ucn-1028-c and Arthritis--Rheumatoid

ucn-1028-c has been researched along with Arthritis--Rheumatoid* in 1 studies

Other Studies

1 other study(ies) available for ucn-1028-c and Arthritis--Rheumatoid

Article	Year
Phorbol 12-myristate 13-acetate (PMA)-induced oxyradical production in rheumatoid synovial cells. Japanese journal of pharmacology, 1997, Volume: 73, Issue:4 We successfully detected the oxyradical production in human synovial A (macrophage-like) and B (fibroblast-like) cells by phorbol 12-myristate 13-acetate (PMA) using the luminol-chemiluminescence method. The PMA (0.1 microgram/ml)-induced photon generation was abolished by an O2- scavenger, superoxide dismutase, and an H2O2 scavenger, catalase, suggesting that the stimulus produced oxyradicals in synovial cells. Both of these responses were abolished by a protein kinase C (PKC) inhibitor, calphostine C, but unaffected by an intracellular Ca2+ chelator, BAPTA-AM, and Ca2+ removal from the extracellular medium. These findings suggest that synovial A and B cells produce oxyradicals through PKC-mediated and [Ca2+]i-independent mechanisms, probably through the activation of NADPH oxidase. Topics: Arthritis, Rheumatoid; Calcium; Carcinogens; Catalase; Chelating Agents; Egtazic Acid; Enzyme Inhibitors; Fibroblasts; Humans; Hydrogen Peroxide; Knee Joint; Luminescent Measurements; Macrophages; Naphthalenes; Photons; Protein Kinase C; Superoxide Dismutase; Superoxides; Synovial Fluid; Tetradecanoylphorbol Acetate	1997

Article

Year

Phorbol 12-myristate 13-acetate (PMA)-induced oxyradical production in rheumatoid synovial cells.

Japanese journal of pharmacology, 1997, Volume: 73, Issue:4

We successfully detected the oxyradical production in human synovial A (macrophage-like) and B (fibroblast-like) cells by phorbol 12-myristate 13-acetate (PMA) using the luminol-chemiluminescence method. The PMA (0.1 microgram/ml)-induced photon generation was abolished by an O2- scavenger, superoxide dismutase, and an H2O2 scavenger, catalase, suggesting that the stimulus produced oxyradicals in synovial cells. Both of these responses were abolished by a protein kinase C (PKC) inhibitor, calphostine C, but unaffected by an intracellular Ca2+ chelator, BAPTA-AM, and Ca2+ removal from the extracellular medium. These findings suggest that synovial A and B cells produce oxyradicals through PKC-mediated and [Ca2+]i-independent mechanisms, probably through the activation of NADPH oxidase.

Topics: Arthritis, Rheumatoid; Calcium; Carcinogens; Catalase; Chelating Agents; Egtazic Acid; Enzyme Inhibitors; Fibroblasts; Humans; Hydrogen Peroxide; Knee Joint; Luminescent Measurements; Macrophages; Naphthalenes; Photons; Protein Kinase C; Superoxide Dismutase; Superoxides; Synovial Fluid; Tetradecanoylphorbol Acetate

1997