Effect of Ca2+ ATPase Inhibitors on MCP-1 Release from Bone Marrow-Derived Mast Cells and the Involvement of p38 MAP Kinase Activation

2000 ◽  
Vol 121 (1) ◽  
pp. 34-43 ◽  
Author(s):  
R. Teshima ◽  
J. Onose ◽  
H. Okunuki ◽  
J. Sawada
Keyword(s):  
Bone Marrow ◽  
Mast Cells ◽  
Map Kinase ◽  
P38 Map Kinase ◽  
Kinase Activation ◽  
Atpase Inhibitors

scholarly journals Spred-1 Negatively Regulates Interleukin-3-mediated ERK/Mitogen-activated Protein (MAP) Kinase Activation in Hematopoietic Cells

2004 ◽  
Vol 279 (50) ◽  
pp. 52543-52551 ◽  
Author(s):  
Atsushi Nonami ◽  
Reiko Kato ◽  
Koji Taniguchi ◽  
Daigo Yoshiga ◽  
Takaharu Taketomi ◽  
...  
Keyword(s):  
Bone Marrow ◽  
Mast Cells ◽  
Map Kinase ◽  
Cell Lines ◽  
Colony Formation ◽  
Wild Type ◽  
Kinase Activation ◽  
Erk Activation ◽  
Protein Map ◽  
Mitogen Activated Protein

Sprouty/Spred family proteins have been identified as negative regulators of growth factor-induced ERK/mitogen-activated protein (MAP) kinase activation. However, it has not been clarified whether these proteins regulate cytokine-induced ERK activity. We found that Spred-1 is highly expressed in interleukin-3 (IL-3)-dependent hematopoietic cell lines and bone marrow-derived mast cells. To investigate the roles of Spred-1 in hematopoiesis, we expressed wild-type Spred-1 and a dominant negative form of Spred-1, ΔC-Spred, in IL-3- and stem cell factor (SCF)-dependent cell lines as well as hematopoietic progenitor cells from mouse bone marrow by retrovirus gene transfer. In IL-3-dependent Ba/F3 cells expressing c-kit, forced expression of Spred-1 resulted in a reduced proliferation rate and ERK activation in response to not only SCF but also IL-3. In contrast, ΔC-Spred augmented IL-3-induced cell proliferation and ERK activation. Wild-type Spred-1 inhibited colony formation of bone marrow cells in the presence of cytokines, whereas ΔC-Spred-1 expression enhanced colony formation. Augmentation of ERK activation and proliferation in response to IL-3 was also observed in Spred-1-deficient bone marrow-derived mast cells. These data suggest that Spred-1 negatively regulates hematopoiesis by suppressing not only SCF-induced but also IL-3-induced ERK activation.

Thioredoxin Negatively Regulates p38 MAP Kinase Activation and IL-6 Production by Tumor Necrosis Factor-α

1999 ◽  
Vol 258 (2) ◽  
pp. 443-447 ◽  
Author(s):  
Shu Hashimoto ◽  
Ken Matsumoto ◽  
Yasuhiro Gon ◽  
Sachiko Furuichi ◽  
Shuichiro Maruoka ◽  
...  
Keyword(s):  
Tumor Necrosis Factor ◽  
Map Kinase ◽  
Tumor Necrosis ◽  
Tumor Necrosis Factor Α ◽  
P38 Map Kinase ◽  
Kinase Activation ◽  
Factor Α ◽  
Necrosis Factor

Enhanced tolerance to ischaemia of thyroxine treated rat heart is associated with attenuated P38 map kinase activation

2001 ◽  
Vol 33 (6) ◽  
pp. A89
Author(s):  
Costas Pantos ◽  
Vassilliki Malliopoulou ◽  
Evangelia Karamanoli ◽  
Stelios Tzeis ◽  
Iordanis S. Mourouzis ◽  
...  
Keyword(s):  
Map Kinase ◽  
Rat Heart ◽  
P38 Map Kinase ◽  
Kinase Activation

Specific Regulation of Cytokine-Dependent p38 MAP Kinase Activation by p62/SQSTM1

2007 ◽  
Vol 143 (6) ◽  
pp. 765-772 ◽  
Author(s):  
K. Kawai ◽  
A. Saito ◽  
T. Sudo ◽  
H. Osada
Keyword(s):  
Map Kinase ◽  
P38 Map Kinase ◽  
Kinase Activation ◽  
Specific Regulation

Covariance Among Age, Spinal p38 MAP Kinase Activation and Allodynia

2006 ◽  
Vol 7 (5) ◽  
pp. 337-345 ◽  
Author(s):  
Camilla I. Svensson ◽  
Maria Schäfers ◽  
Toni L. Jones ◽  
Tony L. Yaksh ◽  
Linda S. Sorkin
Keyword(s):  
Map Kinase ◽  
P38 Map Kinase ◽  
Kinase Activation

Gö6976 inhibits LPS-induced microglial TNFα release by suppressing p38 MAP kinase activation

