okadaic-acid and Precursor-B-Cell-Lymphoblastic-Leukemia-Lymphoma

okadaic-acid has been researched along with Precursor-B-Cell-Lymphoblastic-Leukemia-Lymphoma* in 1 studies

Other Studies

1 other study(ies) available for okadaic-acid and Precursor-B-Cell-Lymphoblastic-Leukemia-Lymphoma

Article	Year
Inhibitory role of cAMP on doxorubicin-induced apoptosis in pre-B ALL cells through dephosphorylation of p53 serine residues. Apoptosis : an international journal on programmed cell death, 2010, Volume: 15, Issue:2 Exposure of cells to chemotherapeutic drug doxorubicin, a DNA-damaging agent, induces an increase in the levels and activity of the wild-type p53 protein. Less well appreciated was the effect of cAMP levels on posttranslational modifications of p53 in response to doxorubicin. Here we show that elevation of cAMP in pre-B acute lymphoblastic leukemia NALM-6 cells significantly attenuated phosphorylation state of p53 at Ser6, Ser9, Ser15, Ser20, Ser37, Ser46 and Ser392 upon exposure to doxorubicin. Increased cAMP levels also shifted the ratio of the death promoter to death repressor genes via alteration of Bcl-2 and Bax proteins expression. In conclusion, our results suggest that activation of cAMP-signaling system may repress p53-dependent apoptosis in malignant cells exposed to doxorubicin. Topics: Apoptosis; Ataxia Telangiectasia Mutated Proteins; bcl-2-Associated X Protein; Caspase 3; Cell Cycle Proteins; Cell Line, Tumor; Checkpoint Kinase 2; Cyclic AMP; DNA Damage; DNA-Binding Proteins; Doxorubicin; Gene Expression Regulation, Leukemic; Humans; Intracellular Space; Okadaic Acid; Phosphoprotein Phosphatases; Phosphorylation; Phosphoserine; Precursor B-Cell Lymphoblastic Leukemia-Lymphoma; Protein Phosphatase 1; Protein Phosphatase 2; Protein Phosphatase 2C; Protein Serine-Threonine Kinases; Serine; Tumor Suppressor Protein p53; Tumor Suppressor Proteins	2010

Article

Year

Inhibitory role of cAMP on doxorubicin-induced apoptosis in pre-B ALL cells through dephosphorylation of p53 serine residues.

Apoptosis : an international journal on programmed cell death, 2010, Volume: 15, Issue:2

Exposure of cells to chemotherapeutic drug doxorubicin, a DNA-damaging agent, induces an increase in the levels and activity of the wild-type p53 protein. Less well appreciated was the effect of cAMP levels on posttranslational modifications of p53 in response to doxorubicin. Here we show that elevation of cAMP in pre-B acute lymphoblastic leukemia NALM-6 cells significantly attenuated phosphorylation state of p53 at Ser6, Ser9, Ser15, Ser20, Ser37, Ser46 and Ser392 upon exposure to doxorubicin. Increased cAMP levels also shifted the ratio of the death promoter to death repressor genes via alteration of Bcl-2 and Bax proteins expression. In conclusion, our results suggest that activation of cAMP-signaling system may repress p53-dependent apoptosis in malignant cells exposed to doxorubicin.

Topics: Apoptosis; Ataxia Telangiectasia Mutated Proteins; bcl-2-Associated X Protein; Caspase 3; Cell Cycle Proteins; Cell Line, Tumor; Checkpoint Kinase 2; Cyclic AMP; DNA Damage; DNA-Binding Proteins; Doxorubicin; Gene Expression Regulation, Leukemic; Humans; Intracellular Space; Okadaic Acid; Phosphoprotein Phosphatases; Phosphorylation; Phosphoserine; Precursor B-Cell Lymphoblastic Leukemia-Lymphoma; Protein Phosphatase 1; Protein Phosphatase 2; Protein Phosphatase 2C; Protein Serine-Threonine Kinases; Serine; Tumor Suppressor Protein p53; Tumor Suppressor Proteins

2010