Hsp110 Plays a Critical Role in Tau Hyperphosphorylation and Tauopathies (e.g., Alzheimer’s Disease, ALS, Parkinson’s, and Others)

Description:

State of the Art:
Alzheimer's disease, Parkinson's disease, and amyotrophic lateral sclerosis (ALS), are considered to be protein misfolding disorders. Heat shock proteins provide a line of defense against protein misfolding disorders and are among the most potent suppressors of neurodegeneration in animal models. Several different heat shock proteins are implicated in the misfolding associated with the fore-mentioned diseases. 

 

Problem with the Current Art:
Alzheimer's therapeutics have thus far failed to provide an effective treatment. There are no therapeutics available for Parkinson's Disease or ALS.

 

Advantages of Novel Invention:

Hsp110-deficient (hsp110-/-) mice generated in the inventors laboratory exhibit an age-dependent accumulation of hyperphosphorylated tau and tau filaments, neurodegeneration and neuronal death. Hsp110 deficiency is the second example of a gene deficiency leading to accumulation of p-tau and neurodegeneration; the first was Pin1. Pin1 isomerase activity is required for dephosphorylation of tau. Our inventors analyses indicate that Hsp110 interacts with both tau, but Pin.

 

 

Inventors: Nahid Mivechi, Ph.D; Binnur Eroglu, Ph.D; Demetrius Moskophidis, Ph.D;

 

Case Number: GHSU 2008-015

Patent Information:
Category(s):
Research Tools
For Information, Contact:
GRU
Augusta University
 
Inventors:
Nahid Mivechi
Binnur Eroglu
Dimitrios Moskophidis
Keywords:
ALS
Alzheimer's Disease
Mouse
Parkinson's Disease
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