scholarly journals SINGLE-CHANNEL CURRENTS FROM ZONA-FREE MOUSE EGGS

1987 ◽  
Vol 72 (4) ◽  
pp. 483-492 ◽  
Author(s):  
C. Bountra ◽  
R. J. Martin
1991 ◽  
Vol 161 (1) ◽  
pp. 455-468
Author(s):  
F. ZUFALL ◽  
H. HATT ◽  
T. A. KEIL

Single-channel patch-clamp techniques were used to identify and characterize a Ca2+-activated nonspecific cation channel (CAN channel) on insect olfactory receptor neurones (ORNs) from antennae of male Antheraea polyphemus. The CAN channel was found both in acutely isolated ORNs from developing pupae and in membrane vesicles from mature ORNs that presumably originated from inner dendritic segments. Amplitude histograms of the CAN single-channel currents presented well-defined peaks corresponding to at least four channel substates each having a conductance of about 16 pS. Simultaneous gating of the substates was achieved by intracellular Ca2+ with an EC50 value of about 80 nmoll−1. Activity of the CAN channel could be blocked by application of amiloride (IC50 <100nmoll−1). Moreover, in the presence of 1μmoll−1 Ca2+, opening of the CAN channel was totally suppressed by 10 μmoll−1 cyclic GMP, whereas ATP (1 mmol l−1) was without effect. We suggest that the CAN channel plays a specific role in modulation of cell excitability and in shaping the voltage response of ORNs.


Author(s):  
Davide LOVISOLO ◽  
Renzo LEVI ◽  
Dario CANTINO ◽  
Elena STROBBIA

1993 ◽  
Vol 265 (1) ◽  
pp. C72-C78 ◽  
Author(s):  
H. Sunose ◽  
K. Ikeda ◽  
Y. Saito ◽  
A. Nishiyama ◽  
T. Takasaka

Single-channel currents of the luminal membrane of marginal cells dissected from the guinea pig cochlea were investigated using the patch-clamp technique. Nonselective cation channels having a linear conductance of 27 pS were activated by depolarization, cytoplasmic Ca2+, and cytoplasmic acidification. Cytoplasmic ATP inactivated the channel. A mixture of 3-isobutyl-1-methylxanthine and forskolin activated a small-conductance Cl channel in the cell-attached mode. On excision in the inside-out mode, the Cl channel was inactivated, but it was reactivated by a cytoplasmic catalytic subunit of protein kinase A with ATP. This Cl channel had a linear conductance of 12 pS, and its activity was little affected by voltage. The sequence of permeation by anions was Br- > Cl > I-. The Cl channel blocker diphenylamine-2-carboxylic acid (3 mM) completely blocked the channel, but 5-nitro-2-(3-phenylpropylamino)-benzoic acid (50 microM) blocked it only partially. The above-mentioned characteristics are similar to those of the well-demonstrated Cl- channel, cystic fibrosis transmembrane regulator.


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