Literature DB >> 8512563

Brain protein kinase PK40erk converts TAU into a PHF-like form as found in Alzheimer's disease.

H M Roder1, P A Eden, V M Ingram.   

Abstract

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.

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Year:  1993        PMID： 8512563     DOI： 10.1006/bbrc.1993.1672

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN： 0006-291X            Impact factor:   3.575


  28 in total

1.  Compromised mitochondrial function leads to increased cytosolic calcium and to activation of MAP kinases.

Authors:  Y Luo; J D Bond; V M Ingram
Journal:  Proc Natl Acad Sci U S A       Date:  1997-09-02       Impact factor: 11.205

2.  Non-proline-dependent protein kinases phosphorylate several sites found in tau from Alzheimer disease brain.

Authors:  T J Singh; T Zaidi; I Grundke-Iqbal; K Iqbal
Journal:  Mol Cell Biochem       Date:  1996-01-26       Impact factor: 3.396

Review 3.  Regulated phosphorylation and dephosphorylation of tau protein: effects on microtubule interaction, intracellular trafficking and neurodegeneration.

Authors:  M L Billingsley; R L Kincaid
Journal:  Biochem J       Date:  1997-05-01       Impact factor: 3.857

4.  The GRK2 Overexpression Is a Primary Hallmark of Mitochondrial Lesions during Early Alzheimer Disease.

Authors:  Mark E Obrenovich; Hector H Palacios; Eldar Gasimov; Jerzy Leszek; Gjumrakch Aliev
Journal:  Cardiovasc Psychiatry Neurol       Date:  2010-03-03

5.  Comparison of the phosphorylation of microtubule-associated protein tau by non-proline dependent protein kinases.

Authors:  T J Singh; I Grundke-Iqbal; B McDonald; K Iqbal
Journal:  Mol Cell Biochem       Date:  1994-02-23       Impact factor: 3.396

6.  Okadaic-acid-induced inhibition of protein phosphatase 2A produces activation of mitogen-activated protein kinases ERK1/2, MEK1/2, and p70 S6, similar to that in Alzheimer's disease.

Authors:  Jin-Jing Pei; Cheng-Xin Gong; Wen-Lin An; Bengt Winblad; Richard F Cowburn; Inge Grundke-Iqbal; Khalid Iqbal
Journal:  Am J Pathol       Date:  2003-09       Impact factor: 4.307

Review 7.  Mechanisms of tau-induced neurodegeneration.

Authors:  Khalid Iqbal; Fei Liu; Cheng-Xin Gong; Alejandra Del C Alonso; Inge Grundke-Iqbal
Journal:  Acta Neuropathol       Date:  2009-01-30       Impact factor: 17.088

8.  Dissociation of tau toxicity and phosphorylation: role of GSK-3beta, MARK and Cdk5 in a Drosophila model.

Authors:  Shreyasi Chatterjee; Tzu-Kang Sang; George M Lawless; George R Jackson
Journal:  Hum Mol Genet       Date:  2008-10-17       Impact factor: 6.150

Review 9.  Chaperone signalling complexes in Alzheimer's disease.

Authors:  John Koren; Umesh K Jinwal; Daniel C Lee; Jeffrey R Jones; Cody L Shults; Amelia G Johnson; Laura J Anderson; Chad A Dickey
Journal:  J Cell Mol Med       Date:  2009-04       Impact factor: 5.310

Review 10.  Insights into cerebrovascular complications and Alzheimer disease through the selective loss of GRK2 regulation.

Authors:  Mark E Obrenovich; Ludis A Morales; Celia J Cobb; Justin C Shenk; Gina M Méndez; Kathryn Fischbach; Mark A Smith; Eldar K Qasimov; George Perry; Gjumrakch Aliev
Journal:  J Cell Mol Med       Date:  2008-10-06       Impact factor: 5.310
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