Life Sciences Commons^™

The Chaperone Action Of Clusterin And Its Putative Role In Quality Control Of Extracellular Protein Folding, Amy Wyatt, Justin Yerbury, Stephen Poon, Rebecca Dabbs, Mark Wilson

Mark R Wilson

The function(s) of clusterin may depend upon its topological location. A variety of intracellular "isoforms" of clusterin have been reported but further work is required to better define their identity. The secreted form of clusterin has a potent ability to inhibit both amorphous and amyloid protein aggregation. In the case of amorphous protein aggregation, clusterin forms stable, soluble high-molecular-weight complexes with misfolded client proteins. Clusterin expression is increased during many types of physiological and pathological stresses and is thought to function as an extracellular chaperone (EC). The pathology of a variety of serious human diseases is thought to arise as …