Inhibition of human vascular nadph oxidase by apocynin derived oligophenols

Mora-Pale, Mauricio; Weïwer, Michel; Yu, Jingjing; Linhardt, Robert J.; Dordick, Jonathan S.

doi:10.1016/j.bmc.2009.05.061

Cited by 37Bioactive Compounds and Antitumor AgentsNitric Oxide and Endothelin EffectsRedox biology and oxidative stress

Inhibition of human vascular nadph oxidase by apocynin derived oligophenols

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Mora-Pale, Mauricio, Weïwer, Michel, Yu, Jingjing, Linhardt, Robert J., Dordick, Jonathan S.·2009·Bioorganic & Medicinal Chemistry

DOI 10.1016/j.bmc.2009.05.061PMC PMC2723721

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Abstract

Enzymatic oxidation of apocynin, which may mimic in vivo metabolism, affords a large number of oligomers (apocynin oxidation products, AOP) that inhibit vascular NADPH oxidase. In vitro studies of NADPH oxidase activity were performed to identify active inhibitors, resulting in a trimer hydroxylated quinone (IIIHyQ) that inhibited NADPH oxidase with an IC(50)=31nM. Apocynin itself possessed minimal inhibitory activity. NADPH oxidase is believed to be inhibited through prevention of the interaction between two NADPH oxidase subunits, p47(phox) and p22(phox). To that end, while apocynin was unable to block the interaction of his-tagged p47(phox) with a surface immobilized biotinylated p22(phox) peptide, the IIIHyQ product strongly interfered with this interaction (apparent IC(50)=1.6microM). These results provide evidence that peroxidase-generated AOP, which consist of oligomeric phenols and quinones, inhibit critical interactions that are involved in the assembly and activation of human vascular NADPH oxidase.

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Apocynin was long considered as a specific Nox2 inhibitor, but several studies have shown that this is not the case.
“Apocynin was long considered as specific Nox2 inhibitor. However, several studies have shown that this is indeed not the case.”
From Functions of ROS in Macrophages and Antimicrobial Immunity (2021) · cites this paper as [398]
Apocynin directly scavenges ROS due to its antioxidant capacities.
“Instead, apocynin directly scavenges ROS due to its antioxidant capacities [340,395,396,397,398].”
From Functions of ROS in Macrophages and Antimicrobial Immunity (2021) · cites this paper as [398]

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Analyse der Wirkmechanismen verschiedener NADPH-Oxidase-Hemmstoffe
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Authors: Mora-Pale, M., Weïwer, M., Yu, J., Linhardt, R. J., & Dordick, J. S.
Affiliations: Rensselaer Polytechnic Institute (US)
Corresponding author: Linhardt, Robert J.
Dordick, Jonathan S.
ORCID: Weïwer, Michel
Yu, Jingjing
Linhardt, Robert J.
Dordick, Jonathan S.
Venue: Bioorganic & Medicinal Chemistry
Publisher: Elsevier BV
Published: 2009-07
Volume: 17
Issue: 14
Pages: 5146-5152
ISSN: 0968-0896 (ISSN-L)
DOI: 10.1016/j.bmc.2009.05.061
PMC: PMC2723721
OpenAlex: W2137518469
Cited by: 36
References: 50
Citations by year: 2026: 1 · 2023: 2 · 2022: 1 · 2021: 6 · 2019: 2 · 2018: 3 · 2016: 2 · 2015: 2 · 2014: 1 · 2013: 5 · 2012: 6
FWCI: 5.29
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
Locations: Bioorganic & Medicinal Chemistry (publishedVersion)
PubMed (publishedVersion)
PubMed Central (acceptedVersion)
Funders: National Center for Complementary and Integrative Health (R21AT002115, AT002115)
Topics: Life Sciences › Pharmacology, Toxicology and Pharmaceutics › Toxicology › Bioactive Compounds and Antitumor Agents
Health Sciences › Medicine › Physiology › Nitric Oxide and Endothelin Effects
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
Keywords: apocynin, NADPH oxidase, quinones, p47phox, p22phox, enzyme inhibition, oligomerization
MeSH terms: Acetophenones, Amino Acid Sequence, Biotin, Cells, Cultured, Enzyme Inhibitors, Humans, Molecular Sequence Data, Peroxidase, Oxidation-Reduction, Peptides, Superoxides, NADPH Oxidases, Endothelial Cells, Cytochromes c

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Inhibition of human vascular nadph oxidase by apocynin derived oligophenols

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