okadaic-acid and parinaric-acid

okadaic-acid has been researched along with parinaric-acid* in 1 studies

Other Studies

1 other study(ies) available for okadaic-acid and parinaric-acid

Article	Year
Inactivation of Bcl-2 by phosphorylation. Proceedings of the National Academy of Sciences of the United States of America, 1995, May-09, Volume: 92, Issue:10 The antiapoptosis potential of Bcl-2 protein is well established, but the mechanism of Bcl-2 action is still poorly understood. Using the phosphatase inhibitor okadaic acid or the chemotherapeutic drug taxol, we found that Bcl-2 was phosphorylated in lymphoid cells. Phospho amino acid analysis revealed that Bcl-2 was phosphorylated on serine. Under similar conditions, okadaic acid or taxol treatment led to the induction of apoptosis in these cells. Thus, phosphorylation of Bcl-2 seems to inhibit its ability to interfere with apoptosis. In addition, phosphorylated Bcl-2 can no longer prevent lipid peroxidation as required to protect cells from apoptosis. Topics: Apoptosis; Cell Line; Cell Nucleus; Ethers, Cyclic; Fatty Acids, Unsaturated; Gene Expression; Humans; Lipid Peroxidation; Lymphocytes; Okadaic Acid; Paclitaxel; Phosphates; Phosphoprotein Phosphatases; Phosphorus Radioisotopes; Phosphorylation; Protein-Tyrosine Kinases; Proto-Oncogene Proteins; Proto-Oncogene Proteins c-bcl-2; Transfection	1995

Article

Year

Inactivation of Bcl-2 by phosphorylation.

Proceedings of the National Academy of Sciences of the United States of America, 1995, May-09, Volume: 92, Issue:10

The antiapoptosis potential of Bcl-2 protein is well established, but the mechanism of Bcl-2 action is still poorly understood. Using the phosphatase inhibitor okadaic acid or the chemotherapeutic drug taxol, we found that Bcl-2 was phosphorylated in lymphoid cells. Phospho amino acid analysis revealed that Bcl-2 was phosphorylated on serine. Under similar conditions, okadaic acid or taxol treatment led to the induction of apoptosis in these cells. Thus, phosphorylation of Bcl-2 seems to inhibit its ability to interfere with apoptosis. In addition, phosphorylated Bcl-2 can no longer prevent lipid peroxidation as required to protect cells from apoptosis.

Topics: Apoptosis; Cell Line; Cell Nucleus; Ethers, Cyclic; Fatty Acids, Unsaturated; Gene Expression; Humans; Lipid Peroxidation; Lymphocytes; Okadaic Acid; Paclitaxel; Phosphates; Phosphoprotein Phosphatases; Phosphorus Radioisotopes; Phosphorylation; Protein-Tyrosine Kinases; Proto-Oncogene Proteins; Proto-Oncogene Proteins c-bcl-2; Transfection

1995