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Membrane transport mechanisms probed by capacitance measurements with megahertz voltage clamp.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Mager, S. Frazier, G. A. Hilgemann, D. W. Lu, C. C. Kabakov, A. Markin, V. S.
Description	Author Affiliation: Lu CC ( Department of Physiology, University of Texas Southwestern Medical Center, Dallas 75235, USA.);
Abstract	We have used capacitance measurements with a 1-microsecond voltage clamp technique to probe electrogenic ion-transporter interactions in giant excised membrane patches. The hydrophobic ion dipicrylamine was used to test model predictions for a simple charge-moving reaction. The voltage and frequency dependencies of the apparent dipicrylamine-induced capacitance, monitored by 1-mV sinusoidal perturbations, correspond to single charges moving across 76% of the membrane field at a rate of 9500 s-1 at 0 mV. For the cardiac Na,K pump, the combined presence of cytoplasmic ATP and sodium induces an increase of apparent membrane capacitance which requires the presence of extracellular sodium. The dependencies of capacitance changes on frequency, voltage, ATP, and sodium verify that phosphorylation enables a slow, 300- to 900-s-1, pump transition (the E1-E2 conformational change), which in turn enables fast, electrogenic, extracellular sodium binding reactions. For the GAT1 (gamma-aminobutyric acid,Na,Cl) cotransporter, expressed in Xenopus oocyte membrane, we find that chloride binding from the cytoplasmic side, and probably sodium binding from the extracellular side, results in a decrease of membrane capacitance monitored with 1- to 50-kHz perturbation frequencies. Evidently, ion binding by the GAT1 transporter suppresses an intrinsic fast charge movement which may originate from a mobility of charged residues of the transporter binding sites. The results demonstrate that fast capacitance measurements can provide new insight into electrogenic processes closely associated with ion binding by membrane transporters.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	24
Volume Number	92
Language	English
Publisher	National Academy of Sciences
Publisher Date	1995-12-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Carrier Proteins Metabolism Cell Membrane Physiology Membrane Proteins Membrane Transport Proteins Oocytes Ultrastructure Organic Anion Transporters Patch-Clamp Techniques Sodium-Potassium-Exchanging ATPase Animals Biological Transport, Active Chlorides GABA Plasma Membrane Transport Proteins Guinea Pigs Membrane Potentials Myocardium Cytology Xenopus Laevis Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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