Epithelial sodium channels expressed in Xenopus oocytes are activated by cyclic-AMP

2002 ◽  
Vol 6 (4) ◽  
pp. 195-201 ◽  
Author(s):  
K. Tamba ◽  
Y. S. Oh ◽  
J. K. Tucker ◽  
M. W. Quick ◽  
D. G. Warnock
2002 ◽  
Vol 283 (2) ◽  
pp. C646-C650 ◽  
Author(s):  
Hong-Long Ji ◽  
Catherine M. Fuller ◽  
Dale J. Benos

The hypothesis that there is a highly conserved, positively charged region distal to the second transmembrane domain in α-ENaC (epithelial sodium channel) that acts as a putative receptor site for the negatively charged COOH-terminal β- and γ-ENaC tails was tested in mutagenesis experiments. After expression in Xenopus oocytes, α-ENaC constructs in which positively charged arginine residues were converted into negatively charged glutamic acids could not be inhibited by blocking peptides. These observations provide insight into the gating machinery of ENaC.


2005 ◽  
Vol 25 (1_suppl) ◽  
pp. S190-S190
Author(s):  
Eugene Golanov ◽  
Heather Drummond ◽  
Jasleen Shant ◽  
Benjamin Clower ◽  
Betty Chen

PLoS ONE ◽  
2012 ◽  
Vol 7 (11) ◽  
pp. e49426 ◽  
Author(s):  
Dana Kuntzsch ◽  
Theresa Bergann ◽  
Petra Dames ◽  
Anja Fromm ◽  
Michael Fromm ◽  
...  

2015 ◽  
Vol 290 (9) ◽  
pp. 5241-5255 ◽  
Author(s):  
Hong-Long Ji ◽  
Runzhen Zhao ◽  
Andrey A. Komissarov ◽  
Yongchang Chang ◽  
Yongfeng Liu ◽  
...  

PLoS ONE ◽  
2013 ◽  
Vol 8 (1) ◽  
pp. e54750 ◽  
Author(s):  
Charles A. Downs ◽  
David Q. Trac ◽  
Lisa H. Kreiner ◽  
Amity F. Eaton ◽  
Nicholle M. Johnson ◽  
...  

2016 ◽  
Vol 12 (9) ◽  
pp. 1150-1154 ◽  
Author(s):  
Yang Liu ◽  
Bi-Jie Jiang ◽  
Run-Zhen Zhao ◽  
Hong-Long Ji

1996 ◽  
Vol 709 (1) ◽  
pp. 37-43 ◽  
Author(s):  
Tomoaki Yuhi ◽  
Akihiko Wada ◽  
Ryuichi Yamamoto ◽  
Toshihiko Yanagita ◽  
Hiromi Niina ◽  
...  

1996 ◽  
Vol 76 (3) ◽  
pp. 1423-1429 ◽  
Author(s):  
H. Terlau ◽  
M. Stocker ◽  
K. J. Shon ◽  
J. M. McIntosh ◽  
B. M. Olivera

1. A 31-amino-acid peptide from the venom of the snail-hunting species Conus marmoreus, microO-conotoxin MrVIA, inhibits mammalian voltage-gated sodium channels through a novel mechanism distinct from saxitoxin, tetrodotoxin, or mu-conotoxin. 2. MicroO-Conotoxin MrVIA blocks rat brain type II sodium channels expressed in Xenopus oocytes (IC50 approximately 200 nM, Hill coefficient approximately 1.6 +/- 0.2, mean +/- SE). Channel activation/inactivation kinetics and current-voltage relationships were unperturbed. 3. MicroO-Conotoxin MrVIA does not cause phasic or use-dependent inhibition of sodium currents measured in Xenopus oocytes expressing rat brain type II sodium channels, but shifts the steady-state availability of these sodium channels to more hyperpolarized potentials. 4. MicroO-Conotoxin MrVIA inhibited rapidly inactivating sodium channel conductance in rat hippocampal cells in culture. The inhibition was rapidly reversible. 5. MicroO-Conotoxin MrVIA does not displace specific [3H]saxitoxin binding to either rat brain or Electrophorus electric organ sites, indicating inhibitory effects mediated through a binding site distinct from site I.


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