n-caproylsphingosine and Neuroectodermal-Tumors--Primitive--Peripheral

n-caproylsphingosine has been researched along with Neuroectodermal-Tumors--Primitive--Peripheral* in 1 studies

Other Studies

1 other study(ies) available for n-caproylsphingosine and Neuroectodermal-Tumors--Primitive--Peripheral

Article	Year
Ceramide-induced apoptosis is mediated by caspase activation independently from retinoblastoma protein post-translational modification. Biochemical and biophysical research communications, 1998, Feb-24, Volume: 243, Issue:3 Recent evidence suggests that untimely retinoblastoma protein (RB) dephosphorylation and/or proteolytic degradation might provide key events down-stream cysteine protease (caspase) activation in apoptosis induction. We have dealt with this issue by studying apoptosis induced by N-hexanoylsphingosine (C6-Cer) in CHP-100 human neuroepithelioma cells, maintained in complete growth medium. We report that C6-Cer-induced apoptosis occurred predominantly in G1/S phases of the cycle and was associated with RB dephosphorylation, in the setting of negligible Bcl-2 expression. Apoptosis was also associated with poly(ADP-ribose) polymerase (PARP) cleavage, thus indicating activation of CPP32/Yama/apopain (caspase-3); however, while the tripeptide caspase inhibitor Z-Val-Ala-DL-Asp-fluoromethylketone was able to prevent both C6-Cer-induced PARP cleavage and apoptosis, it was ineffective in preventing RB dephosphorylation. Moreover proteolytic RB cleavage occurred only to a marginal extent after C6-Cer treatment. These results indicate that apoptosis induced by ceramide in CHP-100 cells is caspase-mediated, but RB post-translational modification does not provide a key step, downstream caspase activation, in apoptosis execution. Topics: Apoptosis; Blotting, Western; Caspase 3; Caspases; Ceramides; Cysteine Endopeptidases; Enzyme Activation; Flow Cytometry; G1 Phase; Humans; Neuroectodermal Tumors, Primitive, Peripheral; Phosphorylation; Poly(ADP-ribose) Polymerases; Protein Processing, Post-Translational; Retinoblastoma Protein; S Phase; Tumor Cells, Cultured	1998

Article

Year

Ceramide-induced apoptosis is mediated by caspase activation independently from retinoblastoma protein post-translational modification.

Biochemical and biophysical research communications, 1998, Feb-24, Volume: 243, Issue:3

Recent evidence suggests that untimely retinoblastoma protein (RB) dephosphorylation and/or proteolytic degradation might provide key events down-stream cysteine protease (caspase) activation in apoptosis induction. We have dealt with this issue by studying apoptosis induced by N-hexanoylsphingosine (C6-Cer) in CHP-100 human neuroepithelioma cells, maintained in complete growth medium. We report that C6-Cer-induced apoptosis occurred predominantly in G1/S phases of the cycle and was associated with RB dephosphorylation, in the setting of negligible Bcl-2 expression. Apoptosis was also associated with poly(ADP-ribose) polymerase (PARP) cleavage, thus indicating activation of CPP32/Yama/apopain (caspase-3); however, while the tripeptide caspase inhibitor Z-Val-Ala-DL-Asp-fluoromethylketone was able to prevent both C6-Cer-induced PARP cleavage and apoptosis, it was ineffective in preventing RB dephosphorylation. Moreover proteolytic RB cleavage occurred only to a marginal extent after C6-Cer treatment. These results indicate that apoptosis induced by ceramide in CHP-100 cells is caspase-mediated, but RB post-translational modification does not provide a key step, downstream caspase activation, in apoptosis execution.

Topics: Apoptosis; Blotting, Western; Caspase 3; Caspases; Ceramides; Cysteine Endopeptidases; Enzyme Activation; Flow Cytometry; G1 Phase; Humans; Neuroectodermal Tumors, Primitive, Peripheral; Phosphorylation; Poly(ADP-ribose) Polymerases; Protein Processing, Post-Translational; Retinoblastoma Protein; S Phase; Tumor Cells, Cultured

1998