Characterization of high molecular weight FK-506 binding activities reveals a novel FK-506-binding protein as well as a protein complex.

@article{Wiederrecht1992CharacterizationOH,
  title={Characterization of high molecular weight FK-506 binding activities reveals a novel FK-506-binding protein as well as a protein complex.},
  author={Gregory J. Wiederrecht and Shang-Cheng Hung and Ho Kin Chan and Alex. Marcy and Myriam Martin and Jimmy Calaycay and David Boulton and Natalia G. Sigal and Randall L. Kincaid and J. John Towaco Siekierka},
  journal={The Journal of biological chemistry},
  year={1992},
  volume={267 30},
  pages={
          21753-60
        }
}
The immunoregulant FK-506 potently inhibits particular calcium-associated signal transduction events that occur early during T-lymphocyte activation and during IgE receptor-mediated exocytosis in mast cells. FK-506 binds to a growing family of receptors termed FK-506-binding proteins (FKBPs), the most abundant being a 12-kDa cytosolic receptor, FKBP12. To date, there is no formal evidence proving that FKBP12 is the sole receptor mediating the immunosuppressive effects or toxic side effects of… CONTINUE READING

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