healthcare-biosimilars-2018-posters-accepted-abstracts

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Asian Journal of Biomedical and Pharmaceutical Sciences | Volume 8

March 26-27, 2018 | Orlando, USA

World Summit on

Healthcare & Hospital Management

International Conference & Exhibition on

Biologics and Biosimilars

lzheimer’s disease (AD) is a neurodegenerative

disease characterized by progressive cognitive decline.

It accounts for 60%-70% of total dementia cases. The

extracellular plaques of amyloid beta and the intracellular

neurofibrillary tangles of Tau protein are the hallmarks of

AD. Tau is a microtubule-associated protein, which stabilizes

the microtubules and maintains neuronal structure as well

as trafficking. It is amenable to various post-translational

modifications (PTMs), which influence its microtubule

binding affinity. The most exclusively studied PTM is

hyperphosphorylation, which affects themicrotubule binding

and leads to Tau aggregation. Other PTMs include glycation,

acetylation, methylation, nitration etc. Chaperones such as

Hsp70 and Hsp90 tries to resolve the toxic conformations of

Tau which is then either folded to its native form or in the

downstream is degraded and eliminated from the cell. But

in diseased conditions, the chaperones fail to remove the

mutated or toxic Tau species. Chaperones are also involved in

lysosomal degradation of Tau by a process called chaperone

mediated autophagy (CMA) and helps in removal of modified

Tau. The cellular machinery directs Tau degradation via UPS.

In the other hand, inhibiting the chaperone activity would

lead to degradation and elimination of toxic Tau species.

Small molecules inhibitors against chaperone activity are

known to be effective in clearance of the aberrant Tau from

cell.

Microtubule associated Tau squired by molecular chaperones in Alzheimer’s disease

Subashchandrabose Chinnathambi

1, 2

and

Nalini V Gorantla

1, 2

CSIR-National Chemical Laboratory, Pune, India

Academy of Scientific and Innovative Research, India