Document Detail


The prolyl isomerase Pin1 acts as a novel molecular switch for TNF-alpha-induced priming of the NADPH oxidase in human neutrophils.
MedLine Citation:
PMID:  20956805     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Neutrophils play a key role in host defense by releasing reactive oxygen species (ROS). However, excessive ROS production by neutrophil nicotinamide adenine dinucleotide phosphate (NADPH) oxidase can damage bystander tissues, thereby contributing to inflammatory diseases. Tumor necrosis factor-α (TNF-α), a major mediator of inflammation, does not activate NADPH oxidase but induces a state of hyperresponsiveness to subsequent stimuli, an action known as priming. The molecular mechanisms by which TNF-α primes the NADPH oxidase are unknown. Here we show that Pin1, a unique cis-trans prolyl isomerase, is a previously unrecognized regulator of TNF-α-induced NADPH oxidase hyperactivation. We first showed that Pin1 is expressed in neutrophil cytosol and that its activity is markedly enhanced by TNF-α. Inhibition of Pin1 activity with juglone or with a specific peptide inhibitor abrogated TNF-α-induced priming of neutrophil ROS production induced by N-formyl-methionyl-leucyl-phenylalanine peptide (fMLF). TNF-α enhanced fMLF-induced Pin1 and p47phox translocation to the membranes and juglone inhibited this process. Pin1 binds to p47phox via phosphorylated Ser345, thereby inducing conformational changes that facilitate p47phox phosphorylation on other sites by protein kinase C. These findings indicate that Pin1 is critical for TNF-α-induced priming of NADPH oxidase and for excessive ROS production. Pin1 inhibition could potentially represent a novel anti-inflammatory strategy.
Authors:
Tarek Boussetta; Marie-Anne Gougerot-Pocidalo; Gilles Hayem; Silvia Ciappelloni; Houssam Raad; Riad Arabi Derkawi; Odile Bournier; Yolande Kroviarski; Xiao Zhen Zhou; James S Malter; Ping K Lu; Aghleb Bartegi; Pham My-Chan Dang; Jamel El-Benna
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't     Date:  2010-10-18
Journal Detail:
Title:  Blood     Volume:  116     ISSN:  1528-0020     ISO Abbreviation:  Blood     Publication Date:  2010 Dec 
Date Detail:
Created Date:  2010-12-24     Completed Date:  2011-02-22     Revised Date:  2012-04-06    
Medline Journal Info:
Nlm Unique ID:  7603509     Medline TA:  Blood     Country:  United States    
Other Details:
Languages:  eng     Pagination:  5795-802     Citation Subset:  AIM; IM    
Affiliation:
Inserm U773, Paris, France.
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MeSH Terms
Descriptor/Qualifier:
Blotting, Western
Cell Membrane / metabolism
Cytosol / metabolism
Humans
N-Formylmethionine Leucyl-Phenylalanine / pharmacology
NADPH Oxidase / chemistry,  metabolism*
Naphthoquinones / pharmacology
Neutrophils / drug effects*,  enzymology
Peptidylprolyl Isomerase / metabolism*
Phosphorylation
Protein Transport
Reactive Oxygen Species / metabolism
Tumor Necrosis Factor-alpha / pharmacology*
Grant Support
ID/Acronym/Agency:
P01 HL088594/HL/NHLBI NIH HHS; P01 HL088594-02/HL/NHLBI NIH HHS; P01 HL088594-03/HL/NHLBI NIH HHS; P01 HL088594-04/HL/NHLBI NIH HHS; P01 HL088594-05/HL/NHLBI NIH HHS; P30 HD03352/HD/NICHD NIH HHS; R01 HL087950/HL/NHLBI NIH HHS
Chemical
Reg. No./Substance:
0/NIMA-interacting peptidylprolyl isomerase; 0/Naphthoquinones; 0/Reactive Oxygen Species; 0/Tumor Necrosis Factor-alpha; 481-39-0/juglone; 59880-97-6/N-Formylmethionine Leucyl-Phenylalanine; EC 1.6.3.1/NADPH Oxidase; EC 1.6.3.1/neutrophil cytosolic factor 1; EC 5.2.1.8/Peptidylprolyl Isomerase
Comments/Corrections
Comment In:
Blood. 2010 Dec 23;116(26):5788-9   [PMID:  21183694 ]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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