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Rat Brain Glyceraldehyde‐3‐Phosphate Dehydrogenase Interacts with the Recombinant Cytoplasmic Domain of Alzheimer's β‐Amyloid Precursor Protein
Author(s) -
Schulze Hermann,
Schuler Angelika,
Stüber Dietrich,
Döbeli Heinz,
Langen Hanno,
Huber Gerda
Publication year - 1993
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1993.tb13420.x
Subject(s) - glyceraldehyde 3 phosphate dehydrogenase , biochemistry , amyloid precursor protein , senile plaques , cytoplasm , dehydrogenase , peptide , amyloid (mycology) , fusion protein , alzheimer's disease , p3 peptide , biology , chemistry , enzyme , microbiology and biotechnology , recombinant dna , medicine , pathology , disease , botany , gene
Abundant senile plaques are a histological hallmark in the brain of Alzheimer's disease patients. Such plaques consist of, among many other constituents, aggregated βA4 amyloid peptide. This peptide is derived from an amyloid precursor protein (APP) by irregular proteolytic processing and is considered to be involved in the development of Alzheimer's disease. To study possible interactions of brain proteins with 0A4 amyloid or other fragments of APP, βA4 amyloid and βA4 amyloid extended to the C‐terminus of APP were recombinantly produced as fusion proteins termed “Amy” and “AmyC,” respectively. Using Amy and AmyC affinity chromatography, a 35‐kDa protein from rat brain was isolated that bound tightly to AmyC but not to Amy, thus indicating an interaction of the protein with the C‐terminus of APP. This 35‐kDa protein was identified as the glycolytic enzyme gIyceraldehyde‐3‐phosphate dehydrogenase (GAPDH). Binding of GAPDH to AmyC but not to Amy was confirmed by gel filtration. Although AmyC slightly reduced the V max of GAPDH, the same reduction was observed in the presence of Amy. These findings suggest that the interaction of the cytoplasmic domain of APP with GAPDH is unlikely to influence directly the rate of glycolysis but may serve another function.