Disease relevance of Mapkapk2

• Co-induction of alphaB-crystallin and MAPKAPK-2 in astrocytes in the penumbra after transient focal cerebral ischemia [1].
• In addition, levels of MAPKAPK-2, one of the alpha-BC upstream kinases, and its phosphorylated form were upregulated gradually and peaked 4 days after ischemia/reperfusion injury [1].

High impact information on Mapkapk2

• The activity of p38 kinase was inhibited by SB203580, a member of the novel class of cytokine suppressive anti-inflammatory drugs (CSAIDs), as revealed by blocked activation of the downstream kinase, MAP kinase-activated protein kinase-2 [2].
• Heat shock protein (HSP27) is a cytoskeleton-interacting substrate of MAPKAPK-2 [3].
• Xe-PC induced phosphorylation of MAPKAPK-2 (control 1.0 +/- 0.2 vs Xe-PC 1.6 +/- 0.1, P < 0.05) and HSP27 (control 5.0 +/- 0.5 vs Xe-PC 9.8 +/- 1.0, P < 0.001) [4].
• In addition, angiotensin II stimulates the association of MAPKAPK-2 with the Akt-p38 MAPK complex, and an in vitro kinase assay shows that MAPKAPK-2 immunoprecipitates of VSMC lysates phosphorylate recombinant Akt in an angiotensin II-inducible manner [5].
• Taken together, the results clearly demonstrate that MAPKAPK-2 may function as a vimentin kinase in vitro and in vivo [6].

Biological context of Mapkapk2

• Finally, intracellular delivery of a MAPKAPK-2 peptide inhibitor blocks Akt phosphorylation on Ser(473) [5].

Anatomical context of Mapkapk2

• Role of p38 MAPK and MAPKAPK-2 in angiotensin II-induced Akt activation in vascular smooth muscle cells [5].
• Mechanisms of xenon- and isoflurane-induced preconditioning - a potential link to the cytoskeleton via the MAPKAPK-2/HSP27 pathway [4].
• These findings shed new light on the possible involvement of the p38MAPK signaling cascade, via MAPKAPK-2, in the maintenance of integrity and possible physiological regulation of intermediate filaments [6].
• The present study was undertaken to examine the localization of MAPKAPK-2 in the rat TMJ by immunocytochemical techniques [7].
• In addition to cytoplasmic localization, MAPKAPK-2 immunoreactions were found in the nucleus of some synovial lining cells, cells in the articular disk, and chondrocytes [7].

Associations of Mapkapk2 with chemical compounds

• Angiotensin II-induced phosphorylation of MAPKAPK-2 is also attenuated by SB-203580, as well as by inhibitors of ROS [5].
• Inhibition of p38 MAP kinase by treatment with the p38 MAP kinase inhibitor SB239063 (800 ppm in standard rat chow) reduced MAPKAPK-2 phosphorylation, preserved acetylcholine-induced relaxation (Rmax: 80+/-4%, p<0.01), and reduced vascular superoxide formation [8].

Enzymatic interactions of Mapkapk2

• Comparative analysis of tryptic phosphopeptide maps also indicates that corresponding phosphopeptides emerged in vimentin from OA-treated cells and were phosphorylated by MAPKAPK-2 [6].

Regulatory relationships of Mapkapk2

• In vitro kinase assays, cell labeling and immunoprecipitation showed activation of signaling pathways downstream of p38 stress-activated kinase as revealed by an increase in phosphorylation of MAPKAPK-2/3 kinases and HSP27 [9].
• Current observations imply the presence of the phosphorylation of Hsp25 via activated MAPKAPK-2 in the cytoplasm [7].

Analytical, diagnostic and therapeutic context of Mapkapk2

• Phosphorylation of MAPKAPK-2 and HSP27 were assessed by Western blot [4].
• Immunocytochemistry for MAPKAPK-2 showed an intense immunoreaction in the cytoplasm of the synovial lining cells, the endothelial cells, and the fibroblasts in the synovial membrane of the rat TMJ [7].
• Furthermore, confocal microscopy with double staining was employed to demonstrate the colocalization of MAPKAPK-2 and Hsp25 [7].

References