脑蛋白激酶PK40erk可将TAU转化为阿尔茨海默病中发现的类似PHF的形式。
Brain protein kinase PK40erk converts TAU into a PHF-like form as found in Alzheimer's disease.
作者信息
Roder H M, Eden P A, Ingram V M
机构信息
Department of Biology, Massachusetts Institute of Technology, Cambridge 02139.
出版信息
Biochem Biophys Res Commun. 1993 Jun 15;193(2):639-47. doi: 10.1006/bbrc.1993.1672.
The novel protein kinase PK40 (1) was characterized by its ability to phosphorylate Lys-Ser-Pro sites in neurofilament and TAU proteins. PK40 is now recognized to be a member of the family of External-stimulus Regulated Kinases (ERKs) by its reactivity with ERK-specific antibodies and will therefore be called PK40erk. Bovine TAU or recombinant human TAU proteins can be hyperphosphorylated by PK40erk to produce the electrophoretic mobility shifts and certain immunochemical properties characteristic of PHF-TAU isolated from Alzheimer's disease brain tissue. PK40erk may play a crucial role in the etiology of this disease.
新型蛋白激酶PK40(1)的特征在于其能够磷酸化神经丝和TAU蛋白中的赖氨酸 - 丝氨酸 - 脯氨酸位点。PK40现在通过其与ERK特异性抗体的反应性被认为是外部刺激调节激酶(ERK)家族的成员，因此将被称为PK40erk。牛TAU或重组人TAU蛋白可被PK40erk过度磷酸化，以产生从阿尔茨海默病脑组织中分离出的PHF-TAU的电泳迁移率变化和某些免疫化学特性。PK40erk可能在这种疾病的病因学中起关键作用。
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