Faculty Opinions recommendation of Gap junction hemichannels contribute to the generation of diarrhoea during infectious enteric disease.

Author(s):  
Kim Barrett
2007 ◽  
Vol 21 (5) ◽  
Author(s):  
Julian Andrew Guttman ◽  
Ann Enju Lin ◽  
Yuling Li ◽  
Christian Naus ◽  
A Wayne Vogl ◽  
...  

2003 ◽  
Vol 26 (11) ◽  
pp. 610-617 ◽  
Author(s):  
Michael V.L. Bennett ◽  
Jorge E. Contreras ◽  
Feliksas F. Bukauskas ◽  
Juan C. Sáez

2006 ◽  
Vol 116 (12) ◽  
pp. 2205-2210 ◽  
Author(s):  
Benjamin C. Stong ◽  
Qing Chang ◽  
Shoeb Ahmad ◽  
Xi Lin

2002 ◽  
Vol 365 (3) ◽  
pp. 693-699 ◽  
Author(s):  
Shoeb AHMAD ◽  
W. Howard EVANS

Gap-junction channels provide a widespread intercellular signalling mechanism. They are constructed of a family of connexin membrane proteins that thread across the membrane four times and oligomerize to generate hexameric gap-junction hemichannels. Using an in vitro cell-free transcription/translation system, we demonstrate that connexin (Cx) 26, one of the smallest connexins, is integrated directly in a post-translational manner into plasma membranes. Protein-cleavage studies of Cx26 integrated into plasma membranes indicate a similar native transmembrane topography to that of Cx26 integrated co-translationally into microsomes. Cx26 integrated post-translationally into plasma membranes oligomerizes and, when incorporated into liposomes, provides permeability to ascorbic acid, suggesting that gap-junction hemichannels are generated. The results provide the basis of a novel alternative mechanism for spontaneous assembly in plasma membranes of Cx26 gap-junction hemichannels that occurs independently of the conventional biogenesis of gap junctions involving connexin trafficking and oligomerization via membrane components of the secretory pathway.


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