Latest Publications

@article{vaculova_different_2006,

title = {Different modulation of TRAIL-induced apoptosis by inhibition of pro-survival pathways in TRAIL-sensitive and TRAIL-resistant colon cancer cells.},

author = {Alena Vaculová and Jirina Hofmanová and Karel Soucek and Alois Kozubík},

doi = {10.1016/j.febslet.2006.11.004},

issn = {0014-5793},

year  = {2006},

date = {2006-12-01},

journal = {FEBS letters},

volume = {580},

number = {28-29},

pages = {6565–6569},

abstract = {Epithelial cells can be manipulated to undergo apoptosis depending on the balance between pro-survival and apoptotic signals. We showed that TRAIL-induced apoptosis may be differentially regulated by inhibitors of MEK ERK (U0126) or PI3K/Akt (LY294002) pathway in TRAIL-sensitive (HT-29) and TRAIL-resistant (SW620) human epithelial colon cancer cells. U0126 or LY294002 significantly enhanced TRAIL-induced apoptosis in HT-29 cells, but not in SW620 cells. We report a different regulation of the level of an anti-apoptotic Mcl-1 protein under MEK/ERK or PI3K/Akt pathway inhibition and suggest the mechanisms involved. A special attention was paid to the role of the ERK1/2, Akt, and glycogen synthase kinase 3beta.},

note = {Place: England},

keywords = {Apoptosis/*drug effects, Caspase 8/metabolism, Cell Survival/drug effects, Colonic Neoplasms/*pathology, Enzyme Activation/drug effects, Enzyme Inhibitors/pharmacology, Extracellular Signal-Regulated MAP Kinases/antagonists & inhibitors, Glycogen Synthase Kinase 3 beta, Glycogen Synthase Kinase 3/metabolism, HT29 Cells, Humans, Keratin-18/metabolism, Mitogen-Activated Protein Kinase 1/antagonists & inhibitors, Mitogen-Activated Protein Kinase 3/antagonists & inhibitors, Mitogen-Activated Protein Kinase Kinases/antagonists & inhibitors, Myeloid Cell Leukemia Sequence 1 Protein, Neoplasm Proteins/metabolism, Phosphoinositide-3 Kinase Inhibitors, Phosphorylation/drug effects, Poly(ADP-ribose) Polymerases/metabolism, Proto-Oncogene Proteins c-akt/antagonists & inhibitors, Proto-Oncogene Proteins c-bcl-2/metabolism, TNF-Related Apoptosis-Inducing Ligand/*pharmacology},

pubstate = {published},

tppubtype = {article}

}

@article{vondracek_dimethyl_2006,

title = {Dimethyl sulfoxide potentiates death receptor-mediated apoptosis in the human myeloid leukemia U937 cell line through enhancement of mitochondrial membrane depolarization.},

author = {Jan Vondrácek and Karel Soucek and Michael A. Sheard and Katerina Chramostová and Zdenek Andrysík and Jirina Hofmanová and Alois Kozubík},

doi = {10.1016/j.leukres.2005.05.016},

issn = {0145-2126},

year  = {2006},

date = {2006-01-01},

journal = {Leukemia research},

volume = {30},

number = {1},

pages = {81–89},

abstract = {Dimethyl sulfoxide (DMSO) is a widely used prototypical chemical inducer of cell differentiation. In the present study, the effects of DMSO on susceptibility of human myeloid leukemia U937 cells towards ligation of distinct death receptors (DRs) were investigated. DMSO sensitized cells towards induction of apoptosis by anti-Fas antibody, tumour necrosis factor-alpha or Apo2 ligand/TNF-related apoptosis-inducing ligand (TRAIL). Apart from increasing Fas levels, DMSO did not affect expression of proteins in death signal transduction, such as Bcl-2 family proteins, FADD, caspase-3 and -8, the inhibitor of apoptosis proteins (IAPs) or cFLIP(L). However, DMSO significantly potentiated mitochondrial membrane depolarization, suggesting that this mechanism might be involved in sensitisation of myeloid cells to DR-mediated apoptosis.},

note = {Place: England},

keywords = {Adaptor Proteins, Apoptosis Regulatory Proteins/*metabolism, Apoptosis/*drug effects, CASP8 and FADD-Like Apoptosis Regulating Protein, Caspase 3, Caspase 8, Caspases/metabolism, Cryoprotective Agents/*pharmacology, Dimethyl Sulfoxide/*pharmacology, fas Receptor/*metabolism, Fas-Associated Death Domain Protein, Humans, Intracellular Signaling Peptides and Proteins, Leukemia, Membrane Glycoproteins/*metabolism, Mitochondria/metabolism/pathology, Mitochondrial Membranes/*metabolism/pathology, Myeloid/*metabolism/pathology, Proto-Oncogene Proteins c-bcl-2/metabolism, Signal Transducing/metabolism, TNF-Related Apoptosis-Inducing Ligand, Tumor Necrosis Factor-alpha/*metabolism, U937 Cells},

pubstate = {published},

tppubtype = {article}

}

@article{vaculova_ethanol_2004,

title = {Ethanol acts as a potent agent sensitizing colon cancer cells to the TRAIL-induced apoptosis.},

author = {Alena Vaculová and Jirina Hofmanová and Karel Soucek and Ladislav Andera and Alois Kozubík},

doi = {10.1016/j.febslet.2004.10.013},

issn = {0014-5793},

year  = {2004},

date = {2004-11-01},

journal = {FEBS letters},

volume = {577},

number = {1-2},

pages = {309–313},

abstract = {Identification of mechanisms of modulation of the TNF-related apoptosis-inducing ligand (TRAIL)-induced apoptosis is important for its potential use in anticancer therapy. Ethanol can induce cell death in vitro and in vivo by different signalling pathways. Its effect in combination with death ligands is unknown. We investigated how ethanol modulates the effects of TRAIL in colon cancer cells. After combined TRAIL and ethanol treatment, a potentiation of caspase-8, -9, -3 activation, a proapoptotic Bid protein cleavage, a decrease of mitochondrial membrane potential, a complete poly(ADP)ribose polymerase cleavage, and disappearance of antiapoptotic Mcl-1 protein were demonstrated. Ethanol acts as a potent agent sensitizing colon cancer cells to TRAIL-induced apoptosis.},

note = {Place: England},

keywords = {Apoptosis Regulatory Proteins, Apoptosis/*drug effects/physiology, BH3 Interacting Domain Death Agonist Protein, Blotting, Carrier Proteins/metabolism, Caspases/metabolism, Colonic Neoplasms/enzymology/metabolism/*pathology, Ethanol/*pharmacology, HT29 Cells, Humans, Membrane Glycoproteins/*physiology, Myeloid Cell Leukemia Sequence 1 Protein, Neoplasm Proteins/metabolism, Proto-Oncogene Proteins c-bcl-2/metabolism, TNF-Related Apoptosis-Inducing Ligand, Tumor Necrosis Factor-alpha/*physiology, Western},

pubstate = {published},

tppubtype = {article}

}