Arachidonic acid closes gap junction channels in rat lacrimal glands

1989 ◽  
Vol 413 (3) ◽  
pp. 273-279 ◽  
Author(s):  
Christian Giaume ◽  
Clotilde Randriamampita ◽  
Alain Trautmann
Keyword(s):  
Arachidonic Acid ◽  
Gap Junction ◽  
Lacrimal Glands ◽  
Gap Junction Channels

scholarly journals Regulation of connexin36 gap junction channels byn-alkanols and arachidonic acid

2013 ◽  
Vol 591 (8) ◽  
pp. 2087-2101 ◽  
Author(s):  
Alina Marandykina ◽  
Nicolás Palacios-Prado ◽  
Lina Rimkutė ◽  
Vytenis A. Skeberdis ◽  
Feliksas F. Bukauskas
Keyword(s):  
Arachidonic Acid ◽  
Gap Junction ◽  
Gap Junction Channels

scholarly journals The Effect of Arachidonic Acid on Junctional Conductance and Gating of Connexin 36 Gap Junction Channels and their Modulation by N-Alkanols

2013 ◽  
Vol 104 (2) ◽  
pp. 632a
Author(s):  
Alina Marandykina ◽  
Lina Rimkutė ◽  
Nicolás Palacios-Prado ◽  
Arvydas Skeberdis ◽  
Feliksas Bukauskas
Keyword(s):  
Arachidonic Acid ◽  
Gap Junction ◽  
Gap Junction Channels ◽  
Connexin 36 ◽  
Junctional Conductance

scholarly journals Two Drosophila Innexins Are Expressed in Overlapping Domains and Cooperate to Form Gap-Junction Channels

2000 ◽  
Vol 11 (7) ◽  
pp. 2459-2470 ◽  
Author(s):  
Lucy A. Stebbings ◽  
Martin G. Todman ◽  
Pauline Phelan ◽  
Jonathan P. Bacon ◽  
Jane A. Davies
Keyword(s):  
Gap Junctions ◽  
Gap Junction ◽  
Ectopic Expression ◽  
In Vivo Studies ◽  
Electrophysiological Properties ◽  
Gap Junction Channels ◽  
Overlapping Domains ◽  
In Vitro Data

Members of the innexin protein family are structural components of invertebrate gap junctions and are analogous to vertebrate connexins. Here we investigate two Drosophila innexin genes,Dm-inx2 and Dm-inx3 and show that they are expressed in overlapping domains throughout embryogenesis, most notably in epidermal cells bordering each segment. We also explore the gap-junction–forming capabilities of the encoded proteins. In pairedXenopus oocytes, the injection of Dm-inx2mRNA results in the formation of voltage-sensitive channels in only ∼ 40% of cell pairs. In contrast, Dm-Inx3 never forms channels. Crucially, when both mRNAs are coexpressed, functional channels are formed reliably, and the electrophysiological properties of these channels distinguish them from those formed by Dm-Inx2 alone. We relate these in vitro data to in vivo studies. Ectopic expression ofDm-inx2 in vivo has limited effects on the viability ofDrosophila, and animals ectopically expressingDm-inx3 are unaffected. However, ectopic expression of both transcripts together severely reduces viability, presumably because of the formation of inappropriate gap junctions. We conclude that Dm-Inx2 and Dm-Inx3, which are expressed in overlapping domains during embryogenesis, can form oligomeric gap-junction channels.

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