phorbol-12-13-didecanoate and Leukemia--Erythroblastic--Acute

phorbol-12-13-didecanoate has been researched along with Leukemia--Erythroblastic--Acute* in 2 studies

Other Studies

2 other study(ies) available for phorbol-12-13-didecanoate and Leukemia--Erythroblastic--Acute

Article	Year
Regulation of synthesis and activity of NAD(+)-dependent 15-hydroxy-prostaglandin dehydrogenase (15-PGDH) by dexamethasone and phorbol ester in human erythroleukemia (HEL) cells. Biochemical and biophysical research communications, 1991, Jun-28, Volume: 177, Issue:3 Dexamethasone stimulated 15-PGDH activity in HEL cells in a time and concentration dependent manner. Increase in 15-PGDH activity by dexamethasone was found to be accompanied by an increase in enzyme synthesis as revealed by Western blot and [35S]methionine labeling studies. In addition to dexamethasone, other anti-inflammatory steroids also increased 15-PGDH activity in the order of their glucocorticoid activity. Among sex steroids only progesterone increased significantly 15-PGDH activity. 12-0-Tetradecanoylphorbol-13-acetate (TPA) also induced the synthesis of 15-PGDH but inhibited the enzyme activity. It appears that TPA caused a time dependent inactivation of 15-PGDH by a protein kinase C mediated mechanism. Topics: Blotting, Western; Carcinogens; Cell Line; Dexamethasone; Dinoprostone; Electrophoresis, Polyacrylamide Gel; Enzyme Induction; Humans; Hydroxyprostaglandin Dehydrogenases; Kinetics; Leukemia, Erythroblastic, Acute; Methionine; NAD; Phorbol Esters; Steroids; Sulfur Radioisotopes; Tetradecanoylphorbol Acetate	1991
Phorbol ester induces increased expression, altered glycosylation, and reduced adhesion of K562 erythroleukemia cell fibronectin receptors. The Journal of biological chemistry, 1989, Aug-05, Volume: 264, Issue:22 The human multipotential hematopoietic cell line K562 expresses fibronectin receptor (FNR) subunits of 160 kDa (alpha chain) and 120 kDa (beta chain). Treatment with 12-O-tetradecanoylphorbol 13-acetate (TPA) led to reduced binding of K562 to immobilized fibronectin (FN), although treated cells expressed 10-fold more cell surface FNR than untreated cells. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis confirmed this and showed altered electrophoretic mobilities of FNR subunits from TPA-treated cells. TPA treatment affected N-linked glycosylation, as tunicamycin treatment of K562 cells abolished differences in FNR mobility. Sialidase treatment of FNR immunoprecipitates minimized and sialidase treatment of intact cells eliminated these mobility differences between subunits from control and TPA-treated cells. Reduced sialylation of FNR from TPA-treated cells was further demonstrated by chromatography with bead-coupled lectins and by the greater negative charge of untreated K562 FNR subunits in two-dimensional isoelectric focusing-polyacrylamide gel electrophoresis. A relationship between reduced FNR sialylation and reduced FN binding was suggested by adhesion assays of sialidase-treated K562 which showed that desialylation of cell surface FNR was associated with decreased cell adhesion. Thus, TPA treatment reduces the function, increases the expression, and alters the structure of K562 FNR, and these changes appear to involve FNR sialylation. Topics: Cell Adhesion; Cell Line; Chromatography, Affinity; Electrophoresis, Polyacrylamide Gel; Fibronectins; Glycosylation; Humans; Kinetics; Leukemia, Erythroblastic, Acute; Neuraminidase; Phorbol Esters; Receptors, Fibronectin; Receptors, Immunologic; Tetradecanoylphorbol Acetate; Tumor Cells, Cultured	1989

Article

Year

Regulation of synthesis and activity of NAD(+)-dependent 15-hydroxy-prostaglandin dehydrogenase (15-PGDH) by dexamethasone and phorbol ester in human erythroleukemia (HEL) cells.

Biochemical and biophysical research communications, 1991, Jun-28, Volume: 177, Issue:3

Dexamethasone stimulated 15-PGDH activity in HEL cells in a time and concentration dependent manner. Increase in 15-PGDH activity by dexamethasone was found to be accompanied by an increase in enzyme synthesis as revealed by Western blot and [35S]methionine labeling studies. In addition to dexamethasone, other anti-inflammatory steroids also increased 15-PGDH activity in the order of their glucocorticoid activity. Among sex steroids only progesterone increased significantly 15-PGDH activity. 12-0-Tetradecanoylphorbol-13-acetate (TPA) also induced the synthesis of 15-PGDH but inhibited the enzyme activity. It appears that TPA caused a time dependent inactivation of 15-PGDH by a protein kinase C mediated mechanism.

Topics: Blotting, Western; Carcinogens; Cell Line; Dexamethasone; Dinoprostone; Electrophoresis, Polyacrylamide Gel; Enzyme Induction; Humans; Hydroxyprostaglandin Dehydrogenases; Kinetics; Leukemia, Erythroblastic, Acute; Methionine; NAD; Phorbol Esters; Steroids; Sulfur Radioisotopes; Tetradecanoylphorbol Acetate

1991

Phorbol ester induces increased expression, altered glycosylation, and reduced adhesion of K562 erythroleukemia cell fibronectin receptors.

The Journal of biological chemistry, 1989, Aug-05, Volume: 264, Issue:22

The human multipotential hematopoietic cell line K562 expresses fibronectin receptor (FNR) subunits of 160 kDa (alpha chain) and 120 kDa (beta chain). Treatment with 12-O-tetradecanoylphorbol 13-acetate (TPA) led to reduced binding of K562 to immobilized fibronectin (FN), although treated cells expressed 10-fold more cell surface FNR than untreated cells. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis confirmed this and showed altered electrophoretic mobilities of FNR subunits from TPA-treated cells. TPA treatment affected N-linked glycosylation, as tunicamycin treatment of K562 cells abolished differences in FNR mobility. Sialidase treatment of FNR immunoprecipitates minimized and sialidase treatment of intact cells eliminated these mobility differences between subunits from control and TPA-treated cells. Reduced sialylation of FNR from TPA-treated cells was further demonstrated by chromatography with bead-coupled lectins and by the greater negative charge of untreated K562 FNR subunits in two-dimensional isoelectric focusing-polyacrylamide gel electrophoresis. A relationship between reduced FNR sialylation and reduced FN binding was suggested by adhesion assays of sialidase-treated K562 which showed that desialylation of cell surface FNR was associated with decreased cell adhesion. Thus, TPA treatment reduces the function, increases the expression, and alters the structure of K562 FNR, and these changes appear to involve FNR sialylation.

Topics: Cell Adhesion; Cell Line; Chromatography, Affinity; Electrophoresis, Polyacrylamide Gel; Fibronectins; Glycosylation; Humans; Kinetics; Leukemia, Erythroblastic, Acute; Neuraminidase; Phorbol Esters; Receptors, Fibronectin; Receptors, Immunologic; Tetradecanoylphorbol Acetate; Tumor Cells, Cultured

1989