Decrease of dehydrogenase activity of cerebral glyceraldehyde-3-phosphate dehydrogenase in different animal models of Alzheimer's disease

• Published in: Biochimica et biophysica acta Vol. 1770; no. 5; pp. 826 - 832
• Main Authors: Shalova, Irina N., Cechalova, Katerina, Rehakova, Zuzana, Dimitrova, Petya, Ognibene, Elisa, Caprioli, Antonio, Schmalhausen, Elena V., Muronetz, Vladimir I., Saso, Luciano
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01-05-2007
• Subjects: Alzheimer disease; Alzheimer Disease - metabolism; Alzheimer Disease - pathology; Amyloid beta-Peptides - administration & dosage; Amyloid beta-Peptides - genetics; Amyloid beta-Peptides - metabolism; Animal models; Animals; Catalytic activity; Disease Models, Animal; Enzyme Inhibitors - administration & dosage; Enzyme Inhibitors - pharmacology; Glyceraldehyde-3-phosphate dehydrogenase; Glyceraldehyde-3-Phosphate Dehydrogenases - analysis; Glyceraldehyde-3-Phosphate Dehydrogenases - genetics; Glyceraldehyde-3-Phosphate Dehydrogenases - isolation & purification; Glyceraldehyde-3-Phosphate Dehydrogenases - metabolism; Humans; Infusion Pumps; Injections, Intraventricular; Interferon-gamma - administration & dosage; Interferon-gamma - pharmacology; Lipopolysaccharides - administration & dosage; Lipopolysaccharides - toxicity; Male; Maze Learning; Mice; Mice, Transgenic; Mutation; Neprilysin - antagonists & inhibitors; Peptide Fragments - administration & dosage; Peptide Fragments - genetics; Peptide Fragments - metabolism; Rats; Rats, Inbred F344; Telencephalon - enzymology; Telencephalon - metabolism; Thiorphan - administration & dosage; Thiorphan - pharmacology; Glyceraldehyde-3-phosphate dehydrogenase; Animal models; Catalytic activity; Alzheimer disease
• ISSN: 0304-4165; 0006-3002; 1872-8006
• DOI: 10.1016/j.bbagen.2007.01.014

Recently, a relationship between glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and the β-amyloid precursor protein (βAPP) in relationship with the pathogenesis of Alzheimer's disease (AD) has been suggested. Therefore, we studied the specific activity of GAPDH in the different animal models of AD: transgenic mice (Tg2576) and rats treated with β-amyloid, or thiorphan, or lipopolysaccharides (LPS) and interferon γ (INFγ). We observed that GAPDH activity was significantly decreased in the brain samples from TG mice. The injection of β-amyloid, or thiorphan, an inhibitor of neprilysin involved in β-amyloid catabolism, in rat brains resulted in a pronounced reduction of the enzyme activity. The infusion of LPS and IFNγ, which can influence the progression of the AD, significantly reduced the enzyme activity.