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J. Biol. Chem., Vol. 279, Issue 4, 2657-2665, January 23, 2004
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Integrins and Cytokines Activate Nuclear Transcription Factor-
B in Human Neutrophils*
From the Medical Faculty of the Charité, Department of Nephrology and Hypertension, Franz Volhard Clinic, HELIOS-Klinikum-Berlin and Max Delbrück Center for Molecular Medicine, 13125 Berlin, Germany
Neutrophil adhesion to extracellular matrix is necessary for an effective inflammatory response. Adhesion may accelerate neutrophil activation by affecting intracellular signaling pathways. The nuclear transcription factor 
B (NF-B) controls several cellular functions, including inflammation, proliferation, and cell survival. We explored the role of adhesion in NF-B activation in human neutrophils. Cells were stimulated with tumor necrosis factor-
(TNF-), granulocyte macrophage-colony-stimulating factor (GM-CSF), interleukin-8 (IL-8), and formyl-methionyl-leucyl-phenylalanine (fMLP). All four initiated neutrophil adherence to and spreading on fibronectin. GM-CSF and IL-8 did not activate NF-B in suspended neutrophils but rapidly activated NF-B under adherent conditions on matrix, as shown by IB kinase activity assay, IB degradation, electromobility shift assay, and quantitative reverse transcriptase-PCR. In contrast, TNF– activated NF-B both in suspended cells and adherent cells. fMLP did not activate NF-B in either suspended or adherent cells. Specific 
2 integrin blockade prevented NF-B activation by GM-CSF and IL-8 on fibronectin. Co-stimulating CD18 and CD11b with activating antibodies resulted in NF-B activation by GM-CSF and IL-8 in suspended cells. We inhibited actin polymerization with cytochalasin and blocked the non-receptor kinase Syk with piceatannol. Both maneuvers prevented the co-stimulatory NF-B-activating signal by 2 integrins. Thus, in addition to 2 integrin ligand binding, NF-B activation depended on the formation of the receptor-associated intracellular focal adhesion complex. We conclude that 2 integrins may provide co-stimulatory signals allowing some soluble mediators to activate the NF-B pathway even when they are not capable of doing so in suspension. This effect may become important when human neutrophils leave the circulating blood and migrate through extracellular matrix during inflammation.
Received for publication, September 3, 2003 , and in revised form, November 5, 2003.
* This work was supported by Grants DFG Ke 576/5-1 and 5-2 from the Deutsche Forschungsgemeinschaft. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.
To whom correspondence should be addressed: Wiltberg Strasse 50, 13125 Berlin, Germany. Tel.: 49-30-9417-2202; Fax: 49-30-9417-2206; E-mail: kettritz{at}fvk-berlin.de.
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