BRAIN PROTEIN-KINASE PK40(ERK) CONVERTS TAU INTO A PHF-LIKE FORM AS FOUND IN ALZHEIMERS-DISEASE

被引:116
作者
RODER, HM
EDEN, PA
INGRAM, VM
机构
[1] MIT,DEPT BIOL,CAMBRIDGE,MA 02139
[2] MILES INC,W HAVEN,CT 06516
[3] BIOMEASURES INC,MILFORD,MA 01757
关键词
D O I
10.1006/bbrc.1993.1672
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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 hyper-phosphorylated by PK40erk to produce the electrophoretic mobility shifts and certain iminunochemical properties characteristic of PHF-TAU isolated from Alzheimer′s disease brain tissue. PK40erk may play a crucial role in the etiology of this disease. © 1993 Academic Press. All rights reserved.
引用
收藏
页码:639 / 647
页数:9
相关论文
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