A three-state model for connexin37 gating kinetics.
The gating behavior of human connexin 37 (hCx37) is unaffected by the nature of the bathing monovalent (for Na, K, Rb). It is modified by [Mg] in the millimolar range. For fitting the kinetics, we propose a simple extension to three states of the canonical 2-state model of the hemichannel. The extra closed state allows for some immobilization of a hemichannel at high transjunctional voltages. The model is reasonably efficient at fitting data at various voltage protocols. Interpreting the fits of the data at different [Mg] is consistent with a binding site for Mg.
Ramanan
S V
SV
Department of Physiology and Biophysics, State University of New York at Stony Brook, Stony Brook, New York 11794-8661, USA.
Brink
P R
PR
Varadaraj
K
K
Peterson
E
E
Schirrmacher
K
K
Banach
K
K
D055592:Biophysical Phenomena; D001703:Biophysics; D017630:Connexins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D004563:Electrochemistry; D006801:Humans; D066298:In Vitro Techniques; D015640:Ion Channel Gating / Q000187:drug effects; D007700:Kinetics; D008274:Magnesium / Q000494:pharmacology; D008954:Models, Biological; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D014162:Transfection; D014407:Tumor Cells, Cultured; D000097006:Gap Junction alpha-4 Protein
D017630:Connexins; D008274:Magnesium; D011994:Recombinant Proteins; D000097006:Gap Junction alpha-4 Protein