scholarly journals PLASMA MEMBRANE VESICLES FROM TYPE II PNEUMOCYTES INSERT CATION CHANNELS INTO PLANAR LIPID BILAYERS. 2319

1996 ◽  
Vol 39 ◽  
pp. 389-389
Author(s):  
David G Oelberg ◽  
Ana Raiko ◽  
Fang Xu ◽  
Dieter K Bartschat
1992 ◽  
Vol 262 (6) ◽  
pp. G1027-G1032 ◽  
Author(s):  
M. Sellinger ◽  
S. A. Weinman ◽  
R. M. Henderson ◽  
A. Zweifach ◽  
J. L. Boyer ◽  
...  

Previous studies from this laboratory have demonstrated a Cl(-)-HCO3- exchanger and have provided evidence for a Cl- conductance in rat liver canalicular plasma membrane vesicles. To further investigate the apical Cl- conductance, we performed single-channel analysis after incorporation of canalicular liver plasma membrane vesicles into planar lipid bilayers. This was necessary, because the canalicular membrane is not accessible for the patch-clamp technique. Two types of anion channels could be identified (30- and 90-pS conductance) corresponding to the class of small and intermediate channels, respectively. The kinetics of the small channel were found to be voltage dependent with a maximum for the open probability at -20 mV. In contrast, intermediate channel kinetics were voltage independent. The anion channels described above could allow electrogenic Cl- efflux, to compensate Cl- influx via the electroneutral Cl(-)-HCO3- exchanger. Further studies will be required to prove their functional importance in bile formation.


1984 ◽  
Vol 84 (5) ◽  
pp. 665-686 ◽  
Author(s):  
E Moczydlowski ◽  
S S Garber ◽  
C Miller

Single Na+ channels from rat skeletal muscle plasma membrane vesicles were inserted into planar lipid bilayers formed from neutral phospholipids and were observed in the presence of batrachotoxin. The batrachotoxin-modified channel activates in the voltage range -120 to -80 mV and remains open almost all the time at voltages positive to -60 mV. Low levels of tetrodotoxin (TTX) induce slow fluctuations of channel current, which represent the binding and dissociation of single TTX molecules to single channels. The rates of association and dissociation of TTX are both voltage dependent, and the association rate is competitively inhibited by Na+. This inhibition is observed only when Na+ is increased on the TTX binding side of the channel. The results suggest that the TTX receptor site is located at the channel's outer mouth, and that the Na+ competition site is not located deeply within the channel's conduction pathway.


2012 ◽  
Vol 33 (7) ◽  
pp. 535-542 ◽  
Author(s):  
Wenjun J. Sun ◽  
Mehri Kaviani Mogadam ◽  
Marianne Sommarin ◽  
Henrietta Nittby ◽  
Leif G. Salford ◽  
...  

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