Phosphorylation of tau protein to sites found in Alzheimer's disease brain is catalyzed by Ca2+/calmodulin-dependent protein kinase II as demonstrated tandem mass spectrometry

• Published in: Neuroscience letters Vol. 353; no. 3; pp. 185 - 188
• Main Authors: YOSHIMURA, Yoshiyuki, ICHINOSE, Tatsuya, YAMAUCHI, Takashi
• Format: Journal Article
• Language: English
• Published: Shannon Elsevier 26.12.2003
• Subjects: Alzheimer Disease - metabolism; Biological and medical sciences; Brain - metabolism; Brain Chemistry; Calcium-Calmodulin-Dependent Protein Kinase Type 2; Calcium-Calmodulin-Dependent Protein Kinases - metabolism; Catalysis; Degenerative and inherited degenerative diseases of the nervous system. Leukodystrophies. Prion diseases; Gas Chromatography-Mass Spectrometry - methods; Humans; Medical sciences; Neurology; Phosphorylation; Recombinant Proteins - metabolism; Serine - metabolism; Spectrometry, Mass, Electrospray Ionization; tau Proteins - metabolism; Threonine - metabolism; Human; Nervous system diseases; Phosphorylation; calmodulin-dependent protein kinase; Enzyme; Alzheimer disease; Transferases; Central nervous system; Cerebral disorder; Encephalon; Tau protein; Mass spectrometry MS/MS; Central nervous system disease; Degenerative disease; Ca

Neuronal Ca2+/calmodulin-dependent protein kinase II (CaMKII) is one of the most abundant protein kinases in the brain, and phosphorylates a broad range of substrate proteins. The phosphorylation of microtubule tau by CaMKII was investigated using tandem mass spectrometry (MS/MS). Recombinant human...