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Cadmium increases GLUT1 substrate binding affinity in vitro while reducing its cytochalasin B binding affinity

M Lachaal1, H Liu, S Kim

  • 1Biophysics Laboratory, Veterans Administration Medical Center, Buffalo, New York, USA.

Biochemistry
|November 26, 1996
PubMed
Summary

Cadmium alters glucose transporter 1 (GLUT1) function by enhancing substrate binding while hindering cytochalasin B interaction. This suggests a specific conformational change induced by cadmium in GLUT1.

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Area of Science:

  • Biochemistry
  • Cell Biology
  • Toxicology

Background:

  • Cadmium is known to stimulate glucose transport in fibroblasts.
  • This stimulation is thought to be mediated by increased intrinsic activity of glucose transporter 1 (GLUT1).

Purpose of the Study:

  • To investigate the effect of cadmium on the in vitro binding of purified GLUT1 to glucose and cytochalasin B.
  • To elucidate the mechanism by which cadmium influences GLUT1 activity.

Main Methods:

  • In vitro binding assays using purified GLUT1.
  • Competitive inhibition studies with cytochalasin B and D-glucose in the presence and absence of cadmium.
  • Analysis of binding affinities and inhibition constants.

Main Results:

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  • Cadmium competitively inhibited cytochalasin B binding to GLUT1, reducing its binding affinity.
  • D-glucose displaced bound cytochalasin B effectively, indicating cadmium enhances substrate binding affinity.
  • Cadmium significantly increased the substrate binding affinity of GLUT1.

Conclusions:

  • Cadmium induces a specific conformational change in GLUT1.
  • This conformational change differentially affects GLUT1's interaction with cytochalasin B and its substrate, glucose.
  • These findings provide new insights into the functional mechanisms of glucose transporters.