Cytotoxicity of α-synuclein amyloid fibrils generated with phage chaperonin OBP.

Chaperonins are known to be important players in the conversion of amyloidogenic proteins into amyloid precursors in a variety of neurodegenerative diseases. However, the mechanisms of their action is still poorly understood. In this work, we used a single-ring chaperonin of the bacteriophage OBP, which functions in an ATP-dependent manner but has a simpler structure than other chaperonins.

Enzyme-induced degradation of natural and artificial linear polyanions.

Synthetic and natural polymers are widely used for constructing drug delivery systems. Biocompatibility, water solubility and non-toxicity make polymers a convenient matrix for encapsulation, delivery and release of bioactive compounds. Coupling of a drug with a biodegraded polymer matrix is a promising way for a controlled drug delivery.

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.

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.

Modulation of TRPV1 and TRPA1 Channels Function by Sea Anemones' Peptides Enhances the Viability of SH-SY5Y Cell Model of Parkinson's Disease.

Cellular dysfunction during Parkinson's disease leads to neuroinflammation in various brain regions, inducing neuronal death and contributing to the progression of the disease. Different ion channels may influence the process of neurodegeneration. The peptides Ms 9a-1 and APHC3 can modulate the function of TRPA1 and TRPV1 channels, and we evaluated their cytoprotective effects in differentiated to dopaminergic neuron-like SH-SY5Y cells.