stellettin-a and Prostatic-Neoplasms

stellettin-a has been researched along with Prostatic-Neoplasms* in 1 studies

Other Studies

1 other study(ies) available for stellettin-a and Prostatic-Neoplasms

Article	Year
Stellettin A induces oxidative stress and apoptosis in HL-60 human leukemia and LNCaP prostate cancer cell lines. Journal of natural products, 2006, Volume: 69, Issue:6 The present study has demonstrated a differential cytotoxicity of stellettin A (1) between human leukemia HL-60 cells (IC50 0.4 microg/mL) and human prostate cancer LNCaP cells (IC50 120 microg/mL). Treatment of cells with 1 revealed the activation of NADPH oxidase, the dramatic generation of reactive oxygen species, and the dissipation of mitochondrial membrane potentials, with HL-60 cells being more sensitive than LNCaP cells by an order of magnitude. Immunoblotting analysis further demonstrated a stronger upregulation of the apoptosis marker proteins, FasL and caspase-3, in HL-60 cells, and pretreatment of cells with antisense oligonucleotide for caspase-3 abolished apoptosis. All available evidence suggests that 1 induces oxidative cell death through a FasL-caspase-3-apoptotic pathway. Topics: Animals; Apoptosis; Caspase 3; Caspases; Fas Ligand Protein; HL-60 Cells; Humans; Male; Membrane Glycoproteins; Membrane Potentials; Mitochondria; Oxidative Stress; Porifera; Prostatic Neoplasms; Triterpenes; Tumor Cells, Cultured; Tumor Necrosis Factors	2006

Article

Year

Stellettin A induces oxidative stress and apoptosis in HL-60 human leukemia and LNCaP prostate cancer cell lines.

Journal of natural products, 2006, Volume: 69, Issue:6

The present study has demonstrated a differential cytotoxicity of stellettin A (1) between human leukemia HL-60 cells (IC50 0.4 microg/mL) and human prostate cancer LNCaP cells (IC50 120 microg/mL). Treatment of cells with 1 revealed the activation of NADPH oxidase, the dramatic generation of reactive oxygen species, and the dissipation of mitochondrial membrane potentials, with HL-60 cells being more sensitive than LNCaP cells by an order of magnitude. Immunoblotting analysis further demonstrated a stronger upregulation of the apoptosis marker proteins, FasL and caspase-3, in HL-60 cells, and pretreatment of cells with antisense oligonucleotide for caspase-3 abolished apoptosis. All available evidence suggests that 1 induces oxidative cell death through a FasL-caspase-3-apoptotic pathway.

Topics: Animals; Apoptosis; Caspase 3; Caspases; Fas Ligand Protein; HL-60 Cells; Humans; Male; Membrane Glycoproteins; Membrane Potentials; Mitochondria; Oxidative Stress; Porifera; Prostatic Neoplasms; Triterpenes; Tumor Cells, Cultured; Tumor Necrosis Factors

2006