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Activation of m1 muscarinic acetylcholine receptor regulates τ phosphorylation in transfected PC12 cells
Year:
1996
Source of publication :
Journal of Neurochemistry
Authors :
Sadot, Einat
;
.
Volume :
66
Co-Authors:
Sadot, E., Department of Neurobiology, Weizmann Institute of Science, Rehovot, Israel
Gurwitz, D., Natl. Lab. Genet. Israeli P., Tel Aviv University, Tel Aviv, Israel
Barg, J., Department of Neurobiology, Weizmann Institute of Science, Rehovot, Israel
Behar, L., Department of Neurobiology, Weizmann Institute of Science, Rehovot, Israel
Ginzburg, I., Department of Neurobiology, Weizmann Institute of Science, Rehovot, Israel, Department of Neurobiology, Weizmann Institute of Science, 76100 Rehovot, Israel
Fisher, A., Israel Inst. for Biological Research, Ness Ziona, Israel
Facilitators :
From page:
877
To page:
880
(
Total pages:
4
)
Abstract:
Hyperphosphorylated τ proteins are the principal fibrous component of the neurofibrillary tangle pathology in Alzheimer's disease. The possibility that τ phosphorylation is controlled by cell surface neurotransmitter receptors was examined in PC12 cells transfected with the gene for the rat m1 muscarinic acetylcholine receptor. Stimulation of m1 receptor in these cells with two acetylcholine agonists, carbachol and AF102B, decreased τ phosphorylation, as indicated by specific τ monoclonal antibodies that recognize phosphorylation-dependent epitopes and by alkaline phosphatase treatment. The muscarinic effect was both time and dose dependent. In addition, a synergistic effect on τ phosphorylation was found between treatments with muscarinic agonists and nerve growth factor. These studies provide the first evidence for a link between the cholinergic signal transduction system and the neuronal cytoskeleton that can be mediated by regulated phosphorylation of τ microtubule-associated protein.
Note:
Related Files :
Animal
animal cell
Animals
cell strain
drug effect
Genetics
metabolism
PC12 Cells
Quinuclidines
τ protein
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More details
DOI :
Article number:
Affiliations:
Database:
Scopus
Publication Type:
article
;
.
Language:
English
Editors' remarks:
ID:
20050
Last updated date:
02/03/2022 17:27
Creation date:
16/04/2018 23:33
Scientific Publication
Activation of m1 muscarinic acetylcholine receptor regulates τ phosphorylation in transfected PC12 cells
66
Sadot, E., Department of Neurobiology, Weizmann Institute of Science, Rehovot, Israel
Gurwitz, D., Natl. Lab. Genet. Israeli P., Tel Aviv University, Tel Aviv, Israel
Barg, J., Department of Neurobiology, Weizmann Institute of Science, Rehovot, Israel
Behar, L., Department of Neurobiology, Weizmann Institute of Science, Rehovot, Israel
Ginzburg, I., Department of Neurobiology, Weizmann Institute of Science, Rehovot, Israel, Department of Neurobiology, Weizmann Institute of Science, 76100 Rehovot, Israel
Fisher, A., Israel Inst. for Biological Research, Ness Ziona, Israel
Activation of m1 muscarinic acetylcholine receptor regulates τ phosphorylation in transfected PC12 cells
Hyperphosphorylated τ proteins are the principal fibrous component of the neurofibrillary tangle pathology in Alzheimer's disease. The possibility that τ phosphorylation is controlled by cell surface neurotransmitter receptors was examined in PC12 cells transfected with the gene for the rat m1 muscarinic acetylcholine receptor. Stimulation of m1 receptor in these cells with two acetylcholine agonists, carbachol and AF102B, decreased τ phosphorylation, as indicated by specific τ monoclonal antibodies that recognize phosphorylation-dependent epitopes and by alkaline phosphatase treatment. The muscarinic effect was both time and dose dependent. In addition, a synergistic effect on τ phosphorylation was found between treatments with muscarinic agonists and nerve growth factor. These studies provide the first evidence for a link between the cholinergic signal transduction system and the neuronal cytoskeleton that can be mediated by regulated phosphorylation of τ microtubule-associated protein.
Scientific Publication
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