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While impediments of cellular respiration and mitochondrial pathology have been thoroughly investigated, less is known about central carbon metabolism, its role in Parkinson's disease and interconnection with α-synuclein aggregation. Elevation in glyceraldehyde-3-phosphate, substrate of glyceraldehyde-3-phosphatedehydrogenase (GAPDH), was shown in paraquat-induced model of PD, which may indicate important role of GAPDH in pathology. Our laboratory has previously shown in vitro that human GAPDH is inactivated by monomeric α-synuclein, which may play an important role in enzyme regulation and changes in glycolytic rate in synucleinopathies. We further investigated interaction of hGAPDH with α-synuclein oligomers and found that they were more potent inactivators of GAPDH than monomeric protein.