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. Author manuscript; available in PMC: 2008 Aug 18.
Published in final edited form as: J Proteome Res. 2006 Jul;5(7):1636–1646. doi: 10.1021/pr0502469

Figure 6. Interaction of Akt with Chaperone Proteins in Mesangial Cells.

Figure 6

To determine if Akt interacts with chaperone proteins in mesangial cells, agarose-conjugated anti-Akt antibody was used to immunoprecipitate Akt from lysate of mesangial cells that were either unstimulated or stimulated with PDGF for 10 and 30 minutes. The precipitated complex was eluted from the beads, separated by SDS-PAGE and proteins transferred to nitrocellulose. The presence of chaperone proteins in the complex was determined by immunobloting for each specific chaperone. The figure shows that Akt was associated with Grp78 and Hsp70 in unstimulated mesangial cells (A). Stimulation of mesangial cells with PDGF resulted in increased binding of Grp78 and Hps70 (A). PDGF Stimulation of mesangial cells for up to 30 minutes did not alter expression of Grp78 or Hsp70 (B).