TY - JOUR
T1 - Prion-like properties of Tau protein
T2 - The importance of extracellular Tau as a therapeutic target
AU - Holmes, Brandon B.
AU - Diamond, Marc I.
PY - 2014
Y1 - 2014
N2 - Work over the past 4 years indicates that multiple proteins associated with neurodegenerative diseases, especially Tau and α-synuclein, can propagate aggregates between cells in a prion-like manner. This means that once an aggregate is formed it can escape the cell of origin, contact a connected cell, enter the cell, and induce further aggregation via templated conformational change. The prion model predicts a key role for extracellular protein aggregates in mediating progression of disease. This suggests new therapeutic approaches based on blocking neuronal uptake of protein aggregates and promoting their clearance. This will likely include therapeutic antibodies or small molecules, both of which can be developed and optimized in vitro prior to preclinical studies.
AB - Work over the past 4 years indicates that multiple proteins associated with neurodegenerative diseases, especially Tau and α-synuclein, can propagate aggregates between cells in a prion-like manner. This means that once an aggregate is formed it can escape the cell of origin, contact a connected cell, enter the cell, and induce further aggregation via templated conformational change. The prion model predicts a key role for extracellular protein aggregates in mediating progression of disease. This suggests new therapeutic approaches based on blocking neuronal uptake of protein aggregates and promoting their clearance. This will likely include therapeutic antibodies or small molecules, both of which can be developed and optimized in vitro prior to preclinical studies.
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U2 - 10.1074/jbc.R114.549295
DO - 10.1074/jbc.R114.549295
M3 - Short survey
C2 - 24860099
AN - SCOPUS:84904488776
SN - 0021-9258
VL - 289
SP - 19855
EP - 19861
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 29
ER -