Neuroscience ◽  
2002 ◽  
Vol 114 (3) ◽  
pp. 689-697 ◽  
Author(s):  
G.-H Jeohn ◽  
C.L Cooper ◽  
K.-J Jang ◽  
B Liu ◽  
D.-S Lee ◽  
...  
Keyword(s):  
Map Kinase ◽  
P38 Map Kinase ◽  
Kinase Activation

scholarly journals Fer Kinase Is Required for Sustained p38 Kinase Activation and Maximal Chemotaxis of Activated Mast Cells

2002 ◽  
Vol 22 (18) ◽  
pp. 6363-6374 ◽  
Author(s):  
Andrew W. B. Craig ◽  
Peter A. Greer
Keyword(s):  
Mast Cells ◽  
Map Kinases ◽  
Immunoglobulin E ◽  
P38 Map Kinase ◽  
Mast Cell Activation ◽  
Receptor Protein ◽  
Mouse Bone Marrow ◽  
P38 Kinase ◽  
Kinase Activation ◽  
Kit Receptor

ABSTRACT Mast cells play important roles in inflammation and immunity and express the high-affinity immunoglobulin E receptor (FcεRI) and the receptor protein-tyrosine kinase Kit. Aggregation of FcεRI via antigen binding elicits signals leading to the release of preformed inflammatory mediators as well as de novo-synthesized lipid mediators and cytokines and to elevated cell adhesion and migration. Here, we report that in mouse bone marrow-derived mast cells, Fer kinase is activated downstream of activated FcεRI and activated Kit receptor, and this activation is abolished in cells homozygous for a kinase-inactivating mutation in Fer (fer DR/DR ). Interestingly, the highly related Fps/Fes kinase is also activated upon FcεRI aggregation. This report represents the first description of a common signaling pathway activating Fer and Fps/Fes. While Fer-deficient cells showed similar activation of the Erk mitogen-activated protein (MAP) kinases, p38 MAP kinase activation was less sustained than that in wild-type cells. Although no major defects were observed in degranulation, leukotriene biosynthesis, and cytokine secretion, Fer-deficient cells displayed increased adhesion and decreased motility upon activation of FcεRI and the Kit receptor. The restoration of Fer kinase activity in fer DR/DR mast cells resulted in prolonged p38 kinase activation and increased antigen-mediated cell migration of sensitized mast cells. Thus, Fer is required for maximal p38 kinase activation to promote the chemotaxis of activated mast cells. Further studies with mast cells derived from fps/fes-deficient mice will be required to provide insight into the role of Fps/Fes in mast cell activation.

p38 MAP kinase-mediated negative inotropic effect of HIV gp120 on cardiac myocytes

2004 ◽  
Vol 286 (1) ◽  
pp. C1-C7 ◽  
Author(s):  
Hong Kan ◽  
Zirong Xie ◽  
Mitchell S. Finkel
Keyword(s):  
Map Kinase ◽  
Cardiac Myocytes ◽  
Myocardial Dysfunction ◽  
Negative Inotropic Effect ◽  
P38 Map Kinase ◽  
Neonatal Rat ◽  
Inotropic Effect ◽  
Kinase Activation ◽  
Hiv Gp120 ◽  
Sb 203580

Myocardial dysfunction leading to dilated cardiomyopathy has been documented with surprisingly high frequency in human immunodeficiency virus (HIV)-infected individuals. p38 MAP kinase has been implicated as a mediator of myocardial dysfunction. We previously reported p38 MAP kinase activation by the HIV coat protein gp120 in neonatal rat cardiac myocytes. We now report the direct inotropic effects of HIV gp120 on adult rat ventricular myocytes (ARVM). ARVM were continuously superfused with gp120, and percent fractional shortening (FS) was determined by automated border detection and simultaneous intracellular ionized free Ca2+concentration ([Ca2+]i) measured by fura 2-AM fluorescence: gp120 alone increased FS and increased [Ca2+]iwithin 5 min and then depressed FS without a decrease in [Ca2+]iby 20–60 min, which persisted for at least 2 h. Exposure of ARVM to gp120 also resulted in the phosphorylation of the upstream regulator of p38 MAP kinase MKK3/6, p38 MAP kinase itself, and its downstream effector, ATF-2, over a similar time course. ERK (p44/42) and JNK stress signaling pathways were not similarly activated. The effects of the p38 MAP kinase inhibitor were concentration dependent. SB-203580 (10 μM) blocked both p38 MAP kinase phosphorylation and the delayed negative inotropic effect of gp120. SB-203580 (5 μM) selectively blocked phosphorylation of ATF-2 without blocking the phosphorylation of MKK3/6 or p38 MAP kinase itself. SB-203580 (5 μM) administered before, with, or after gp120 blocked the negative inotropic effect of gp120 in ARVM. p38 MAP kinase activation may be a common stress-response mechanism contributing to myocardial dysfunction in HIV and other nonischemic as well as ischemic cardiomyopathies.

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