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Published ahead of print on March 31, 2005, doi:10.1165/rcmb.2005-0076OC

Am. J. Respir. Cell Mol. Biol., Volume 33, Number 1, July 2005, 65-70

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Submitted on February 21, 2005
Revised on March 31, 2005

Regulation of IL-5 Induced {beta}2-Integrin Adheison of Human Eosinophils by Phosphoinsotide 3-Kinase

Masaaki Sano1, Alan R Leff2*, Shigeharu Myou1, Evan Boetticher1, Angelo Y Meliton1, Jonathan Learoyd1, Anissa T Lambertino1, Nilda M Munoz1, and Xiangdong Zhu1

1 Department of Medicine, Section of Pulmonary and Critical Care Medicine, University of Chicago, Chicago, IL, USA, 2 Department of Medicine, Section of Pulmonary and Critical Care Medicine, University of Chicago, Chicago, IL, USA; Department of Neurobiology Pharmacology and Physiology and Committees on Molecular Medicine, University of Chicago, Chicago, IL, USA

* To whom correspondence should be addressed. E-mail: aleff{at}medicine.bsd.uchicago.edu.

We examined the role of phosphoinositide 3-kinase (PI3K) in integrin-mediated eosinophil adhesion. {Delta}p85, a dominant negative form of the class IA PI3K adaptor subunit, was fused to an HIV-TAT protein transduction domain (TAT-{Delta}p85). Recombinant TAT-{Delta}p85 inhibited IL-5-stimulated phosphorylation of protein kinase B, a downstream target of PI3K. {beta}2-integrin dependent adhesion caused by IL-5 to the plated ICAM-1 surrogate, BSA, was inhibited by TAT-{Delta}p85 in concentration-dependent manner. Similarly, two PI3K inhibitors, wortmannin and LY294002, blocked eosinophil adhesion to plated BSA. By contrast, {beta}1-integrin mediated eosinophil adhesion to VCAM-1 was not blocked by TAT-{Delta}p85, wortmannin, or LY294002. Rottlerin, a PKC-{delta} inhibitor, also blocked {beta}2-integrin adhesion of eosinophils caused by IL-5, while {beta}1 adhesion to VCAM-1 was not affected. IL-5 caused translocation of PKC{delta} from the cytosol to cell membrane; inhibition of PI3K inhibition by wortmannin blocked translocation of PKC{delta}. Western blot analysis demonstrated that ERK phosphorylation, a critical intermediary in adhesion elicited by IL-5, was blocked by inhibition of either PI3K or PKC-{delta}. These data suggest that ERK-mediated adhesion of {beta}2-integrin caused by IL-5 is mediated in human eosinophils by a class IA PI3K through activation of a PKC{delta} pathway.




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