Biochemical characterization of mitogen-activated protein (MAP) kinase activity in Toxoplasma gondii

2000 ◽  
Vol 86 (7) ◽  
pp. 588-598 ◽  
Author(s):  
Marie-Paule Roisin ◽  
Florence Robert-Gangneux ◽  
Claudine Creuzet ◽  
Jean Dupouy-Camet
Keyword(s):  
Toxoplasma Gondii ◽  
Map Kinase ◽  
Kinase Activity ◽  
Biochemical Characterization ◽  
Protein Map ◽  
Mitogen Activated Protein

MITOGEN-ACTIVATED PROTEIN (MAP) KINASE ACTIVITY INCREASES AFTER FOCAL CEREBRAL ISCHEMIA IN RATS

1998 ◽  
Vol 26 (Supplement) ◽  
pp. 84A
Author(s):  
John W. Kuluz ◽  
Charles L. Schleien ◽  
Y. Kang ◽  
Joseph Neary
Keyword(s):  
Cerebral Ischemia ◽  
Map Kinase ◽  
Kinase Activity ◽  
Focal Cerebral Ischemia ◽  
Protein Map ◽  
Mitogen Activated Protein

Lysophosphatidylcholine activates mesangial cell PKC and MAP kinase by PLCγ-1 and tyrosine kinase-Ras pathways

1999 ◽  
Vol 277 (3) ◽  
pp. F328-F337 ◽  
Author(s):  
Babu V. Bassa ◽  
Daeyoung D. Roh ◽  
Nosratola D. Vaziri ◽  
Michael A. Kirschenbaum ◽  
Vaijinath S. Kamanna
Keyword(s):  
Tyrosine Kinase ◽  
Map Kinase ◽  
Protein Tyrosine Kinase ◽  
Kinase Activity ◽  
Mesangial Cells ◽  
Kinase Activation ◽  
Kinase C ◽  
Protein Map ◽  
Mitogen Activated Protein ◽  
Pkc Activation

Although lysophosphatidylcholine (LPC)-mediated cellular responses are attributed to the activation of protein kinase C (PKC), relatively little is known about the upstream signaling mechanisms that regulate the activation of PKC and downstream mitogen-activated protein (MAP) kinase. LPC activated p42 MAP kinase and PKC in mesangial cells. LPC-mediated MAP kinase activation was inhibited (but not completely) by PKC inhibition, suggesting additional signaling events. LPC stimulated protein tyrosine kinase (PTK) activity and induced Ras-GTP binding. LPC-induced MAP kinase activity was blocked by the PTK inhibitor genistein. Because LPC increased PTK activity, we examined the involvement of phospholipase Cγ-1 (PLCγ-1) as a key participant in LPC-induced PKC activation. LPC stimulated the phosphorylation of PLCγ-1. PTK inhibitors suppressed LPC-induced PKC activity, whereas the same had no effect on phorbol 12-myristate 13-acetate-mediated PKC activity. Other lysophospholipids [e.g., lysophosphatidylinositol and lysophosphatidic acid (LPA)] also induced MAP kinase activity, and only LPA-induced MAP kinase activation was sensitive to pertussis toxin. These results indicate that LPC-mediated PKC activation may be regulated by PTK-dependent activation of PLCγ-1, and both PKC and PTK-Ras pathways are involved in LPC-mediated downstream MAP kinase activation.

Inhibition of p42 and p44 MAP kinase does not alter smooth muscle contraction in swine carotid artery

1998 ◽  
Vol 275 (1) ◽  
pp. H131-H138 ◽  
Author(s):  
Isabelle Gorenne ◽  
Xiaoling Su ◽  
Robert S. Moreland
Keyword(s):  
Smooth Muscle ◽  
Muscle Contraction ◽  
Map Kinase ◽  
Map Kinases ◽  
Kinase Activity ◽  
Smooth Muscle Contraction ◽  
Protein Map ◽  
Mitogen Activated Protein ◽  
Kinase Phosphorylation

Caldesmon inhibits myosin ATPase activity; phosphorylation of caldesmon reverses the inhibition. The caldesmon kinase is believed to be mitogen-activated protein (MAP) kinase. MAP kinases are activated during vascular stimulation, but a cause-and-effect relationship between kinase activity and contraction has not been established. We examined the role of MAP kinase in contraction using PD-098059, an inhibitor of MAP kinase kinase (MEK). MAP kinase activity was assessed using an anti-active MAP kinase antibody and direct measurement of MAP kinase catalyzed phosphorylation of myelin basic protein, MBP-(95—98). MAP kinase phosphorylation, stimulated by histamine (50 μM) or phorbol 12,13-dibutyrate (PDBu, 0.1 μM), was inhibited by PD-098059 (100 μM). PD-098059 did not alter the sensitivity or the maximal level of force in smooth muscle stimulated by histamine or PDBu, nor did PD-098059 affect contraction of β-escin-permeabilized tissue. Our data suggest that p44 and p42 MAP kinases are not involved in regulation of vascular smooth muscle contraction. These results do not, however, preclude a role for other isoforms of the MAP kinase family.

scholarly journals Stimulation of tyrosine phosphorylation and mitogen-activated-protein (MAP) kinase activity in human SH-SY5Y neuroblastoma cells by carbachol

