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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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R. Huang, J. P. Lian, D. Robinson, and J. A. Badwey
Neutrophils Stimulated with a Variety of Chemoattractants Exhibit Rapid Activation of p21-Activated Kinases (Paks): Separate Signals Are Required for Activation and Inactivation of Paks
Mol. Cell. Biol., December 1, 1998; 18(12): 7130 - 7138.
[Abstract] [Full Text]


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J. Biol. Chem.Home page
I. D. McGilvray, Z. Lu, A. C. Wei, A. P. B. Dackiw, J. C. Marshall, A. Kapus, G. Levy, and O. D. Rotstein
Murine Hepatitis Virus Strain 3 Induces the Macrophage Prothrombinase fgl-2 through p38 Mitogen-activated Protein Kinase Activation
J. Biol. Chem., November 27, 1998; 273(48): 32222 - 32229.
[Abstract] [Full Text] [PDF]


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Physiol. Rev.Home page
E. J. PETTIT
Cytosolic Free Calcium and the Cytoskeleton in the Control of Leukocyte Chemotaxis
Physiol Rev, October 1, 1998; 78(4): 949 - 967.
[Abstract] [Full Text] [PDF]


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J. Biol. Chem.Home page
C. Schafer, S. E. Ross, M. J. Bragado, G. E. Groblewski, S. A. Ernst, and J. A. Williams
A Role for the p38 Mitogen-activated Protein Kinase/Hsp 27 Pathway in Cholecystokinin-induced Changes in the Actin Cytoskeleton in Rat Pancreatic Acini
J. Biol. Chem., September 11, 1998; 273(37): 24173 - 24180.
[Abstract] [Full Text] [PDF]


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J. Immunol.Home page
P. A. Detmers, D. Zhou, E. Polizzi, R. Thieringer, W. A. Hanlon, S. Vaidya, and V. Bansal
Role of Stress-Activated Mitogen-Activated Protein Kinase (p38) in {beta}2-Integrin-Dependent Neutrophil Adhesion and the Adhesion-Dependent Oxidative Burst
J. Immunol., August 15, 1998; 161(4): 1921 - 1929.
[Abstract] [Full Text] [PDF]


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J. Biol. Chem.Home page
M. J. Rane, J. M. Arthur, E. R. Prossnitz, and K. R. McLeish
Activation of Mitogen-activated Protein Kinases by Formyl Peptide Receptors Is Regulated by the Cytoplasmic Tail
J. Biol. Chem., August 14, 1998; 273(33): 20916 - 20923.
[Abstract] [Full Text] [PDF]


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JCBHome page
A. Clerk, A. Michael, and P. H. Sugden
Stimulation of the p38 Mitogen-activated Protein Kinase Pathway in Neonatal Rat Ventricular Myocytes by the G Protein-coupled Receptor Agonists, Endothelin-1 and Phenylephrine: A Role in Cardiac Myocyte Hypertrophy?
J. Cell Biol., July 27, 1998; 142(2): 523 - 535.
[Abstract] [Full Text] [PDF]


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J. Biol. Chem.Home page
M. Ushio-Fukai, R. W. Alexander, M. Akers, and K. K. Griendling
p38 Mitogen-activated Protein Kinase Is a Critical Component of the Redox-sensitive Signaling Pathways Activated by Angiotensin II. ROLE IN VASCULAR SMOOTH MUSCLE CELL HYPERTROPHY
J. Biol. Chem., June 12, 1998; 273(24): 15022 - 15029.
[Abstract] [Full Text] [PDF]


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J. Biol. Chem.Home page
D. Sheikh-Hamad, J. Di Mari, W. N. Suki, R. Safirstein, B. A. Watts III, and D. Rouse
p38 Kinase Activity Is Essential for Osmotic Induction of mRNAs for HSP70 and Transporter for Organic Solute Betaine in Madin-Darby Canine Kidney Cells
J. Biol. Chem., January 16, 1998; 273(3): 1832 - 1837.
[Abstract] [Full Text] [PDF]


