okadaic-acid and Leukemia--Monocytic--Acute

okadaic-acid has been researched along with Leukemia--Monocytic--Acute* in 2 studies

Other Studies

2 other study(ies) available for okadaic-acid and Leukemia--Monocytic--Acute

Article	Year
The serine/threonine phosphatase, PP2A: endogenous regulator of inflammatory cell signaling. Journal of immunology (Baltimore, Md. : 1950), 2001, Jan-15, Volume: 166, Issue:2 We have investigated the regulation of kinases and phosphatases in early gene activation in monocytes because these cells are implicated in the pathogenesis of acute inflammatory states, such as sepsis and acute lung injury. One early gene up-regulated by endotoxin is c-Jun, a member of the activating protein (AP) family. C-Jun is phosphorylated by c-Jun N-terminal kinase (JNK) and associates with c-Fos to form the AP-1 transcriptional activation complex that can drive cytokine expression. Inhibition of the serine/threonine phosphatase, PP2-A, with okadaic acid resulted in a significant increase in JNK activity. This finding was associated with increased phosphorylation of c-Jun, AP-1 transcriptional activity, and IL-1beta expression. Activation of PP2A inhibited JNK activity and JNK coprecipitated with the regulatory subunit, PP2A-Aalpha, supporting the conclusion that PP2A is a key regulator of JNK in the context of an inflammatory stimulus. Topics: Chemical Precipitation; Enzyme Activation; Enzyme Inhibitors; Humans; Inflammation; JNK Mitogen-Activated Protein Kinases; Leukemia, Monocytic, Acute; Lipopolysaccharides; Mitogen-Activated Protein Kinases; Monocytes; Okadaic Acid; Phosphatidic Acids; Phosphoprotein Phosphatases; Signal Transduction; Transcription Factor AP-1; Tumor Cells, Cultured	2001
Tumor necrosis factor-alpha production-inhibiting activity of phthalimide analogues on human leukemia THP-1 cells and a structure-activity relationship study. Bioorganic & medicinal chemistry, 1997, Volume: 5, Issue:11 N-Substituted phthalimides (2-substituted 1H-isoindole-1,3-diones) were prepared and their inhibitory effects on tumor necrosis factor-alpha (TNF-alpha) production by human leukemia cell line THP-1 stimulated with 12-O-tetradecanoylphorbol 13-acetate (TPA) or okadaic acid (OA) were examined. A structure-activity relationship study of these phthalimide analogues revealed that their inhibitory effects on TPA- and OA-induced TNF-alpha production by THP-1 cells are well correlated to each other, i.e. they may involve the same target molecule(s). An analysis by the use of phthalimide analogue-immobilized affinity gels indicated the existence of several phthalimide-binding proteins in THP-1 cell extract. Topics: Drug Screening Assays, Antitumor; Humans; Leukemia, Monocytic, Acute; Okadaic Acid; Phthalimides; Structure-Activity Relationship; Tetradecanoylphorbol Acetate; Tumor Cells, Cultured; Tumor Necrosis Factor-alpha	1997

Article

Year

The serine/threonine phosphatase, PP2A: endogenous regulator of inflammatory cell signaling.

Journal of immunology (Baltimore, Md. : 1950), 2001, Jan-15, Volume: 166, Issue:2

We have investigated the regulation of kinases and phosphatases in early gene activation in monocytes because these cells are implicated in the pathogenesis of acute inflammatory states, such as sepsis and acute lung injury. One early gene up-regulated by endotoxin is c-Jun, a member of the activating protein (AP) family. C-Jun is phosphorylated by c-Jun N-terminal kinase (JNK) and associates with c-Fos to form the AP-1 transcriptional activation complex that can drive cytokine expression. Inhibition of the serine/threonine phosphatase, PP2-A, with okadaic acid resulted in a significant increase in JNK activity. This finding was associated with increased phosphorylation of c-Jun, AP-1 transcriptional activity, and IL-1beta expression. Activation of PP2A inhibited JNK activity and JNK coprecipitated with the regulatory subunit, PP2A-Aalpha, supporting the conclusion that PP2A is a key regulator of JNK in the context of an inflammatory stimulus.

Topics: Chemical Precipitation; Enzyme Activation; Enzyme Inhibitors; Humans; Inflammation; JNK Mitogen-Activated Protein Kinases; Leukemia, Monocytic, Acute; Lipopolysaccharides; Mitogen-Activated Protein Kinases; Monocytes; Okadaic Acid; Phosphatidic Acids; Phosphoprotein Phosphatases; Signal Transduction; Transcription Factor AP-1; Tumor Cells, Cultured

2001

Tumor necrosis factor-alpha production-inhibiting activity of phthalimide analogues on human leukemia THP-1 cells and a structure-activity relationship study.

Bioorganic & medicinal chemistry, 1997, Volume: 5, Issue:11

N-Substituted phthalimides (2-substituted 1H-isoindole-1,3-diones) were prepared and their inhibitory effects on tumor necrosis factor-alpha (TNF-alpha) production by human leukemia cell line THP-1 stimulated with 12-O-tetradecanoylphorbol 13-acetate (TPA) or okadaic acid (OA) were examined. A structure-activity relationship study of these phthalimide analogues revealed that their inhibitory effects on TPA- and OA-induced TNF-alpha production by THP-1 cells are well correlated to each other, i.e. they may involve the same target molecule(s). An analysis by the use of phthalimide analogue-immobilized affinity gels indicated the existence of several phthalimide-binding proteins in THP-1 cell extract.

Topics: Drug Screening Assays, Antitumor; Humans; Leukemia, Monocytic, Acute; Okadaic Acid; Phthalimides; Structure-Activity Relationship; Tetradecanoylphorbol Acetate; Tumor Cells, Cultured; Tumor Necrosis Factor-alpha

1997