Nov 21, 1991

Modulation of synovial fibroblast plasminogen activator and plasminogen activator inhibitor production by protein kinase C

Biochimica Et Biophysica Acta
J UhlE Mochan


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).

Mentioned in this Paper

Plant alkaloid
Specimen Type - Fibroblasts
Extrinsic Plasminogen Activators
SERPINE1 wt Allele
Plasminogen Activator Inhibitor Assay

About this Paper

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