Interactions of adriamycin with a calcium binding site

Biochem Biophys Res Commun. 1988 Mar 15;151(2):679-85. doi: 10.1016/s0006-291x(88)80334-6.

Abstract

Terbium (Tb3+) luminescence has been used to investigate the interactions of adriamycin with a specific calcium binding protein, in the plasma membrane of GH3/B6 pituitary tumor cells. The luminescence intensity and lifetime of the Tb3+-GH3/B6 complex was quenched in the presence of adriamycin. According to Stern-Volmer analysis, the quenching of Tb3+-GH3/B6 luminescence was by both membrane bound adriamycin (Ka = 3.7 x 10(5) M-1) and free adriamycin (kq = 7.3 x 10(7) M-1 s-1). The data suggests that, the calcium binding site at the outer surface of the membrane is collisionally accessible to freely diffusing adriamycin; and, that the toxin receptor site is located near the bound metal ion.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Calcium-Binding Proteins / metabolism*
  • Cell Line
  • Cell Membrane / metabolism
  • Doxorubicin / metabolism*
  • Kinetics
  • Luminescent Measurements
  • Pituitary Neoplasms / metabolism
  • Terbium

Substances

  • Calcium-Binding Proteins
  • Terbium
  • Doxorubicin