1993 ◽  
Vol 294 (2) ◽  
pp. 545-550 ◽  
Author(s):  
S Offermanns ◽  
E Bombien ◽  
G Schultz
Keyword(s):  
Map Kinase ◽  
Tyrosine Phosphorylation ◽  
Kinase Activity ◽  
Neuroblastoma Cells ◽  
Anion Exchange Column ◽  
Human Neuroblastoma ◽  
Protein Map ◽  
Mitogen Activated Protein ◽  
M3 Receptor ◽  
Stimulation Of

Activation of the G-protein-coupled muscarinic (M3) receptor in human neuroblastoma SH-SY5Y cells is known to lead to phosphoinositol hydrolysis and noradrenaline release. In this study, the effect of carbachol on tyrosine phosphorylation and mitogen-activated protein (MAP) kinase activity in SH-SY5Y cells was examined. Carbachol concentration-dependently induced tyrosine phosphorylation of several proteins, including one of 42 kDa. This tyrosine-phosphorylated 42 kDa protein co-eluted from a Mono Q anion-exchange column with MAP kinase activity and with immunologically detected MAP kinase. Stimulation of tyrosine phosphorylation and activation of MAP kinase were also observed after incubation of cells with phorbol 12-myristate 13-acetate (PMA) and epidermal growth factor (EGF). Down-regulation or inhibition of protein kinase C (PKC) abolished the stimulatory effects of both carbachol and PMA on MAP kinase activity, whereas EGF-stimulated MAP kinase activity remained unaffected. Thus carbachol acting through the muscarinic (M3) receptor PKC-dependently induced tyrosine phosphorylation and activation of a 42 kDa MAP kinase in SH-SY5Y cells, whereas EGF-induced MAP kinase activation occurred independently of PKC.

Genetic Analysis of rolled, Which Encodes a Drosophila Mitogen-Activated Protein Kinase

Genetics ◽  
1999 ◽  
Vol 153 (2) ◽  
pp. 763-771 ◽  
Author(s):  
Young-Mi Lim ◽  
Kimiko Nishizawa ◽  
Yoshimi Nishi ◽  
Leo Tsuda ◽  
Yoshihiro H Inoue ◽  
...  
Keyword(s):  
Map Kinase ◽  
Mitogen Activated Protein Kinase ◽  
Female Sterility ◽  
Tor Signaling ◽  
Map Kinase Cascade ◽  
Dominant Female ◽  
Protein Map ◽  
Mitogen Activated Protein ◽  
Kinase Cascade

Abstract Genetic and molecular characterization of the dominant suppressors of D-rafC110 on the second chromosome identified two gain-of-function alleles of rolled (rl), which encodes a mitogen-activated protein (MAP) kinase in Drosophila. One of the alleles, rlSu23, was found to bear the same molecular lesion as rlSem, which has been reported to be dominant female sterile. However, rlSu23 and the current stock of rlSem showed only a weak dominant female sterility. Detailed analyses of the rl mutations demonstrated moderate dominant activities of these alleles in the Torso (Tor) signaling pathway, which explains the weak dominant female sterility observed in this study. The dominant rl mutations failed to suppress the terminal class maternal-effect mutations, suggesting that activation of Rl is essential, but not sufficient, for Tor signaling. Involvement of rl in cell proliferation was also demonstrated by clonal analysis. Branching and integration of signals in the MAP kinase cascade is discussed.

scholarly journals Development of a Microsphere-Based p38α Kinase No-Wash Assay

2006 ◽  
Vol 11 (5) ◽  
pp. 528-536 ◽  
Author(s):  
Stefan Laufer ◽  
Sabine Linsenmaier
Keyword(s):  
Map Kinase ◽  
Kinase Activity ◽  
Kinase Inhibitors ◽  
Glutathione S Transferase ◽  
Drug Candidates ◽  
Protein Map ◽  
Mitogen Activated Protein ◽  
Substrate Phosphorylation ◽  
Activating Transcription Factor ◽  
P38α Kinase

A nonradioactive, microsphere-based, no-wash assay for the measurement of p38[.alpha] mitogen-activated protein (MAP) kinase activity was established. In this assay, a glutathione-S-transferase activating transcription factor 2 (amino acids 19-96) fusion protein (GST-ATF-2) was used as substrate for p38[.alpha] MAP kinase. The assay involves immobilization of GST-ATF-2 on glutathione-microspheres (GSH-microspheres), addition of test solution containing p38[.alpha] MAP kinase and test compounds, and measurement of the respective substrate phosphorylation with the aid of a bi-phospho-specific antibody. The optimization of test conditions is described in this article. With an optimized standard protocol, p38[.alpha] MAP kinase inhibitors were investigated and IC50 values were compared to those derived using known assays. This assay might be useful in testing drug candidates.

scholarly journals Characterization of a mitogen‐activated protein (MAP) kinase from Plasmodium falciparum

1997 ◽  
Vol 23 (1) ◽  
pp. 151-159 ◽  
Author(s):  
Ralph Graeser ◽  
Patrick Ku¨ry ◽  
Richard M. Franklin ◽  
Barbara Kappes
Keyword(s):  
Plasmodium Falciparum ◽  
Map Kinase ◽  
Protein Map ◽  
Mitogen Activated Protein
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