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Related Experiment Videos

Intrinsically fluorescent luteinizing hormone receptor demonstrates hormone-driven aggregation.

R D Horvat1, S Nelson, C M Clay

  • 1Department of Cell and Molecular Biology, Colorado State University, Fort Collins 80523, USA.

Biochemical and Biophysical Research Communications
|March 2, 1999
PubMed
Summary

Unoccupied luteinizing hormone (LH) receptors are mobile on cell surfaces. Upon binding LH or hCG, these receptors cluster and their movement significantly slows, revealing new insights into hormone receptor dynamics.

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Area of Science:

  • Cell Biology
  • Molecular Endocrinology
  • Biophysics

Background:

  • The behavior of luteinizing hormone (LH) receptors in their unbound state has been difficult to study in living cells.
  • A lack of suitable non-hormone probes limited previous investigations into receptor aggregation upon gonadotropin binding.

Purpose of the Study:

  • To investigate the mobility and aggregation of LH receptors in viable cells using a novel fluorescent probe.
  • To understand how LH and hCG binding affects the lateral diffusion and distribution of LH receptors on the plasma membrane.

Main Methods:

  • Genetically engineered Chinese hamster ovary (CHO) cells expressing a fluorescently tagged rat LH receptor (rLHR-GFP).
  • Fluorescence photobleaching recovery (FPR) techniques to measure receptor lateral diffusion and mobility.

Related Experiment Videos

  • Hormone stimulation assays (LH and hCG) to observe changes in receptor behavior.

    • Main Results:

    • Over half of the expressed rLHR-GFP receptors were functional and located on the plasma membrane, increasing cAMP levels upon LH/hCG stimulation.
    • Unoccupied rLHR-GFP receptors exhibited significant lateral mobility (54% mobile, D = 16 x 10^-10 cm²/s).
    • LH and hCG binding drastically reduced receptor mobility and induced clustering, with hCG causing near-complete immobility and patch formation.

    Conclusions:

    • Unoccupied LH receptors exist as dispersed, mobile proteins on the plasma membrane.
    • Hormone binding triggers significant receptor aggregation and restricts their lateral diffusion, indicating a key mechanism in signal transduction.
    • The development of the fluorescent rLHR-GFP probe enables real-time studies of receptor dynamics in response to ligands.