In vivo and in vitro binding of microcystin to protein phosphatases 1 and 2A.

@article{Runnegar1995InVA,
  title={In vivo and in vitro binding of microcystin to protein phosphatases 1 and 2A.},
  author={Maria T. C. Runnegar and N Berndt and Siu Ming Kong and Eminy H. Y. Lee and Long Zhang},
  journal={Biochemical and biophysical research communications},
  year={1995},
  volume={216 1},
  pages={162-9}
}
The hepatotoxic microcystins (Mcyst) are potent inhibitors of the ser/thr protein phosphatases (PP1 and PP2A) with IC50's of 0.1-1.0 nM. Mcyst and other PP inhibitors like okadaic acid or calyculin A interact with the C-terminal region of PP1 and PP2A. Using [125I]-Mcyst and antibodies specific for PP1 and PP2A, we show by immunoprecipitation and autoradiography, that in hepatocytes Mcyst forms secondary covalent bonds with both PP1 and PP2A catalytic subunits. We demonstrate that the bond… CONTINUE READING