نتایج جستجو برای: tau hyperphosphorylation

تعداد نتایج: 21929  

Journal: :Human molecular genetics 2015
Fadi Mikhail Noel Calingasan Luca Parolari Aarthi Subramanian Lichuan Yang M Flint Beal

LRRK2 (leucine-rich repeat kinase) mutations constitute the most common cause of familial Parkinson's disease (PD). Microtubule-associated protein tau mutations cause a group of neurodegenerative diseases termed tauopathies. Genome-wide association studies show that, after α-synuclein, polymorphisms in the tau gene have the second strongest genetic association with PD. In a proportion of PD pat...

Journal: :The European journal of neuroscience 2005
Evan Elliott Roee Atlas Aya Lange Irith Ginzburg

The microtubule-associated protein tau is essential for microtubule stabilization in neuronal axons. Hyperphosphorylation and intracellular fibrillar formation of tau protein is a pathology found in Alzheimer's disease (AD) brains, and in a variety of neurodegenerative disorders referred to as 'taupathies'. In the present study, we investigated how brain-derived neurotrophic factor (BDNF), an e...

Journal: :Brain : a journal of neurology 2006
Jaya Padmanabhan Monique Levy Dennis W Dickson Huntington Potter

Amyloid plaques and neurofibrillary tangles are key pathological features of Alzheimer's disease. Alzheimer's disease pathology is also characterized by neuroinflammation and neuronal degeneration, with the proteins associated with inflammatory responses being found in tight association with the plaques. One such protein is the serine protease inhibitor alpha-1-antichymotrypsin (ACT). ACT has b...

2015
Tomohiro Umeda Hiroshi Eguchi Yuichi Kunori Yoichi Matsumoto Taizo Taniguchi Hiroshi Mori Takami Tomiyama

OBJECTIVE Cellular inclusions of hyperphosphorylated tau are a hallmark of tauopathies, which are neurodegenerative disorders that include Alzheimer's disease (AD). Active and passive immunization against hyperphosphorylated tau has been shown to attenuate phenotypes in model mice. We developed new monoclonal antibodies to hyperphosphorylated tau and sought high therapeutic efficacy for future ...

2012
Jesús Avila Gonzalo León-Espinosa Esther García Vega García-Escudero Félix Hernández Javier DeFelipe

Almost a 20% of the residues of tau protein are phosphorylatable amino acids: serine, threonine, and tyrosine. In this paper we comment on the consequences for tau of being a phosphoprotein. We will focus on serine/threonine phosphorylation. It will be discussed that, depending on the modified residue in tau molecule, phosphorylation could be protective, in processes like hibernation, or toxic ...

2012
Tohru Matsuki Mariam Zaka Rita Guerreiro Marcel P. van der Brug Jonathan A. Cooper Mark R. Cookson John A. Hardy Brian W. Howell

Hyperphosphorylation of the microtubule binding protein Tau is a feature of a number of neurodegenerative diseases, including Alzheimer's disease. Tau is hyperphosphorylated in the hippocampus of dab1-null mice in a strain-dependent manner; however, it has not been clear if the Tau phosphorylation phenotype is a secondary effect of the morbidity of these mutants. The dab1 gene encodes a docking...

2017
Zhihui Gai Donghong Su Yawen Wang Wenlong Li Bo Cui Kang Li Xiaojun She Rui Wang

BACKGROUND Chronic noise exposure has been associated with tau hyperphosphorylation and Alzheimer's disease (AD)-like pathological changes, but the underlying mechanism is unknown. In this study, we explored the effects of long-term noise exposure on the corticotropin-releasing factor (CRF) system in the hippocampus and its role in noise-induced tau phosphorylation. METHODS Sixty-four rats we...

Journal: :The Journal of biological chemistry 2007
Björn Kuhla Cathleen Haase Katharina Flach Hans-Joachim Lüth Thomas Arendt Gerald Münch

Accumulation of hyperphosphorylated Tau protein as paired helical filaments in pyramidal neurons is a major hallmark of Alzheimer disease. Besides hyperphosphorylation, other modifications of the Tau protein, such as cross-linking, are likely to contribute to the characteristic features of paired helical filaments, including their insolubility and resistance against proteolytic degradation. In ...

Journal: :Neurobiology of Aging 2016
Jonathan Gilley Kunie Ando Anjan Seereeram Teresa Rodríguez-Martín Amy M. Pooler Laura Sturdee Brian H. Anderton Jean-Pierre Brion Diane P. Hanger Michael P. Coleman

Hyperphosphorylation and fibrillar aggregation of the microtubule-associated protein tau are key features of Alzheimer's disease and other tauopathies. To investigate the involvement of tau phosphorylation in the pathological process, we generated a pair of complementary phosphomutant tau knockin mouse lines. One exclusively expresses phosphomimetic tau with 18 glutamate substitutions at serine...

Journal: :Biochimica et biophysica acta 2003
Tony Lefebvre Stéphanie Ferreira Laetitia Dupont-Wallois Thierry Bussière Marie-Joëlle Dupire André Delacourte Jean-Claude Michalski Marie-Laure Caillet-Boudin

Both phosphorylation and O-GlcNAc glycosylation posttranslationally modify microtubule-associated Tau proteins. Whereas the hyperphosphorylation of these proteins that occurs in Alzheimer's disease is well characterized, little is known about the O-GlcNAc glycosylation. The present study demonstrates that a balance exists between phosphorylation and O-GlcNAc glycosylation of Tau proteins, and f...

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