ABSTRACT
 The purpose of this study was to isolate and test its cytotoxic activity starting from extract fraction compound, then carried out molecular docking confirm the potential biological ligands (vocangine, vobtusine, vobtusine lactone) against inhibition proteins (Bcl-2, Bcl-xL, Mcl-1), activation protein Bax apoptotic execution Caspase-3. This research is an experimental quantitativ...

Gustafsson, Åsa B., and Roberta A. Gottlieb. Bcl-2 family members and apoptosis, taken to heart. Am J Physiol Cell Physiol 292: C45–C51, 2007. First published August 30, 2006; doi:10.1152/ajpcell.00229.2006.—Loss of myocardial cells via apoptosis has been observed in many cardiovascular diseases and has been shown to contribute to the initiation and progression of heart failure. The Bcl-2 famil...

Release of apoptogenic proteins such as cytochrome c from mitochondria is regulated by pro- and anti-apoptotic Bcl-2 family proteins, with pro-apoptotic BH3-only proteins activating Bax and Bak. Current models assume that apoptosis induction occurs via the binding and inactivation of anti-apoptotic Bcl-2 proteins by BH3-only proteins or by direct binding to Bax. Here, we analyze apoptosis induc...

Radiotherapy plays an important role in the treatment of hepatocellular carcinoma (HCC). Cyclin G1 is a novel member cyclin family, and it abnormally expressed HCC. In this study we investigated radiotherapy HCC cells. The expression was silenced by transfection G1-siRNA into HepG2 cells Huh7 cells, mRNA protein measured qRT-PCR Western blot analysis. proliferation analyzed using MTT assay, rad...

In the intracellular death program, hetero- and homodimerization of different anti- and pro-apoptotic Bcl-2-related proteins are critical in the determination of cell fate. From a rat ovarian fusion cDNA library, we isolated a new pro-apoptotic Bcl-2 gene, Bcl-2-related ovarian killer (Bok). Bok had conserved Bcl-2 homology (BH) domains 1, 2, and 3 and a C-terminal transmembrane region present ...

BH3 only proteins trigger cell death by interacting with pro- and anti-apoptotic members of the BCL-2 family of proteins. Here we report that BH3 peptides corresponding to the death domain of BH3-only proteins, which bind all the pro-survival BCL-2 family proteins, induce cell death in the absence of BAX and BAK. The BH3 peptides did not cause the release of cytochrome c from isolated mitochond...

Bcl-2 family proteins regulate the release of proteins like cytochrome c from mitochondria during apoptosis. We used cell-free systems and ultimately a vesicular reconstitution from defined molecules to show that outer membrane permeabilization by Bcl-2 family proteins requires neither the mitochondrial matrix, the inner membrane, nor other proteins. Bid, or its BH3-domain peptide, activated mo...