S-nitrosylation of ApoE in Alzheimer's disease

Alexander J. Abrams, Amjad Farooq, Gaofeng Wang

Research output: Contribution to journalArticlepeer-review

33 Scopus citations


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 lipoprotein (LDL) receptors. Collectively, our data suggest that S-nitrosylation of ApoE proteins may play an important role in regulating lipid metabolism and in the pathogenesis of LOAD.

Original languageEnglish (US)
Pages (from-to)3405-3407
Number of pages3
Issue number17
StatePublished - May 3 2011

ASJC Scopus subject areas

  • Biochemistry


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