Innovation Anthology #248:
Research into what causes mad cow or prion folding diseases is giving scientists new insight into how normal prion proteins function.
One finding is that prion proteins bind with copper.
Jake Pushey is a post-doctoral fellow at the University of Saskatchewan. His poster at the recent Prion Conference in Edmonton looked at whether copper binding is linked to the pathogenesis of certain prion diseases.
DR. JAKE PUSHEY: Some of our early work which was looking at multiple atoms of copper binding to the prion protein, we find that the end terminal domain where those copper binding sites are, we find that part of the protein can fold or be induced to fold by copper. And the copper binding sites sort of stack up on top of one another and each of those individual copper binding sites is redux silent. So you don’t get any reduction of Copper 2 to Copper 1, which is the event which is normally associated with, triggering oxidative damage in tissues.
Dr. Jake Pushey believes this binding of copper has a neuro-protective effect in the brain.
Thanks today to The Canadian Institutes for Health Research.
FOR INNOVATION ANTHOLOGY I’M CHERYL CROUCHER
Guest
,
, , , ,
Sponsor
Canadian Institutes of Health Research
Program Date: 2009-08-06