NDLI: Regulation of Phosphorylation of tau by Protein Kinases in Rat Brain

Please wait, while we are loading the content...

Paraquat-induced Oxidative Stress in Drosophila melanogaster: Effects of Melatonin, Glutathione, Serotonin, Minocycline, Lipoic Acid and Ascorbic Acid

Calpain-induced Proteolysis After Transient Global Cerebral Ischemia and Ischemic Tolerance in a Rat Model

Pontine and Cerebellar Norepinephrine Content in Adult Rats Recovering from Focal Cortical Injury

Brain Catecholamine Alterations and Pathological Features with Aging in Parkinson Disease Model Rat Induced by Japanese Encephalitis Virus

Pharmacological Activity of Ruthenium Complexes trans-[RuCl$_{2}$(L)$_{4}$] (L = Nicotinic or i-Nicotinic acid) on Anxiety and Memory in Rats

Nuclear Ca$^{++}$-influx, Ca$^{++}$/Calmodulin-Dependent Protein Kinase IV Activity and CREB Protein Phosphorylation during Post-Hypoxic Reoxygenation in Neuronal Nuclei of Newborn Piglets: The Role of Nitric Oxide

Regulation of Phosphorylation of tau by Protein Kinases in Rat Brain

Nerve Growth Factor Differentially Affects Spatial and Recognition Memory in Aged Rats

Carbon Disulfide-Induced Alterations of Neurofilaments and Calpains Content in Rat Spinal Cord

Neurochemical Research : Volume 31, Issue 11, November 2006

Neurochemical Research : Volume 31, Issue 10, October 2006

Neurochemical Research : Volume 31, Issue 9, September 2006

Neurochemical Research : Volume 31, Issue 8, August 2006

Neurochemical Research : Volume 31, Issue 7, July 2006

Neurochemical Research : Volume 31, Issue 6, June 2006

Neurochemical Research : Volume 31, Issue 5, May 2006

Neurochemical Research : Volume 31, Issue 4, April 2006

Neurochemical Research : Volume 31, Issue 3, March 2006

Neurochemical Research : Volume 31, Issue 2, February 2006

Neurochemical Research : Volume 31, Issue 1, January 2006

Neurochemical Research : Volume 30

Neurochemical Research : Volume 29

Neurochemical Research : Volume 28

Neurochemical Research : Volume 27

Neurochemical Research : Volume 26

Neurochemical Research : Volume 25

Neurochemical Research : Volume 24

Neurochemical Research : Volume 23

Neurochemical Research : Volume 22

Regulation of Phosphorylation of tau by Protein Kinases in Rat Brain

Content Provider	Springer Nature Link
Author	Sengupta, Amitabha Grundke Iqbal, Inge Iqbal, Khalid
Copyright Year	2006
Abstract	Microtubule associated protein tau is abnormally hyperphosphorylated in Alzheimer disease (AD) brain. To investigate the role of protein kinases involved in this lesion, metabolically active slices made from brains of adult rats were treated with or without various specific kinase activators in oxygenated artificial cerebrospinal fluid. The basal kinase activities of protein kinase-A (PKA), CaM Kinase II and GSK-3 were stimulated more than two-fold by isoproterenol, bradykinin and wortmannin, respectively. We found that cdk5 activity was co-stimulated with PKA by isoproterenol. Sequential activation of PKA (+cdk5), CaM Kinase II and GSK-3 produced hyperphosphorylation of tau at Ser-198/Ser-199/Ser-202, Ser-214, Thr-231/Ser-235, Ser-262, Ser-396/Ser-404 and Ser-422 sites. Like AD P-tau, the P-tau from brain slices bound to normal tau and its binding to tubulin was inhibited. These studies suggest that PKA, cdk5, CaM Kinase II and GSK-3 are involved in the regulation of phosphorylation of tau and that AD-type phosphorylation of tau is probably a product of the synergistic action of two or more of these kinases.
Starting Page	1473
Ending Page	1480
Page Count	8
File Format	PDF
ISSN	03643190
Journal	Neurochemical Research
Volume Number	31
Issue Number	12
e-ISSN	15736903
Language	English
Publisher	Kluwer Academic Publishers-Plenum Publishers
Publisher Date	2006-11-21
Publisher Place	New York
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Alzheimer disease tau Neurofibrillary degeneration tau hyperphosphorylation Neurology Biochemistry Neurosciences
Content Type	Text
Resource Type	Article
Subject	Medicine Biochemistry Cellular and Molecular Neuroscience

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

Estradiol Attenuates Tau Hyperphosphorylation Induced by Upregulation of Protein Kinase-A

Increased Expression of p130 in Alzheimer Disease

Phosphorylation sensitizes microtubule-associated protein τ to Al$^{3+}$-induced aggregation

RNA Interference Silencing of Glycogen Synthase Kinase 3β Inhibites Tau Phosphorylation in Mice with Alzheimer Disease

Conditional inactivation of Akt three isoforms causes tau hyperphosphorylation in the brain

Alzheimer neurofibrillary degeneration : Therapeutic targets and high-throughput assays

High copy wildtype human 1N4R tau expression promotes early pathological tauopathy accompanied by cognitive deficits without progressive neurofibrillary degeneration

Tau hyperphosphorylation induces apoptotic escape and triggers neurodegeneration in Alzheimer's disease.

Cytosine β-D-arabinofuranoside used as a Paradigm Modifier to Increase Production of Tau Aggregates in a Cellular Model of Tauopathy

Regulation of Phosphorylation of tau by Protein Kinases in Rat Brain

Similar Documents

Estradiol Attenuates Tau Hyperphosphorylation Induced by Upregulation of Protein Kinase-A

Increased Expression of p130 in Alzheimer Disease

Phosphorylation sensitizes microtubule-associated protein τ to Al$^{3+}$-induced aggregation

RNA Interference Silencing of Glycogen Synthase Kinase 3β Inhibites Tau Phosphorylation in Mice with Alzheimer Disease

Conditional inactivation of Akt three isoforms causes tau hyperphosphorylation in the brain

Alzheimer neurofibrillary degeneration : Therapeutic targets and high-throughput assays

High copy wildtype human 1N4R tau expression promotes early pathological tauopathy accompanied by cognitive deficits without progressive neurofibrillary degeneration

Tau hyperphosphorylation induces apoptotic escape and triggers neurodegeneration in Alzheimer's disease.

Cytosine β-D-arabinofuranoside used as a Paradigm Modifier to Increase Production of Tau Aggregates in a Cellular Model of Tauopathy

Regulation of Phosphorylation of tau by Protein Kinases in Rat Brain