| Literature DB >> 20043236 |
Guillermo Bodega1, Sergio Ciordia, Isabel Suárez, Luis Andrés López-Fernández, Enrique Vacas, Gonzalo Sánchez-Tejeda, María Amparo Albert, Silvia Juárez, Juan Pablo Albar, Benjamín Fernández.
Abstract
Mitogen-activated protein kinases (MAPKs) are a superfamily of cytoplasmic serine/threonine kinases that transduce many types of extracellular stimuli into cellular responses. p38MAPK is a member of this family with its active form in a diphosphorylated state (p38MAPKdiP). Two strong anti-p38MAPKdiP immunoreactive bands (apparent molecular weight 38 and 34 kDa) were detected by Western blotting in cultured astrocytes. Using a specific antibody and employing immunoprecipitation procedures and SELDI-TOF analysis, the 34 kDa band was found to correspond to Mxi2, a splice variant of p38MAPK; cultured astrocytes therefore express Mxi2. Separate protein extractions of different subcellular fractions, and fluorescent immunovisualisation employing confocal microscopy, showed Mxi2 to have a non-nuclear, cytosolic distribution in the studied cells. ERK1/2, protein whose intracellular distribution is influenced by Mxi2, showed the same cytoplasmic pattern than Mxi2.Entities:
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Year: 2009 PMID: 20043236 DOI: 10.1007/s10735-009-9248-8
Source DB: PubMed Journal: J Mol Histol ISSN: 1567-2379 Impact factor: 2.611