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Kinase p38 MAPK

There are numerous data that peroxynitrite is involved in cell death and tissue injuries in many clinical conditions. An important mechanism underlying peroxynitrite toxicity is the reaction of tyrosine nitration. Tyrosine nitration inactivates certain enzymes, as was postulated for prostacyclin (PGI2) synthase (M14), cytochrome P450 2B1 (RIO), tyrosine hydroxylase (A 14), and MnSOD (Yl). Moreover, nitration blocks tyrosine phosphorylation, and thus interferes with the tyrosine kinase signaling pathways (K18). The peroxynitrite treatment of rat liver epithelial cells stimulates mitogen-activated protein kinases p38 MAPK, JNK1/2, and ERK1/2 the mechanism of this effect awaits elucidation (S9). [Pg.216]

The abnormal phosphorylation of tau associated with AD may be related to either an increase in kinase activity (glycogen synthase kinase 3P, cyclin-dependent kinase-5, p42/44 MAP kinase, p38 MAPK, stress-activated protein kinases, mitotic protein kinases) or a decrease in phosphatase activity (protein phosphatases 1, 2a, 2b), suggesting soluble tau as a cause of neuronal degeneration (Buee et al., 2000 Tian and Wang, 2002 Chen et al., 2008 Liu et al., 2008 Yang et al., 2008 Zhou et al., 2008a). [Pg.613]

Second, oleanolic acid (43) could induce their early phosphorylation of two such as p38 mitogen-activated protein kinase (p38 MAPK) of) a class of mitogen-activated protein kinases that are responsive to the stress stimuli such as cytokines, ultraviolet irradiation, heat shock, osmotic shock, cell differentiation, apoptosis and autophagy and p42/44 mitogen-activated protein kinase (p42/44 MAPK) [31] that regulated by p53 mitogen-activated protein kinase and nitric oxide in human pulmonary arterial smooth muscle cells. However, oleanolic acid (43) could not induce the early phosphorylation of c-Jun N-terminal kinase-1 (JNK-1) [32] that mediate both survival and apoptosis of tumor cells [33]. [Pg.88]

Roux, P. P., and Blenis, J. (2004). ERK and p38 MAPK-activated protein kinases A family of protein kinases with diverse biological functions. Microbiol. Mol. Biol. Rev. 68, 320-344. [Pg.174]

A third group of MAPKs are p38 kinases, of which there are four subtypes a, [3, y, and 8. P38 MAPKs are activated by many stimuli including hormones, ligands for G-protein-coupled receptors and stresses [13,17]. P38 MAPK has been implicated in the pathological changes accompanying inflammatory and apoptotic processes of various cell types, including neurons [17] (see Ch. 35 for... [Pg.398]

Conversely, the SAPK/JNK cascade, which is closely associated with apoptosis, is activated by sphingosine (Pyne et al, 1996). Exogenous sphingosine also activates caspase-7in a Bcl-x(L)-sensitive manner wha-eas caspase-8 was unaffected (Nava et al, 2000 Cuvillier et al, 2001). hi addition, sphingosine stimulates p38 MAPK in osteoblast-like cells (Kozawa et al, 2000) but not in oligodendrocytes where is produces lysis (Hida et al, 1999). p38 MAPK is up-stream of MAPKAP kinase-2 and the... [Pg.251]

Increased p42/p44 MAPK Increased c-jun and c-fos Increased non-receptor tyrosine kinase activity-increased phospholipase C Increased p38 MAPK Reduced cAMP Increased NO and NOS... [Pg.253]

In an in vitro model, exposure of lymphoma cells to rituximab resulted in the activation of the Src-family of protein tyrosine kinases (13), leading to the phosphorylation of PLCy2, which induces calcium influx and activates caspase 3, resulting in promotion of apoptotic cell death (8,14). Another in vitro model showed that exposure to rituximab resulted in the sustained phosphorylation of p38-MAPK, JNK, and ERK kinases... [Pg.206]

Blanc, A., N.R. Pandey, and A.K. Srivastava. 2004. Distinct roles of Ca2+, calmodulin, and protein kinase C in Oj-induced activation of ERK1/2, p38 MAPK, and protein kinase B signaling in vascular smooth muscle cells. Antioxid. Redox Signal. 6 353-366. [Pg.187]


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See also in sourсe #XX -- [ Pg.68 , Pg.70 ]




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MAPKs

P38 MAPK

P38 kinase

P38 mitogen-activated protein kinase MAPK)

P38 mitogen-activated protein kinase MAPK) pathway

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