期刊
BIOCHEMISTRY
卷 50, 期 17, 页码 3405-3407出版社
AMER CHEMICAL SOC
DOI: 10.1021/bi200266v
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资金
- Michael J. Fox Foundation for Parkinson's disease Research
- National Institutes of Health [R01-GM083897]
- USylvester Braman Family Breast Cancer Institute
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.
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