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Rapid turnover of the 1,25-dihydroxyvitamin D3 receptor in human target cells

J A Eisman1, J C Fragonas, M L McMenemy

  • 1Bone and Mineral Research Group, Garvan Institute of Medical Research, St. Vincents Hospital, Sydney, New South Wales, Australia.

Endocrinology
|April 1, 1988
PubMed

Insights

This study characterizes 1,25-dihydroxyvitamin D3 [1,25-(OH)2D3] receptor binding kinetics in T47 D breast cancer cells. It reveals variations in receptor binding capacity and half-life across different cell sublines, crucial for understanding vitamin D

Area of Science:

  • Endocrinology
  • Molecular Biology
  • Cell Biology

Background:

  • Studying early biochemical events of 1,25-dihydroxyvitamin D3 [1,25-(OH)2D3] in human cells is challenging due to limited in vitro systems.
  • The T47 D human breast cancer cell line, with specific high-affinity 1,25-(OH)2D3 receptors, serves as a functional model for responsive human cells.

Purpose of the Study:

  • To investigate the kinetics of 1,25-(OH)2D3 uptake and binding in T47 D cells.
  • To analyze variations in receptor binding parameters (capacity, affinity, half-life) among different T47 D sublines.

Main Methods:

  • Utilized [3H]1,25-(OH)2D3 for specific uptake and binding studies in intact T47 D cells.
  • Employed Scatchard analysis in broken cell preparations of wild-type, T47-10, and T47-M1 sublines.
  • Assessed occupied receptor half-life using puromycin in intact cells and unoccupied receptor half-life in broken cell preparations.

Main Results:

  • Binding parameters, including peak binding capacity and receptor affinity, varied significantly among the three T47 D sublines.
  • Peak binding capacity ranged from 10-65 fmol/10(6) cells (intact) and 2.8-12.7 fmol/10(6) cells (broken).
  • Receptor affinity was consistently high (1.1-2.8 x 10(-11) M); occupied receptor half-life ranged from 1.4-3.1 hours, and unoccupied receptor half-life was approximately 4.1-4.2 hours.

Conclusions:

  • The T47 D cell system effectively models 1,25-(OH)2D3-responsive human cells, exhibiting distinct receptor binding characteristics.
  • Variations in receptor binding kinetics among sublines highlight the importance of cell-specific factors in vitamin D3 action.
  • Receptor half-life demonstrated differences between intact and broken cell preparations, suggesting potential post-translational modifications or cellular environment influences.

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