Binding of glyceraldehyde-3-phosphate dehydrogenase to G-actin promotes the transnitrosylation reaction.

In this study, we investigated formation of the complex between glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and actin and the possibility of nitrosyl group transfer between GAPDH and actin. A complex of GAPDH with beta-actin was isolated from lysates of HEK293T cells using immunoprecipitation with antibodies against GAPDH or against beta-actin. The treatment of the cells with HO or NO donor did not affect the formation of the complex.

Predicting citations in Dutch case law with natural language processing.

With the ever-growing accessibility of case law online, it has become challenging to manually identify case law relevant to one's legal issue. In the Netherlands, the planned increase in the online publication of case law is expected to exacerbate this challenge. In this paper, we tried to predict whether court decisions are cited by other courts or not after being published, thus in a way distinguishing between more and less authoritative cases.

Glyceraldehyde-3-phosphate dehydrogenase is involved in the pathogenesis of Alzheimer's disease.

One of important characteristics of Alzheimer's disease is a persistent oxidative/nitrosative stress caused by pro-oxidant properties of amyloid-beta peptide (Aβ) and chronic inflammation in the brain. Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is easily oxidized under oxidative stress. Numerous data indicate that oxidative modifications of GAPDH in vitro and in cell cultures stimulate GAPDH denaturation and aggregation, and the catalytic cysteine residue Cys152 is important for these processes.

S-nitrosylation and S-glutathionylation of GAPDH: Similarities, differences, and relationships.

The aim of this work was to compare the effect of reversible post-translational modifications, S-nitrosylation and S-glutathionylation, on the properties of glyceraldehyde-3-phosphate dehydrogenase (GAPDH), and to reveal the mechanism of the relationship between these modifications. Comparison of S-nitrosylated and S-glutathionylated GAPDH showed that both modifications inactivate the enzyme and change its spatial structure, decreasing the thermal stability of the protein and increasing its sensitivity to trypsin cleavage. Both modifications are reversible in the presence of dithiothreitol, however, in the presence of reduced glutathione and glutaredoxin 1, the reactivation of S-glutathionylated GAPDH is much slower (10% in 2 h) compared to S-nitrosylated GAPDH (60% in 10 min).

Proteomic Profiling of Mouse Brain Pyruvate Kinase Binding Proteins: A Hint for Moonlighting Functions of PKM1?

Affinity-based proteomic profiling is widely used for the identification of proteins involved in the formation of various interactomes. Since protein-protein interactions (PPIs) reflect the role of particular proteins in the cell, identification of interaction partners for a protein of interest can reveal its function. The latter is especially important for the characterization of multifunctional proteins, which can play different roles in the cell.