Two cytosolic neutrophil oxidase components absent in autosomal chronic granulomatous disease

Volpp, Bryan D.; Nauseef, William M.; Clark, Robert A.

doi:10.1126/science.2848318

Cited by 407Neutrophil, Myeloperoxidase and Oxidative MechanismsRedox biology and oxidative stressImmunodeficiency and Autoimmune Disorders

Two cytosolic neutrophil oxidase components absent in autosomal chronic granulomatous disease

Volpp, Bryan D., Nauseef, William M., Clark, Robert A.·1988·Science

DOI 10.1126/science.2848318

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Abstract

Neutrophils kill microorganisms with oxygen radicals generated by an oxidase that uses the reduced form of nicotinamide adenine dinucleotide phosphate (NADPH) as substrate. This system requires both membrane and cytosolic components and is defective in patients with chronic granulomatous disease. A cytosolic complex capable of activating latent membrane oxidase was eluted from guanosine triphosphate-agarose and was used to raise polyclonal antiserum that recognized 47- and 67-kilodalton proteins. These proteins were restricted to the cytosol of myeloid cells. Both proteins were associated with NADPH oxidase-activating capacity when neutrophil cytosol was purified on nucleotide affinity matrices or molecular sizing columns. Neutrophils from patients with two different forms of autosomal chronic granulomatous disease lacked either the 47- or 67-kilodalton protein.

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H2O2 can modulate gene expression by epigenetic modification and activate transcription factors such as AP-1, NRF2, CREB, HSF1, HIF-1, TP53, NF-κβ, NOTCH, SP1, SCREB-1 and FOXO family.
“For example, H2O2 can also modulate genes expression by epigenetic modification and activate transcription factors such as AP-1, NRF2, CREB, HSF1, HIF-1, TP53, NF-κβ, NOTCH, SP1, SCREB-1 and FOXO family [14,15,16,17,18,19,20,21,22].”
From The Role of Reactive Species on Innate Immunity (2022) · cites this paper as [19]

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Rapid Publication Chronic Granulomatous Disease Due to a Defect in the Cytosolic Factor Required for Nicotinamide Adenine Dinucleotide Phosphate Oxidase Activation
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Authors: Volpp, B. D., Nauseef, W. M., & Clark, R. A.
Affiliations: University of Iowa (US)
ORCID: Nauseef, William M.
Clark, Robert A.
Venue: Science
Publisher: American Association for the Advancement of Science (AAAS)
Published: 1988-12-02
Volume: 242
Issue: 4883
Pages: 1295-1297
ISSN: 0036-8075 (ISSN-L)
1095-9203
DOI: 10.1126/science.2848318
OpenAlex: W2014594279
Cited by: 407
References: 49
Citations by year: 2026: 7 · 2025: 5 · 2024: 4 · 2023: 5 · 2022: 5 · 2021: 4 · 2020: 4 · 2019: 11 · 2018: 3 · 2017: 2 · 2016: 8 · 2015: 1 · 2014: 9 · 2013: 11 · 2012: 2
FWCI: 13.42
Type: journal article
Language: en
Open access: closed
Locations: Science (publishedVersion)
PubMed (publishedVersion)
Funders: U.S. Department of Veterans Affairs (I01 BX000513)
U.S. Public Health Service (DM 01295)
National Institute of Allergy and Infectious Diseases (AI 20866, R01AI020866)
Topics: Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
Life Sciences › Immunology and Microbiology › Immunology › Immunodeficiency and Autoimmune Disorders
Keywords: chronic granulomatous disease, neutrophil NADPH oxidase, NADPH oxidase activation, oxygen free radicals, myeloid cells
MeSH terms: Cytosol, Granulomatous Disease, Chronic, Humans, Molecular Weight, NADH, NADPH Oxidoreductases, Neutrophils, Superoxides, Blotting, Western, GTP-Binding Proteins, NADPH Oxidases

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Two cytosolic neutrophil oxidase components absent in autosomal chronic granulomatous disease

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