Social and Behavioral Sciences Commons^™

Evidence That Clusterin Has Discrete Chaperone And Ligand Binding Sites, Johnathon Lakins, Stephen Poon, Simon Easterbrook-Smith, John Carver, Martin Tenniswood, Mark Wilson

Mark R Wilson

Clusterin is the first identified extracellular mammalian chaperone and binds to a wide variety of partly unfolded, stressed proteins. Clusterin also binds to many different unstressed ligands including the cell surface receptor low density lipoprotein receptor-related protein-2 (LRP-2). It is unknown whether clusterin binds to all of these many ligands via one or more binding sites. Furthermore, the region(s) of clusterin involved in these many binding interactions remain to be identified. As part of an investigation of these issues, we expressed recombinant human clusterin in the yeast Pichia pastoris. The resultant protein had variable proteolytic truncations of the C-terminal region …