Journal
BIOCHEMISTRY
Volume 50, Issue 17, Pages 3405-3407Publisher
AMER CHEMICAL SOC
DOI: 10.1021/bi200266v
Keywords
-
Categories
Funding
- Michael J. Fox Foundation for Parkinson's disease Research
- National Institutes of Health [R01-GM083897]
- USylvester Braman Family Breast Cancer Institute
Ask authors/readers for more resources
The mechanism by which apolipoprotein E (ApoE) isoforms functionally influence the risk and progression of late-onset Alzheimer's disease (LOAD) remains hitherto unknown Herein, we present evidence that all ApoE isoforms bind to nitric oxide synthase 1 (NOS1) and that such protein-protein interaction results in S-nitrosylation of ApoE2 and ApoE3 but not ApoE4. Our structural analysis at the atomic level reveals that S-nitrosylation of ApoE2 and ApoE3 proteins may lead to conformational changes resulting in the loss of binding to low-density receptors. Collectively, our data suggest that S-nitrosylation of ApoE proteins may play an important role in regulating lipid metabolism and in the in the pathogenesis of LOAD.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available