Ganapathi M K
Case Western Reserve University, School of Medicine, Cleveland, OH.
Biochem J. 1992 Jun 15;284 ( Pt 3)(Pt 3):645-8. doi: 10.1042/bj2840645.
Okadaic acid (OA), a specific inhibitor of protein phosphatases 1 and 2A, inhibited in a dose-dependent manner (5-20 nM) the induction of C-reactive protein (CRP), serum amyloid A (SAA) and fibrinogen by interleukin-6 (IL-6) plus interleukin-1 (IL-1), and of fibrinogen by IL-6 alone, in Hep 3B cells. Induction of alpha 1-proteinase inhibitor (alpha 1-PI) by IL-6 plus IL-1 or IL-6 alone was not significantly affected by OA up to concentrations of 20 nM, above which concentration OA was toxic in Hep 3B cells. OA also inhibited the induction of CRP, fibrinogen and alpha 1-PI by IL-6 in the NPLC/PRF/5 cell line, albeit at a higher concentration (80 nM). These results suggest that the signal transduction mechanisms regulating induction of acute-phase proteins by IL-6, either alone or in combination with IL-1, are mediated by activation of protein phosphatases 1 and/or 2A.
冈田酸（OA）是蛋白磷酸酶1和2A的特异性抑制剂，在Hep 3B细胞中，它以剂量依赖方式（5 - 20 nM）抑制白细胞介素-6（IL-6）加白细胞介素-1（IL-1）诱导的C反应蛋白（CRP）、血清淀粉样蛋白A（SAA）和纤维蛋白原，以及单独IL-6诱导的纤维蛋白原。在浓度高达20 nM时，IL-6加IL-1或单独IL-6诱导的α1-蛋白酶抑制剂（α1-PI）不受OA显著影响，高于此浓度时OA对Hep 3B细胞有毒性。OA也抑制NPLC/PRF/5细胞系中IL-6诱导的CRP、纤维蛋白原和α1-PI，尽管所需浓度较高（80 nM）。这些结果表明，单独或与IL-1联合时，调节IL-6诱导急性期蛋白的信号转导机制是由蛋白磷酸酶1和/或2A的激活介导的。
