Neutrophils, which quickly congregate at the sites of infection and inflammation, are capable of ingesting microorganisms or other particles. They do this by a process known as "respiratory burst." This involves activation of an NADPH oxidase enzyme, which produces large quantities of superoxide, a reactive form of oxygen that generally kills the ingested organism.

In a study appearing online on June 15 in advance of print publication in the July issue of the Journal of Clinical Investigation, Jamel El-Benna and colleagues from INSERM in Paris examine neutrophils from the joint fluid of rheumatoid arthritis patients and show that GM-CSF and TNF-alpha induce the phosphorylation of a serine residue at position 345 on a component of NADPH oxidase. This event, which occurs via ERK1/2 and MAPK signaling pathways, "primes" the enzyme for action at sites of inflammation. The authors suggest that using drugs that inhibit this phosphorylation step might prevent the exaggerated neutrophil response in inflammatory conditions like rheumatoid arthritis, yet still preserve the ability of neutrophils to fight infection.

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Contact: Ushma Neill
editors@the-jci.org
212-342-0498
Journal of Clinical Investigation
15-Jun-2006

Page: 1
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