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Mir193a expression pattern in lymph, spleen and brain samples and cell cultures of experimental autoimmune encephalomyelitis induced mice
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Neurological Disorders

ISSN: 2329-6895

Open Access

Mir193a expression pattern in lymph, spleen and brain samples and cell cultures of experimental autoimmune encephalomyelitis induced mice


2nd International Conference on Neuroimmunology & Therapeutics

December 01-02, 2016 Atlanta, USA

Saba Gharibi, Mohammad Bagher Mahmoudi, Bahram Moghimi, Mohammad Taher Tahoori, Ensieh Shahvazian and Ehsan Farashahi Yazd

Shahid Sadoughi University of Medical Sciences and Health Services, Iran
ROJETechnologies, Iran

Posters & Accepted Abstracts: J Neurol Disord

Abstract :

Tau is naturally a neuron-specific soluble protein that promotes microtubule assembly and stabilization. When pathologically modified, tau dissociates from microtubules and becomes insoluble aggregates called neurofibrillary tangles (NFTs). The NFTs formation is one of the main significant pathological signatures in Alzheimer�s disease (AD) and multiple neurodegenerative disorders classified as tauopathies. NFTs are accumulated in axons and dendrites, thereby causing degeneration of tangle-bearing neurons. In addition, tau oligomers propagate in neurons and acting as a seed for native tau aggregation. Accordingly, great efforts have been made to investigate the mechanism of tau aggregation and to identify the pathogenic tau species. Diverse intracellular modifications make soluble tau to be a susceptible substrate for the soluble tau oligomers and insoluble filamentous aggregates. Due to the implications of tau pathology in many neuro-degenerative disorders, preventing the pathological tau aggregation become an important therapeutic strategy to halt the disease. However, progress has been slow due to the lack of understating tau aggregation mechanism. Tau aggregation is a multi-step process regulated by complicated cellular pathways. In tau pathology, diverse tau modifications including phosphorylation, oxidation, acetylation and truncation promote tau aggregation in a defected neuron. At the same time, the neuron activates cellular defense mechanisms such as glycosylation. We are currently focusing on diverse tau modifications associated with tau aggregation, strategy of tau aggregation inhibition, small molecule for tau imaging, and cell-based model that could monitor and quantify tau aggregation process in living cells.

Biography :

Email: mamunbge@gmail.com

Google Scholar citation report
Citations: 1253

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