Ion channels are membrane proteins, a ubiquitous component o all cell membrane, whether excitable or nonexcitable. These channels open in response to various stimuli (membrane potential change, neurotransmitters, and hormones) to allow ions to pass through the membrane manifesting their functions. For example, the voltage-sensitive sodium channel is responsible for impulse initiation and conduction and the GABAA receptor, a pentameric complex gated open by gamma-aminobutyric acid, mediates the major inhibitory input to brain neurons. These ion channels are subject to modulation by intracellular second messengers including cyclic AMP, calcium ions, and guanosine triphosphate-binding proteins and contain numerous receptor sites on which many therapeutic agents and toxins can act.

Since the rate at which these channels open and close is rapid and the speed at which ions flow through the channel is high, channel function is best studied using the electrophysiological approach, which is capable of measuring the ion flux at the rate of one million ions per second with a millisecond time resolution. Using the patch clamp technique, we can analyze the drug-receptor interaction on a real-time basis; and combined with the molecular cloning approach recently applied to neuroscience, we can examine the structure and function of the receptor channel at the molecular level.

My research interest included biophysics and pharmacology of both Na channels and GABA-activated chloride channels with emphases on the molecular mechanism by which local anesthetics and anticonvulsant drugs interact with the Na channel and the molecular mechanisms by which volatile general anesthetics interact with the GABAA receptor CI channel. Using cloned GABAA receptors, we are examining the subunit requirement for the anesthetic action.
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