MG-132

PubMed: 26722260      Oncol Lett

(C) K562 cells were treated with SAHA (1 µM or 2 µM), MG-132 (400 nM) or SAHA plus MG-132 (400 nM) for 24 h. Western blot analysis was performed, using antibodies against Bcr-Abl, Ac-histone H3, caspase-3 and PARP. β-actin was used as a loading control. (D) K562G cells were treated with SAHA (1 µM or 2 µM), MG-132 (200 nM) or SAHA plus MG-132 (200 nM) for 24 h. Western blot analysis was performed, using antibodies against Bcr-Abl, Ac-histone H3, caspase-3 and PARP. β-actin was used as a loading control. Representative blots from three independent experiments are shown.

PubMed: 26722260      Oncol Lett

(C) K562 cells were treated with SAHA (1 µM or 2 µM), MG-132 (400 nM) or SAHA plus MG-132 (400 nM) for 24 h. Western blot analysis was performed, using antibodies against Bcr-Abl, Ac-histone H3, caspase-3 and PARP. β-actin was used as a loading control. (D) K562G cells were treated with SAHA (1 µM or 2 µM), MG-132 (200 nM) or SAHA plus MG-132 (200 nM) for 24 h. Western blot analysis was performed, using antibodies against Bcr-Abl, Ac-histone H3, caspase-3 and PARP. β-actin was used as a loading control. Representative blots from three independent experiments are shown.

PubMed: 26722260      Oncol Lett

(C) K562 cells were treated with SAHA (1 µM or 2 µM), MG-132 (400 nM) or SAHA plus MG-132 (400 nM) for 24 h. Western blot analysis was performed, using antibodies against Bcr-Abl, Ac-histone H3, caspase-3 and PARP. β-actin was used as a loading control. (D) K562G cells were treated with SAHA (1 µM or 2 µM), MG-132 (200 nM) or SAHA plus MG-132 (200 nM) for 24 h. Western blot analysis was performed, using antibodies against Bcr-Abl, Ac-histone H3, caspase-3 and PARP. β-actin was used as a loading control. Representative blots from three independent experiments are shown.

PubMed: 26722260      Oncol Lett

(C) K562 cells were treated with SAHA (1 µM or 2 µM), MG-132 (400 nM) or SAHA plus MG-132 (400 nM) for 24 h. Western blot analysis was performed, using antibodies against Bcr-Abl, Ac-histone H3, caspase-3 and PARP. β-actin was used as a loading control. (D) K562G cells were treated with SAHA (1 µM or 2 µM), MG-132 (200 nM) or SAHA plus MG-132 (200 nM) for 24 h. Western blot analysis was performed, using antibodies against Bcr-Abl, Ac-histone H3, caspase-3 and PARP. β-actin was used as a loading control. Representative blots from three independent experiments are shown.

PubMed: 19765735      J Surg Res

MG-132 decreases the levels of ASCL1 and CgA in carcinoid cancer cells. Pulmonary (NCI-H727) (A) carcinoid cancer cells were treated with MG-132 (0 to 4µM) for 48 hours and cell lysates were analyzed by Western blotting for the expression of ASCL1 and CgA. Treatment with MG-132 results in a dose dependent inhibition of the two neuroendocrine tumor markers. Analysis for GAPDH confirmed equal loading.

PubMed: 19765735      J Surg Res

MG-132 decreases the levels of ASCL1 and CgA in carcinoid cancer cells. Pulmonary (NCI-H727) (A) carcinoid cancer cells were treated with MG-132 (0 to 4µM) for 48 hours and cell lysates were analyzed by Western blotting for the expression of ASCL1 and CgA. Treatment with MG-132 results in a dose dependent inhibition of the two neuroendocrine tumor markers. Analysis for GAPDH confirmed equal loading.

PubMed: 23604711      Am J Physiol Heart Circ Physiol

MG-132 stimulates Nrf2 and HO-1 protein expression in HAECs in a time-dependent fashion. Cells were treated with MG-132 (2 μM) for various times (0–24 h), and Nrf2 and HO-1 protein were quantified by scanning densitometry, normalized with respect to β-actin, and expressed relative to those of control cells.

PubMed: 23604711      Am J Physiol Heart Circ Physiol

MG-132 stimulates Nrf2 and HO-1 protein expression in HAECs in a time-dependent fashion. Cells were treated with MG-132 (2 μM) for various times (0–24 h), and Nrf2 and HO-1 protein were quantified by scanning densitometry, normalized with respect to β-actin, and expressed relative to those of control cells.

PubMed: 20557369      Hepatol Res

Proteasome inhibitor induces Bak activation. Cells were treated with either vehicle or MG-132 at 10 µmol/L for 12 hours and were subjected to Bak immunofluorescence study using antiserum specific for the N terminus of Bak. Upon Bak activation, this epitope is no longer masked within the protein and becomes available for antibody binding upon Bak conformational change.

PubMed: 22525330      Int J Biochem Cell Biol

Confocal images of bC2GnT-M and NMIIA in cells treated with DMSO (D) or MG-132 (E).

PubMed: 20065032      Mol Cell Biol

COS-7 cells were transfected with wild-type or TPR-modified AGS3 (AGS3-TPR [M1 to E470] or AGS3-GPR [E470 to S650]) in pEGFP-N1. Thirty-six hours after transfection, cells were incubated with MG 132 (10 μM) for 12 h, and then the cells were processed for immunofluorescence microscopy. The images presented are representative of 2 to 10 separate transfections.

PubMed: 20557369      Hepatol Res

LX-2 cells were incubated for 24 hours in the presence of increasing concentrations of MG-132 (0, 2.5, 5, 10 µmol/L) and in the presence of the pan-caspase inhibitor QVD at 5 µmol/L for 24 hours. MG-132 and QVD were prepared in DMSO as a vehicle. All data were expressed as mean ± standard error from three individual experiments. * p < 0.01 (10 µmol/L MG-132 treated cells vs. 10 µmol/L MG-132 plus QVD treated cells)

PubMed: 26137056      Oncol Lett

The proteasome inhibitor MG-132 significantly decreased the cell viability in EC9706 cells in a dose- and time-dependent manner.

PubMed: 19765735      J Surg Res

MG-132 significantly inhibits growth of carcinoid tumor cells in vitro. Pulmonary (NCI-H727) and GI (BON) carcinoid tumor cells were treated with MG-132 at the indicated concentrations (0 to 4µM) for up to 6 days and cell viability was measured every 2 days with the MTT assay (P<0.001). The results show that MG-132 leads to the suppression cellular proliferation in NCI-H727 (A) and BON (B) cells. (OD, optical density)

PubMed: 11160671      J Virol

ELISA of IL-8 from supernatant of eTat cells. eTat cells were blocked with Hu (2 mM) and released. MG-132 (50 μM) was added at the time of release. The supernatant was collected at 3 h postrelease and analyzed for IL-8 protein using ELISA. The result shown is representative of three independent experiments ± standard deviation. 

PubMed: 22606244      PLoS One

LPS-primed WT BMDM were incubated in control medium or medium containing 10 ng/ml ricin or 25 µg/ml cycloheximide for 4 h. MG-132 (30 µM) or Bortezimib (0.5 µM) was included as indicated. Secreted IL-1ß was measured by ELISA in triplicate wells.