Research Paper Volume 15, Issue 23 pp 14019—14038

Figure 3. Interaction of co-chaperone TPR domain of CHIP (CHIP-TPR) with IGF1Rβ. (A) Schematic representation of CHIP and IGF1Rβ interaction. The lower figure indicates the CHIP wild-type and point mutation plasmids. (B) Cell viability rate was measured by MTT assay after transfection of HA-vector, HA-CHIP, and mutants of HA-CHIP (K30A, and H260Q) for 24 h. (C) The docking analysis showed the interaction between CHIP-TPR domain and IGF1Rβ. (D) rADSCs were transfected by HA-vector, HA-CHIP wild-type, and HA-CHIP two mutants (K30A, and H260Q) for 24 h and analyzed by Western blotting. (E) Co-immunoprecipitation (co-IP) analysis was performed by using rADSCs after transfection of HA-vector, HA-CHIP wild-type, and HA-CHIP-K30A for 24 h. (F, G) The apoptotic cells were analyzed by using a flow cytometer. (H) rADSCs were knocked down with siCHIP for 24 h and analyzed by Western blotting. (N = 3; ^*p < 0.05; ^**p < 0.01 indicate significant differences).