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J. Biol. Chem.Home page
K.-D. Chen, L.-Y. Chen, H.-L. Huang, C.-H. Lieu, Y.-N. Chang, M. D.-T. Chang, and Y.-K. Lai
Involvement of p38 Mitogen-activated Protein Kinase Signaling Pathway in the Rapid Induction of the 78-kDa Glucose-regulated Protein in 9L Rat Brain Tumor Cells
J. Biol. Chem., January 9, 1998; 273(2): 749 - 755.
[Abstract] [Full Text] [PDF]


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J. Immunol.Home page
G. P. Downey, J. R. Butler, H. Tapper, L. Fialkow, A. R. Saltiel, B. B. Rubin, and S. Grinstein
Importance of MEK in Neutrophil Microbicidal Responsiveness
J. Immunol., January 1, 1998; 160(1): 434 - 443.
[Abstract] [Full Text] [PDF]


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J. Biol. Chem.Home page
J. Yamauchi, M. Nagao, Y. Kaziro, and H. Itoh
Activation of p38 Mitogen-activated Protein Kinase by Signaling through G Protein-coupled Receptors. INVOLVEMENT OF Gbeta gamma AND Galpha q/11 SUBUNITS
J. Biol. Chem., October 31, 1997; 272(44): 27771 - 27777.
[Abstract] [Full Text] [PDF]


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J. Biol. Chem.Home page
E. Krump, K. Nikitas, and S. Grinstein
Induction of Tyrosine Phosphorylation and Na+/H+ Exchanger Activation during Shrinkage of Human Neutrophils
J. Biol. Chem., July 11, 1997; 272(28): 17303 - 17311.
[Abstract] [Full Text] [PDF]


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J. Biol. Chem.Home page
P. H. Naccache, S. Levasseur, G. Lachance, S. Chakravarti, S. G. Bourgoin, and S. R. McColl
Stimulation of Human Neutrophils by Chemotactic Factors Is Associated with the Activation of Phosphatidylinositol 3-Kinase gamma
J. Biol. Chem., July 28, 2000; 275(31): 23636 - 23641.
[Abstract] [Full Text] [PDF]


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J. Biol. Chem.Home page
R. A. Ward, M. Nakamura, and K. R. McLeish
Priming of the Neutrophil Respiratory Burst Involves p38 Mitogen-activated Protein Kinase-dependent Exocytosis of Flavocytochrome b558-containing Granules
J. Biol. Chem., November 17, 2000; 275(47): 36713 - 36719.
[Abstract] [Full Text] [PDF]


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J. Biol. Chem.Home page
M. J. Rane, P. Y. Coxon, D. W. Powell, R. Webster, J. B. Klein, W. Pierce, P. Ping, and K. R. McLeish
p38 Kinase-dependent MAPKAPK-2 Activation Functions as 3-Phosphoinositide-dependent Kinase-2 for Akt in Human Neutrophils
J. Biol. Chem., January 26, 2001; 276(5): 3517 - 3523.
[Abstract] [Full Text] [PDF]


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J. Biol. Chem.Home page
S. Bechoua and L. W. Daniel
Phospholipase D Is Required in the Signaling Pathway Leading to p38 MAPK Activation in Neutrophil-like HL-60 Cells, Stimulated by N-Formyl-methionyl-leucyl-phenylalanine
J. Biol. Chem., August 17, 2001; 276(34): 31752 - 31759.
[Abstract] [Full Text] [PDF]


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J. Biol. Chem.Home page
J. E. Smolen, T. K. Petersen, C. Koch, S. J. O'Keefe, W. A. Hanlon, S. Seo, D. Pearson, M. C. Fossett, and S. I. Simon
L-Selectin Signaling of Neutrophil Adhesion and Degranulation Involves p38 Mitogen-activated Protein Kinase
J. Biol. Chem., May 19, 2000; 275(21): 15876 - 15884.
[Abstract] [Full Text] [PDF]


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Proc. Natl. Acad. Sci. USAHome page
O. Werz, J. Klemm, B. Samuelsson, and O. Radmark
5-Lipoxygenase is phosphorylated by p38 kinase-dependent MAPKAP kinases
PNAS, May 9, 2000; 97(10): 5261 - 5266.
[Abstract] [Full Text] [PDF]




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