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, ß, 
, and 
in Inflammatory Cell Lineages
Department of Biology, Amgen, Boulder, CO 80301
Four p38 mitogen-activated protein kinases (p38
, ß, 
, 
)
have been described. To understand the role of p38 family members in
inflammation, we determined their relative expression in cells that
participate in the inflammatory process. Expression was measured at the
level of mRNA by reverse-transcriptase PCR and protein by Western blot
analysis. p38 was the dominant form of p38 in monocytes; expression
of p38 was low and p38ß was undetected. In macrophages, p38 and
p38 were abundant, but p38ß was undetected. p38 and p38 were
also expressed by neutrophils, CD4+ T cells, and
endothelial cells. Again, p38ß was not detected in neutrophils,
although low amounts were present in CD4+ T cells. In
contrast, p38ß was abundant in endothelial cells. p38 protein was
not detected in any cell type, although p38 mRNA was present in
endothelial cells. Immunokinase assays showed a strong activation of
p38 and a lesser activation of p38 in LPS-stimulated macrophages.
Abs specific for mono- and dual-phophorylated forms of p38 suggested
that LPS induces dual phosphorylation of p38, but primarily
mono-phosphorylation of p38. IL-1ß activated p38 and p38ß in
endothelial cells. However, p38 was the more activated form based on
kinase assays and phosphorylation analysis. Expression and activation
patterns of p38 in macrophages and endothelial cells suggest that
p38 plays a major role in the inflammatory response. Additional
studies will be needed to define the contribution of p38 to
macrophage, neutrophil, and T cell functions, and of p38ß to
signaling in endothelial cells and T cells.
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A. Mocsai, Z. Jakus, T. Vantus, G. Berton, C. A. Lowell, and E. Ligeti Kinase Pathways in Chemoattractant-Induced Degranulation of Neutrophils: The Role of p38 Mitogen-Activated Protein Kinase Activated by Src Family Kinases J. Immunol., April 15, 2000; 164(8): 4321 - 4331. [Abstract] [Full Text] [PDF]
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M. Allen, L. Svensson, M. Roach, J. Hambor, J. McNeish, and C. A. Gabel Deficiency of the Stress Kinase p38{alpha} Results in Embryonic Lethality: Characterization of the Kinase Dependence of Stress Responses of Enzyme-deficient Embryonic Stem Cells J. Exp. Med., March 6, 2000; 191(5): 859 - 870. [Abstract] [Full Text] [PDF]
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 D. A. Partrick, E. E. Moore, P. J. Offner, D. R. Meldrum, D. Y. Tamura, J. L. Johnson, and C. C. Silliman Maximal Human Neutrophil Priming for Superoxide Production and Elastase Release Requires p38 Mitogen-Activated Protein Kinase Activation Arch Surg, February 1, 2000; 135(2): 219 - 225. [Abstract] [Full Text] [PDF]
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P. Kovarik, D. Stoiber, P. A. Eyers, R. Menghini, A. Neininger, M. Gaestel, P. Cohen, and T. Decker Stress-induced phosphorylation of STAT1 at Ser727 requires p38 mitogen-activated protein kinase whereas IFN-gamma uses a different signaling pathway PNAS, November 23, 1999; 96(24): 13956 - 13961. [Abstract] [Full Text] [PDF]
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J. P. Lian, R. Huang, D. Robinson, and J. A. Badwey Activation of p90RSK and cAMP Response Element Binding Protein in Stimulated Neutrophils: Novel Effects of the Pyridinyl Imidazole SB 203580 on Activation of the Extracellular Signal-Regulated Kinase Cascade J. Immunol., October 15, 1999; 163(8): 4527 - 4536. [Abstract] [Full Text] [PDF]
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S.-C. Hsu, M. A. Gavrilin, M.-H. Tsai, J. Han, and M.-Z. Lai p38 Mitogen-activated Protein Kinase Is Involved in Fas Ligand Expression J. Biol. Chem., September 3, 1999; 274(36): 25769 - 25776. [Abstract] [Full Text] [PDF]
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S. R. Dashti, T. Efimova, and R. L. Eckert MEK7-dependent Activation of p38 MAP Kinase in Keratinocytes J. Biol. Chem., March 9, 2001; 276(11): 8059 - 8063. [Abstract] [Full Text] [PDF]
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S. Zhuang, J. T. Demirs, and I. E. Kochevar p38 Mitogen-activated Protein Kinase Mediates Bid Cleavage, Mitochondrial Dysfunction, and Caspase-3 Activation during Apoptosis Induced by Singlet Oxygen but Not by Hydrogen Peroxide J. Biol. Chem., August 18, 2000; 275(34): 25939 - 25948. [Abstract] [Full Text] [PDF]
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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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G. Alonso, C. Ambrosino, M. Jones, and A. R. Nebreda Differential Activation of p38 Mitogen-activated Protein Kinase Isoforms Depending on Signal Strength J. Biol. Chem., December 15, 2000; 275(51): 40641 - 40648. [Abstract] [Full Text] [PDF]
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 T. Matsumoto, I. Turesson, M. Book, P. Gerwins, and L. Claesson-Welsh p38 MAP kinase negatively regulates endothelial cell survival, proliferation, and differentiation in FGF-2-stimulated angiogenesis J. Cell Biol., January 7, 2002; 156(1): 149 - 160. [Abstract] [Full Text] [PDF]
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