Home LiteratureArticle Details
PMID: 3027097 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Regulation of neutrophil NADPH oxidase activation in a cell-free system by guanine nucleotides and fluoride. Evidence for participation of a pertussis and cholera toxin-insensitive G protein.

The Journal of biological chemistry ·Vol. 262 ·No. 4 ·1987-02-05 ·Pages 1685-90

Gabig TG, English D, Akard LP, Schell MJ

Abstract

Guanine nucleotide-binding regulatory proteins (G proteins) transduce a remarkably diverse group of extracellular signals to a relatively limited number of intracellular target enzymes. In the neutrophil, transduction of the signal following fMet-Leu-Phe receptor-ligand interaction is mediated by a pertussis toxin substrate (Gi) that activates inositol-specific phospholipase C. We have utilized a plasma membrane-containing fraction from unstimulated human neutrophils as the target enzyme to explore the role of G proteins in arachidonate and cytosolic cofactor-dependent activation of the NADPH-dependent O-2-generating oxidase. When certain guanine nucleotides or their nonhydrolyzable analogues were present during arachidonate and cytosolic cofactor-dependent activation, they exerted substantial dose-dependent effects. The GTP analogue, GTP gamma S, caused a 2-fold increase in NADPH oxidase activation (half-maximal stimulation, 1.1 microM). Either GDP or its nonhydrolyzable analogue, GDP beta S, inhibited up to 80% of the basal NADPH oxidase activation (Ki GDP = 0.12 mM, GDP beta S = 0.23 mM). GTP caused only slight and variable stimulation, whereas F-, an agent known to promote the active conformation of G proteins, caused a 1.6-fold stimulation of NADPH oxidase activation. NADPH oxidase activation in the cell-free system was absolutely and specifically dependent on Mg2+. Although O2- production in response to fMet-Leu-Phe was inhibited greater than 90% in neutrophils pretreated with pertussis toxin, cytosolic cofactor and target oxidase membranes from neutrophils treated with pertussis toxin showed no change in basal- or GTP gamma S-stimulated NADPH oxidase activation. Cholera toxin treatment of neutrophils also had no effect on the cell-free activation system. Our results suggest a role for a G protein that is distinct from Gs or Gi in the arachidonate and cytosolic cofactor-dependent NADPH oxidase cell-free activation system.

MeSH Terms
Cell-Free System Cholera Toxin/pharmacology Chromatography, Gel Enzyme Activation Fluorides/pharmacology GTP-Binding Proteins/metabolism Guanine Nucleotides/pharmacology Guanosine 5'-O-(3-Thiotriphosphate) Guanosine Triphosphate/analogs & derivatives,pharmacology Humans Magnesium/metabolism N-Formylmethionine Leucyl-Phenylalanine/pharmacology NADH, NADPH Oxidoreductases/metabolism NADPH Oxidases Neutrophils/enzymology Pertussis Toxin Receptors, Formyl Peptide Receptors, Immunologic/metabolism Superoxides/metabolism Thionucleotides/pharmacology Time Factors Virulence Factors, Bordetella/pharmacology
Chemicals
Guanine Nucleotides Receptors, Formyl Peptide Receptors, Immunologic Thionucleotides Virulence Factors, Bordetella Superoxides Guanosine 5'-O-(3-Thiotriphosphate) N-Formylmethionine Leucyl-Phenylalanine Guanosine Triphosphate Cholera Toxin NADH, NADPH Oxidoreductases NADPH Oxidases Pertussis Toxin GTP-Binding Proteins Magnesium Fluorides
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Gabig T G
English D
Akard L P
Schell M J
Article Info
Journal
The Journal of biological chemistry
Abbr.
J Biol Chem
ISSN
0021-9258
Published
1987-02-05
Pages
1685-90
Language
English
Region
United States
NLM ID
2985121R
Subset
IM
Grants
NIAID NIH HHS · AI 21961 · United States
Analysis Services
Analysis Services

Contact

No. 2 Wenbo Road, Zhangqiu District, Jinan, Shandong

Qilu Normal University · Genelibs Bioinformatics Lab

750 Shunhua Rd, Jinan

2F, Bldg F, University Science Park

Tel: 0531-88819269

WeChat Official Account

Follow our WeChat subscription account for real-time updates and the latest in medical and biological research.


Business Email

E-mail: product@genelibs.com