxidation, is a primary event that instigates GAPDH aggregation. Significance: Mutating Met-46 in vivo should elucidate whether GAPDH aggregation causally contributes to disease.

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The possible effect of silver nanoparticles on glyceraldehyde‐3‐phosphate dehydrogenase activity and formation of amyloid‐like aggregates in MCF‐7 cell line

et al. 2020

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Silver nanoparticles (AgNPs) are widely used in medicine, however, the underlying mechanisms of their action on cellular signaling have not been completely determined, and fundamental studies are required to clarify them. We aimed to investigate AgNPs effects on glyceraldehyde‐3‐phosphate dehydrogenase (GAPDH) as both the internal control gene and the redox‐sensitive enzyme involved in apoptosis‐related pathways and the formation of amyloid aggregates. To achieve this purpose, MCF‐7 cells were treated with different concentrations (0, 3, 22, and 200 μg/ml) of AgNPs and then cell viability, generation of reactive oxygen species (ROS), induction of apoptosis, expression of GAPDH gene, the formation of amyloid aggregates, and GAPDH activity were assessed. The results indicated that treatment with AgNPs significantly reduced cell viability and increased apoptosis in a dose‐dependent manner. The ROS levels increased at lower concentrations of AgNPs (up to 22 μg/ml) and during short‐term exposure (30 min). The level of GAPDH gene expression was significantly upregulated by 1.22, 1.47, and 1.56 fold, in the concentrations of 3, 22, and 200 μg/ml, respectively. The amount of amyloid aggregates was significantly increased in a dose‐dependent manner. The results of enzyme activity showed that AgNPs were affected on the activity of GAPDH protein, however, it has fluctuated that could not be interpreted by our limited data. In conclusion, our results suggested that AgNPs could affect the GAPDH gene expression and enzyme activity, therefore the selection of GAPDH as a gene and protein internal control in the (AgNPs)‐related studies requires careful consideration. Additionally, AgNPs may cause apoptosis due to the increase in the production of amyloid aggregates.

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GAPDH: Biological Properties and Diversity

Cited by 41 publications

References 461 publications

Diverting Glycolysis to Combat Oxidative Stress

Diverting Glycolysis to Combat Oxidative Stress

Oxidation of an Exposed Methionine Instigates the Aggregation of Glyceraldehyde-3-phosphate Dehydrogenase

The possible effect of silver nanoparticles on glyceraldehyde‐3‐phosphate dehydrogenase activity and formation of amyloid‐like aggregates in MCF‐7 cell line

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