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Inverse relationship between GLUT-4 phosphorylation and its intrinsic activity

J E Reusch1, K E Sussman, B Draznin

  • 1Department of Medicine, Veterans Affairs Medical Center, Denver, Colorado 80220.

The Journal of Biological Chemistry
|February 15, 1993
PubMed
Summary
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Parathyroid hormone (PTH) increases glucose transporter 4 (GLUT-4) phosphorylation in rat adipocytes, impairing its intrinsic activity. This phosphorylation hinders insulin

Area of Science:

  • Molecular Biology
  • Cellular Metabolism
  • Endocrinology

Background:

  • Glucose transporter 4 (GLUT-4) is crucial for insulin-stimulated glucose uptake in adipocytes.
  • Regulation of GLUT-4 function by post-translational modifications like phosphorylation is key to metabolic control.

Purpose of the Study:

  • To investigate the impact of parathyroid hormone (PTH)-induced phosphorylation on GLUT-4 function in isolated rat adipocytes.
  • To determine if GLUT-4 phosphorylation affects its intrinsic activity and response to insulin.

Main Methods:

  • Adipocytes were labeled with 32P and treated with PTH and insulin.
  • GLUT-4 phosphorylation was assessed via immunoprecipitation, autoradiography, and densitometry.
  • GLUT-4 intrinsic activity was measured using [14C]2-deoxyglucose uptake in plasma membrane vesicles.

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Main Results:

  • PTH significantly increased GLUT-4 phosphorylation and blocked insulin-induced dephosphorylation.
  • Phosphorylated GLUT-4 exhibited significantly reduced intrinsic activity.
  • Calcium channel blockers and cyclic AMP antagonists restored GLUT-4 intrinsic activity in PTH-treated cells.

Conclusions:

  • GLUT-4 phosphorylation, induced by PTH, significantly impairs its intrinsic activity.
  • Phosphorylation of GLUT-4 interferes with insulin's ability to stimulate glucose transport.
  • These findings highlight a novel regulatory mechanism of glucose uptake potentially relevant to metabolic disorders.