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Related Experiment Videos

A putative sirolimus (rapamycin) effector protein

Y Chen1, H Chen, A E Rhoad

  • 1Department of Chemistry, Columbia University, New York, NY 10027.

Biochemical and Biophysical Research Communications
|August 30, 1994
PubMed
Summary

Researchers identified a novel protein, p210, that binds to sirolimus (rapamycin) and its FKBP12 complex. This binding correlates with immunosuppressive activity, suggesting p210 is the sirolimus effector protein.

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Area of Science:

  • Immunology
  • Molecular Biology
  • Pharmacology

Background:

  • Sirolimus (rapamycin) is an immunosuppressive drug that inhibits T and B cell proliferation.
  • The precise immunosuppressive mechanism of sirolimus remains incompletely understood.

Purpose of the Study:

  • To identify the sirolimus effector protein responsible for its immunosuppressive activity.

Main Methods:

  • Isolation of a membrane-associated protein, p210, using affinity matrix methods from human T cells and cell lines (Molt 4, BJAB).
  • Binding assays to assess the interaction of p210 with sirolimus:FKBP12 complex, FKBP12 alone, FK506:FKBP12 complex, and sirolimus-biotin.

Main Results:

  • p210 specifically binds to the sirolimus:FKBP12 complex.

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  • Binding to FKBP12 alone, FK506:FKBP12 complex, or sirolimus-biotin was negligible.
  • The binding affinity of p210 to various drug:FKBP12 complexes correlated directly with the known immunosuppressive potency of the respective sirolimus analogs.

    • Conclusions:

    • The identified protein, p210, is a strong candidate for the sirolimus effector protein.
    • These findings provide crucial insights into the molecular mechanism of sirolimus immunosuppression.