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Related Experiment Videos

Calcium channel alpha(2)delta subunits-structure and Gabapentin binding.

E Marais1, N Klugbauer, F Hofmann

  • 1Institut für Pharmakologie und Toxikologie der Technischen Universität München, München, Germany.

Molecular Pharmacology
|April 18, 2001
PubMed
Summary

Two new alpha(2)delta subunits (alpha(2)delta-2 and -3) were characterized, revealing their structure and N-glycosylation. Both alpha(2)delta-1 and -2 subunits bind the antiepileptic drug gabapentin.

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Area of Science:

  • Neuroscience
  • Molecular Biology
  • Pharmacology

Background:

  • High-voltage activated calcium channels are crucial for neuronal function.
  • Auxiliary alpha(2)delta subunits modulate calcium channel activity.
  • Previously, only alpha(2)delta-1 was known; alpha(2)delta-2 and -3 are newly identified.

Purpose of the Study:

  • To characterize the structure of the novel alpha(2)delta-2 and alpha(2)delta-3 subunits.
  • To investigate the binding of the antiepileptic drug gabapentin to these subunits.
  • To determine the tissue distribution of the alpha(2)delta subunits.

Main Methods:

  • Western blotting using subunit-specific antibodies to analyze gross structure.
  • Analysis of N-glycosylation and subunit composition after reduction.

Related Experiment Videos

  • Gabapentin binding assays to determine affinity (K(d) values).
  • Tissue distribution analysis across different mouse tissues.

    • Main Results:

    • Alpha(2)delta-2 and -3 subunits, like alpha(2)delta-1, consist of alpha(2) and delta proteins separable by reduction.
    • Both novel subunits are highly N-glycosylated.
    • Alpha(2)delta-1 is widely distributed; alpha(2)delta-2 is abundant in brain and heart; alpha(2)delta-3 is brain-specific.
    • Alpha(2)delta-1 and -2 bind gabapentin with K(d) values of 59 nM and 153 nM, respectively; alpha(2)delta-3 does not bind gabapentin.

    Conclusions:

    • The novel alpha(2)delta-2 and -3 subunits share structural similarities with alpha(2)delta-1.
    • Differential tissue distribution suggests distinct roles for each subunit.
    • The binding of gabapentin to alpha(2)delta-1 and -2 provides a molecular basis for its therapeutic effects in epilepsy.