Abstract
Hyperphosphorylated tau is a cardinal feature of Alzheimers disease (AD) pathology. The deregulation of kinases that phosphorylate tau can alter normal tau-related processes, including microtubule dynamics, growth cones, and axonal transport, and induce tau aggregation in paired helical filaments. Here we discuss the possible roles of the Abl family of tyrosine kinases, which are essential regulators of cytoskeleton cellular signaling cascades, in AD tau pathology and how the physiological roles of Abl kinases could be connected with the cytoskeletal alterations induced by Aβ aggregates and AD progression.
Keywords: Alzheimer, tau, phosphorylation, c-Abl, Aging, dementia, genetic epidemiology, metabolism, obesity, twins, predisposing effect, genetic allele, memory impairment, BMI, MET, TICS, TELE
Current Alzheimer Research
Title: C-Abl Tyrosine Kinase Signaling: A New Player in AD Tau Pathology
Volume: 8 Issue: 6
Author(s): L. D. Estrada, S. M. Zanlungo and A. R. Alvarez
Affiliation:
Keywords: Alzheimer, tau, phosphorylation, c-Abl, Aging, dementia, genetic epidemiology, metabolism, obesity, twins, predisposing effect, genetic allele, memory impairment, BMI, MET, TICS, TELE
Abstract: Hyperphosphorylated tau is a cardinal feature of Alzheimers disease (AD) pathology. The deregulation of kinases that phosphorylate tau can alter normal tau-related processes, including microtubule dynamics, growth cones, and axonal transport, and induce tau aggregation in paired helical filaments. Here we discuss the possible roles of the Abl family of tyrosine kinases, which are essential regulators of cytoskeleton cellular signaling cascades, in AD tau pathology and how the physiological roles of Abl kinases could be connected with the cytoskeletal alterations induced by Aβ aggregates and AD progression.
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Cite this article as:
D. Estrada L., M. Zanlungo S. and R. Alvarez A., C-Abl Tyrosine Kinase Signaling: A New Player in AD Tau Pathology, Current Alzheimer Research 2011; 8 (6) . https://dx.doi.org/10.2174/156720511796717249
DOI https://dx.doi.org/10.2174/156720511796717249 |
Print ISSN 1567-2050 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5828 |
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