Spatiotemporal magnetic fields enhance cytosolic Ca 2+ levels and induce actin polymerization via activation of voltage-gated sodium channels in skeletal muscle cells

Biomaterials ◽  
2018 ◽  
Vol 163 ◽  
pp. 174-184 ◽  
Author(s):  
Mónica Rubio Ayala ◽  
Tatiana Syrovets ◽  
Susanne Hafner ◽  
Vitalii Zablotskii ◽  
Alexandr Dejneka ◽  
...  
2016 ◽  
Vol 110 (3) ◽  
pp. 436a-437a ◽  
Author(s):  
Robert E. del Carlo ◽  
Normand Leblanc ◽  
Edmund D. Brodie ◽  
Chis R. Feldman

2014 ◽  
Vol 35 (8) ◽  
pp. 537-546 ◽  
Author(s):  
Sergei V. Surma ◽  
Galina B. Belostotskaya ◽  
Boris F. Shchegolev ◽  
Vasily E. Stefanov

Marine Drugs ◽  
2019 ◽  
Vol 17 (9) ◽  
pp. 510 ◽  
Author(s):  
Rocio K. Finol-Urdaneta ◽  
Jeffrey R. McArthur ◽  
Vyacheslav S. Korkosh ◽  
Sun Huang ◽  
Denis McMaster ◽  
...  

µ-Conotoxin PIIIA, in the sub-picomolar, range inhibits the archetypal bacterial sodium channel NaChBac (NavBh) in a voltage- and use-dependent manner. Peptide µ-conotoxins were first recognized as potent components of the venoms of fish-hunting cone snails that selectively inhibit voltage-gated skeletal muscle sodium channels, thus preventing muscle contraction. Intriguingly, computer simulations predicted that PIIIA binds to prokaryotic channel NavAb with much higher affinity than to fish (and other vertebrates) skeletal muscle sodium channel (Nav 1.4). Here, using whole-cell voltage clamp, we demonstrate that PIIIA inhibits NavBac mediated currents even more potently than predicted. From concentration-response data, with [PIIIA] varying more than 6 orders of magnitude (10−12 to 10−5 M), we estimated an IC50 = ~5 pM, maximal block of 0.95 and a Hill coefficient of 0.81 for the inhibition of peak currents. Inhibition was stronger at depolarized holding potentials and was modulated by the frequency and duration of the stimulation pulses. An important feature of the PIIIA action was acceleration of macroscopic inactivation. Docking of PIIIA in a NaChBac (NavBh) model revealed two interconvertible binding modes. In one mode, PIIIA sterically and electrostatically blocks the permeation pathway. In a second mode, apparent stabilization of the inactivated state was achieved by PIIIA binding between P2 helices and trans-membrane S5s from adjacent channel subunits, partially occluding the outer pore. Together, our experimental and computational results suggest that, besides blocking the channel-mediated currents by directly occluding the conducting pathway, PIIIA may also change the relative populations of conducting (activated) and non-conducting (inactivated) states.


2007 ◽  
Vol 72 (5) ◽  
pp. 1220-1227 ◽  
Author(s):  
Lior Cohen ◽  
Yael Troub ◽  
Michael Turkov ◽  
Nicolas Gilles ◽  
Nitza Ilan ◽  
...  

Sign in / Sign up

Export Citation Format

Share Document