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• W2000339946 abstract "Phorbol myristate acetate (PMA) added to human synovial fibroblast cultures caused a dose-dependent increase in the production of plasminogen activator inhibitor-type 1 (PAI-1). In addition, PMA inhibited endogenous and interleukin-1 (IL-1) induced plasminogen activator (PA) activity, while increasing mRNA PAI-1 levels. Other protein kinase C (PKC) activators, mezerein and teleocidin B4, caused similar effects. The simultaneous addition of the PKC antagonists, H-7 or staurosporine, prevented the inhibition of PA activity by PMA. This study shows that activation of PKC inhibits PA and stimulates PAI production in human synovial fibroblasts. These results suggest that activation of PKC may play an important role in regulating increased PA production associated with joint destruction in rheumatoid arthritis (RA)." @default.
• W2000339946 created "2016-06-24" @default.
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• W2000339946 date "1991-11-01" @default.
• W2000339946 modified "2023-09-27" @default.
• W2000339946 title "Modulation of synovial fibroblast plasminogen activator and plasminogen activator inhibitor production by protein kinase C" @default.
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• W2000339946 doi "https://doi.org/10.1016/0925-4439(91)90082-k" @default.
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