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Volume 272, Number 2, Issue of January 10, 1997 pp. 937-944
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

Chemotactic Peptide N-formyl-Met-Leu-Phe Activation of p38 Mitogen-activated Protein Kinase (MAPK) and MAPK-activated Protein Kinase-2 in Human Neutrophils

(Received for publication, August 8, 1996, and in revised form, October 16, 1996)

Eric Krump Dagger , Jasbinder S. Sanghera , Steven L. Pelech , Wendy Furuya Dagger and Sergio Grinstein Dagger par

From the Dagger  Division of Cell Biology, Research Institute, The Hospital for Sick Children and the par  Department of Biochemistry, University of Toronto, Toronto, Ontario M5G 1X8, Canada and the  Department of Medicine, University of British Columbia, and Kinetek Pharmaceuticals Inc., Vancouver, British Columbia V5Z 1A1, Canada

Activation of polymorphonuclear leukocytes (PMN) by chemotactic peptides initiates a series of functional responses that serve to eliminate pathogens. The intermediate steps that link engagement of the chemoattractant receptor to the microbicidal responses involve protein kinases that have yet to be identified. In this study we detected in human PMN the presence of p38 mitogen-activated protein kinase (MAPK), which became rapidly tyrosine phosphorylated and activated in response to the chemotactic peptide N-formyl-methionyl-leucyl-phenylalanine (fMLP). Pretreatment of PMN with wortmannin, a phosphatidylinositol 3-kinase inhibitor, or bis-indolylmaleimide, a protein kinase C antagonist, resulted in partial inhibition of p38 phosphorylation upon fMLP stimulation. Similarly, phosphorylation of p38 was only partially inhibited when the fMLP-induced cytosolic calcium transient was prevented. Stimulation of PMN by the chemoattractant also resulted in the rapid phosphorylation and activation of MAPK-activated protein kinase-2 (MAPKAPK-2), which was completely inhibited by the specific p38 inhibitor, SB203580. The physical interaction of p38 with MAPKAPK-2 was studied by coimmunoprecipitation. These two kinases were found to be associated in unstimulated PMN but dissociated upon activation of the cells by fMLP. Together these findings demonstrate the activation of p38 by chemotactic peptides in human PMN by a process involving phosphatidylinositol 3-kinase, protein kinase C, and calcium. p38, in turn, is an upstream activator of MAPKAPK-2.


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