Protein levels of glycogen synthase 3 kinase are normal in progressive supranuclear palsy

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• 作者：Borghi ; Roberta ; Piccini ; Alessandra ; Delacourte ; Andrè ; Strocchi ; Paola ; Zaccheo ; Damiano ; et. al.
• 关键词：Progressive supranuclear palsy ; GSK3 ; Tau phosphorylation
• 刊名：Neuroscience Letters
• 出版年：2004
• 出版时间：August 5, 2004
• 年：2004
• 卷：366
• 期：1
• 页码：67-70
• 全文大小：142 K

文摘

Progressive supranuclear palsy (PSP) is a neurodegenerative disorder characterized by pure neurofibrillary tau pathology involving mainly basal ganglia and brain stem nuclei. One of the kinases involved in tau phosphorylation is glycogen synthase 3 kinase (GSK3). In mammals GSK3 is present in two isoforms, α and β regulated by phosphorylation: phosphorylation of Ser9 in GSK3β or Ser21 in GSK3α leads to inactivation while phosphorylation of Tyr216 in GSK3β or Tyr279 in GSK3α leads to activation. We analyzed the protein levels of GSK3α/β and of the phosphorylated forms GSK3β S⁹, GSK3β Y²¹⁶, GSK3α Y²⁷⁹ in brain tissues of subjects with PSP. The analysis failed to show significant differences of all GSK3 isoforms in PSP in comparison to age-matched control cases. This negative result argues against the role of GSK3 in the pathogenesis of PSP.