Analysis of VEGF-Mediated ERK5 Activity in Endothelial Cells

Methods Mol Biol. 2015:1332:133-42. doi: 10.1007/978-1-4939-2917-7_9.

Abstract

Extracellular signal-regulated kinase 5 (ERK5), also known as big MAPK (BMK1), is the most recently identified member of the mitogen-activated kinase pathway. It is ubiquitously expressed in mammalian cells and is activated by a number of growth factors. Gene knockout studies in mice have shown a critical role for ERK5 cardiovascular development and vascular integrity. Current methods to detect ERK5 activation in cells have relied on in vitro kinase assays and more recently phospho-specific antibodies. However, antibodies produced against phosphorylated proteins can often yield inconsistent data. Phos-tag™ Acrylamide is a reagent that enables specific tagging of phosphorylated proteins, resulting in retarded mobility and a distinct upward band shift from the non-phosphorylated protein following SDS-PAGE. Here, we describe the details of Phosphate affinity SDS-PAGE of ERK5 using acrylamide-pendant Phos-tag™.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Blotting, Western
  • Endothelial Cells / metabolism*
  • Enzyme Activation
  • Humans
  • Mitogen-Activated Protein Kinase 7 / metabolism*
  • Vascular Endothelial Growth Factors / metabolism*

Substances

  • Vascular Endothelial Growth Factors
  • Mitogen-Activated Protein Kinase 7