Question

Please explain briefly about how the protein folding is wrong for the Parkinson's disease and give a potential approach to treat it.

Thanks

Answer 1

Ans.

In the cell, protein folding occurs by the oligomers formation and aggregates of proteins. Inside the cell, aggregated proteins leads to the formation of an amyloid?like structure, which causes degenerative disorders and leads to cell death. Common diseases which occurs by the accumulation of misfolded proteins are Parkinson’s disease and Alzheimer's disease and both the diseases are also called as amyloid diseases. In Parkinson disease by the mutation in protein ??synuclein synthesis, folding and degradation is effected and results in the accumulation of misfolded proteins and forms aggregates, and abnormal tendency of proteins to aggregation results into misfolding. Aggregation are mainly caused by protein and by prion self-catalytic conformational conversion, by mutations which makes the protein unstable. By the pathological increase in the intracellular concentrations imbalances protein and leads to duplications (mutations) of the amyloidogenic gene changes the protein's amino acid sequence. Autophagy inhibition also promotes the amyloid aggregation which increases oxidative stress, mitochondrial dysfunction, alteration of cytoplasmic membrane permeability, and abnormal calcium concentration in the Parkinson disease and other types of amyloid diseases.

Stress induced proteins such as molecular chaperones are effective in preventing the misfolding of protein in many of the neurodegenerative diseases such as Parkinson disease. Increase in chaperone expression suppresses the neurotoxicity caused by protein misfolding and is used as a therapeutic agents.