Abstract
Cataract disease results from non-amyloid aggregation of eye lens proteins and is the leading cause of blindness in the world. Zinc concentrations in cataractous lenses are increased significantly relative to those in healthy lenses. It was recently reported that Zn(II) ions induce the aggregation of one of the more abundant proteins in the core of the lens, human γD-crystallin. Here, the mechanism of Zn-induced aggregation has been revealed through a comparative study of three homologous human lens γ-crystallins and a combination of spectroscopic, electron microscopy, and site-directed mutagenesis studies. This work reveals that a single His residue acts as a "switch" for the Zn-induced non-amyloid aggregation of human γ-crystallins. Aggregation can be reversed by a chelating agent, revealing a metal-bridging mechanism. This study sheds light on an aberrant Zn-crystallin interaction that promotes aggregation, a process that is relevant to cataract disease.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
