ArticleJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry2012
Amyloid beta-heme peroxidase promoted protein nitrotyrosination: relevance to widespread protein nitration in Alzheimer's disease.
Article in Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 42 citations in OpenAlex.
- How Sodium Dodecyl Sulfate Micelles Affect the Coordination and Peroxidase-Like Activity of the Hemin-Aβ16 Complex.ChemPlusChem · 2025Article
- Hesperetin Nanocrystals Improve Mitochondrial Function in a Cell Model of Early Alzheimer Disease.Antioxidants (Basel, Switzerland) · 2021Article
- Condition-Dependent Coordination and Peroxidase Activity of Hemin-Aβ Complexes.Molecules (Basel, Switzerland) · 2020Article
- Molecular crowding effects on the biochemical properties of amyloid β-heme, Aβ-Cu and Aβ-heme-Cu complexes.Chemical science · 2020Article
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- Review
- Interaction of apoNeuroglobin with heme-Aβ complexes relevant to Alzheimer's disease.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2015Article
- Amyloid beta modulated the selectivity of heme-catalyzed protein tyrosine nitration: an alternative mechanism for selective protein nitration.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2012Article
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7 authors at 2 institutions in 1 country.
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Abstract
Amyloid beta (Aβ) peptide accumulation has been demonstrated to play a central role in Alzheimer's disease (AD). Substantial evidence indicates that protein nitrotyrosination contributes to Aβ-dependent neurotoxicity; however, the molecular mechanism is unknown. Recent research has shown that Aβ complexes with heme to form Aβ-heme, and increases the pseudo-peroxidase activity of heme. We found that Aβ-heme uses H(2)O(2) and NO(2)(-) to cause nitration of enolase and synaptic proteins more effectively than heme. Thus, the increased peroxidase activity of Aβ-heme may be the molecular link between excess Aβ and the widespread protein nitration in AD. Interestingly, the site of enolase nitration that was catalyzed by Aβ-heme is different from that induced by heme. Moreover, the secondary structural perturbations of Aβ-heme-treated and heme-treated enolase are also different. These observations suggest that Aβ-heme targets specific amino acid sequences in enolase. Furthermore, our data show that Aβ-heme peroxidase activity is independent of the aggregation state of Aβ, suggesting an important role of soluble Aβ in addition to Aβ aggregates and oligomers in AD pathogenesis.
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