D. Monolith Hall, Philadelphia, PA 19106, USA; 2Department of Molecular Genetics and Microbiology, Kimmel Cancer Institute, Thomas. D. Monolith Hall, Philadelphia, PA 19106, USA; 3Department of Molecular Medicine, Kimmel Cancer Institute, Thomas. D. Monolith Hall, Philadelphia, PA 19106, USA, and 4School of Population Health, Albert Einstein College of Medicine, Bronx, New York 12458, USA The purpose of this study was to identify possible inhibitors for the activation of the protein kinase B (AKT) on dot of the cancer cell membrane in vitro. We found that the anti-matrix protein kinase B (AKT) antagonist and tyrosine kinase inhibitor, B2, which inhibits the growth of a range of cancers by modulating the apoptotic pathway, is able to inhibit the growth of cancer cell membranes, including that of pancreatic lipoma, cervical, and colorectal cancer. We also demonstrate that B2 inhibits the initiation of migration in vitro, which would explain why it prevents pancreatic malignancies by inhibiting malignant cell migration. To determine whether B2 prevents the growth of pancreatic cancer cells by directly inducing apoptosis, we assessed whether the anti-matrix protein kinase B antagonist, B2 was able to activate the protein kinase C (PC) complex and phosphorylate the MAP kinase (ERK1/2) to induce apoptosis. In addition, we determined the effects of B2 on the migration of pancreatic cancer cells, including pancreatic cancer cells migrating through the blood vessels, and we tested the effects of B2 on the effects of tumor necrosis factor alpha (TNF) on pancreatic cancer migration. B2 reduced the migration of pancreatic cancer cells in high concentration and was more effective than TNF on the growth and migration of pancreatic malignant cells. Treatment of pancreatic cancer cells with the cancer necrosis virus (CV) and cyclophosphamide (CP; 3 kg/ml) increased the activity of apoptosis-inducing factor (AIF; 100 km) and of the phosphorodiamidate morphology isomerization inhibitor 4D-MPP (15 km; 1 SL/200 SL) and of cyclophosphamide; therefore, B2 was an efficient inhibitor of the apoptosis.
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NIH Public Access Author Manuscript Development. Author manuscript; available in PMC 2009 June 8. NIH-PA Author Manuscript Published in final edited form as: Development. 2003 February ; 130(4): 741
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