title: Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and Alzheimer's disease.
abstract: Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a ubiquitous enzyme that catalyzes the sixth step of glycolysis and thus, serves to break down glucose for energy production. Beyond the traditional aerobic metabolism of glucose, recent studies have highlighted additional roles played by GAPDH in non-metabolic processes, such as control of gene expression and redox post-translational modifications. Neuroproteomics have revealed high affinity interactions between GAPDH and Alzheimer's disease-associated proteins, including the β-amyloid, β-amyloid precursor protein and tau. This neuronal protein interaction may lead to impairment of the GAPDH glycolytic function in Alzheimer's disease and may be a forerunner of its participation in apoptosis. The present review examines the crucial implication of GAPDH in neurodegenerative processes and clarifies its role in apoptotic cell death.
authors.affiliation: Laboratory of Medical Genetics and Molecular Pathology, Faculty of Medicine and Pharmacy, Hassan II University, Casablanca, Morocco; Laboratory of Physiology and Molecular Genetics, Faculty of Sciences Aïn Chock, Hassan II University, Casablanca, Morocco. Electronic address: elkadmiri1979@gmail.com.
authors.forename: N
authors.initials: N
authors.lastname: El Kadmiri
authors.affiliation: Laboratory of Medical Genetics and Molecular Pathology, Faculty of Medicine and Pharmacy, Hassan II University, Casablanca, Morocco; Department of Neurology CHU IBN ROCHD, Casablanca, Morocco.
authors.forename: I
authors.initials: I
authors.lastname: Slassi
authors.affiliation: Laboratory of Medical Genetics and Molecular Pathology, Faculty of Medicine and Pharmacy, Hassan II University, Casablanca, Morocco; Department of Neurology CHU IBN ROCHD, Casablanca, Morocco.
authors.forename: B
authors.initials: B
authors.lastname: El Moutawakil
authors.affiliation: Laboratory of Medical Genetics and Molecular Pathology, Faculty of Medicine and Pharmacy, Hassan II University, Casablanca, Morocco.
authors.forename: S
authors.initials: S
authors.lastname: Nadifi
authors.affiliation: Department of Medicine, Université de Montréal, Montréal, Québec, H3C 3J7, Canada.
authors.forename: A
authors.initials: A
authors.lastname: Tadevosyan
authors.affiliation: Laboratory of Thrombosis and Hemostasis, Montreal Heart Institute, Montreal, Quebec, H1T 1C8, Canada.
authors.forename: A
authors.initials: A
authors.lastname: Hachem
authors.affiliation: Laboratory of Physiology and Molecular Genetics, Faculty of Sciences Aïn Chock, Hassan II University, Casablanca, Morocco.
authors.forename: A
authors.initials: A
authors.lastname: Soukri
mesh_terms: D000544:Alzheimer Disease / Q000209:etiology*; D016564:Amyloid beta-Protein Precursor / Q000378:metabolism; D000818:Animals; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000737:chemistry / Q000502:physiology*; D006801:Humans; D066329:Protein Aggregates / Q000502:physiology; D011487:Protein Conformation; D013329:Structure-Activity Relationship; D016875:tau Proteins / Q000378:metabolism
chemical_list: D016564:Amyloid beta-Protein Precursor; C054369:MAPT protein, human; D066329:Protein Aggregates; D016875:tau Proteins; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases
keywords: Alzheimer's disease; Enchevêtrements neurofibrillaires; GAPDH; La maladie d’Alzheimer; L’agrégation de la β-amyloïde; Neurofibrillary tangles; β-amyloid aggregation