scholarly journals C-Terminal End of Aquaporin 0 Regulates Lens Gap Junction Channel Function

2019 ◽  
Vol 60 (7) ◽  
pp. 2525 ◽  
Author(s):  
Kulandaiappan Varadaraj ◽  
Junyuan Gao ◽  
Richard T. Mathias ◽  
Sindhu Kumari
Keyword(s):  
Gap Junction ◽  
Channel Function ◽  
Gap Junction Channel

scholarly journals Enhanced connexin 43 expression delays intra-mitoitc duration and cell cycle traverse independently of gap junction channel function

2010 ◽  
Vol 110 (3) ◽  
pp. 772-782 ◽  
Author(s):  
Scott R. Johnstone ◽  
Angela K. Best ◽  
Catherine S. Wright ◽  
Brant E. Isakson ◽  
Rachel J. Errington ◽  
...  
Keyword(s):  
Cell Cycle ◽  
Gap Junction ◽  
Connexin 43 ◽  
Channel Function ◽  
Gap Junction Channel

scholarly journals Beyond Gap Junction Channel Function: the Expression of Cx43 Contributes to Aldosterone-Induced Mesangial Cell Proliferation via the ERK1/2 and PKC Pathways

2015 ◽  
Vol 36 (3) ◽  
pp. 1210-1222 ◽  
Author(s):  
Aiqing Zhang ◽  
Ying Han ◽  
Bin Wang ◽  
Shanwen Li ◽  
Weihua Gan
Keyword(s):  
Gap Junction ◽  
Connexin 43 ◽  
Mesangial Cell ◽  
Lucifer Yellow ◽  
Inverse Correlation ◽  
Dye Transfer ◽  
Cx43 Expression ◽  
Pi3k Inhibitor Ly294002 ◽  
Channel Function ◽  
Gap Junction Channel

Aims: This study aimed to explore the precise mechanism and signaling pathways of mesangial cell (MC) proliferation from a new point of view considering Connexin 43 (Cx43). Methods: MC proliferation was measured by the incorporation of 3H-thymidine (3H-TdR). Cx43 was over-expressed in MC cells using lipofectamine 2000, and the expression level was tested with reverse transcription-polymerase chain reaction (RT-PCR) and Western blot analyses. The gap junction channel function was explored by Lucifer Yellow scrape loading and dye transfer (SLDT), and the intracellular calcium concentrations ([Ca2+]i) were characterized by confocal microscopy on cells loaded with Fura-3/AM. Results: There was an inverse correlation between Cx43 expression and MC proliferation (P<0.05). SLDT studies revealed that there was no difference in the gap junction channel function between the normal and Aldosterone (Aldo)-stimulated groups (P>0.05). Our data also showed that the mineralcorticoid receptor (MR) antagonist spironolactone, ERK1/2 inhibitor PD98059 and PKC inhibitor GF109203X could attenuate the down-regulation of Cx43 expression in Aldo-induced MC proliferation; however, the PI3K inhibitor LY294002 could block MC proliferation without affecting Cx43 expression at either the mRNA or protein level. In addition, Aldo promoted MC proliferation in parallel with increasing [Ca2+]i (P<0.05), suggesting that the classical PKC pathway might be activated. Conclusions: Our study provides preliminary evidence that Cx43 is an important regulator of Aldo-promoted MC proliferation. Furthermore, reduced Cx43 expression promoted MC proliferation independent of the gap junction channel function, and this process might be mediated through the ERK1/2- and PKC-dependent pathways.

scholarly journals Cholesterol modulates function of connexin 43 gap junction channel via PKC pathway in H9c2 cells

2014 ◽  
Vol 1838 (8) ◽  
pp. 2019-2025 ◽  
Author(s):  
Jun Zou ◽  
Xiao-Yang Yue ◽  
Sheng-Chao Zheng ◽  
Guangwei Zhang ◽  
He Chang ◽  
...  
Keyword(s):  
Gap Junction ◽  
Connexin 43 ◽  
H9c2 Cells ◽  
Gap Junction Channel

A Closed Gap Junction Channel State Caused By A Single Site Mutation in the 3rd Transmembrane Helix

2004 ◽  
Vol 10 (S02) ◽  
pp. 1498-1499 ◽  
Author(s):  
Derek L Beahm ◽  
Guido Gaietta ◽  
Anjana Chandrasekhar ◽  
Galen M Hand ◽  
Amy Smock ◽  
...  
Keyword(s):  
Gap Junction ◽  
Transmembrane Helix ◽  
Single Site ◽  
Site Mutation ◽  
Channel State ◽  
Gap Junction Channel

Extended abstract of a paper presented at Microscopy and Microanalysis 2004 in Savannah, Georgia, USA, August 1–5, 2004.

scholarly journals Identification of amino acid residues lining the pore of a gap junction channel

2002 ◽  
Vol 159 (2) ◽  
pp. 349-360 ◽  
Author(s):  
I.M. Skerrett ◽  
J. Aronowitz ◽  
J.H. Shin ◽  
G. Cymes ◽  
E. Kasperek ◽  
...  
Keyword(s):  
Gap Junction ◽  
Molecular Level ◽  
Close Association ◽  
Pore Wall ◽  
Van Der Waals Interactions ◽  
Amino Acid Residues ◽  
Fixed Charges ◽  
Gap Junction Channel ◽  
Multicellular Organisms ◽  
Pore Lining

Gap junctions represent a ubiquitous and integral part of multicellular organisms, providing the only conduit for direct exchange of nutrients, messengers and ions between neighboring cells. However, at the molecular level we have limited knowledge of their endogenous permeants and selectivity features. By probing the accessibility of systematically substituted cysteine residues to thiol blockers (a technique called SCAM), we have identified the pore-lining residues of a gap junction channel composed of Cx32. Analysis of 45 sites in perfused Xenopus oocyte pairs defined M3 as the major pore-lining helix, with M2 (open state) or M1 (closed state) also contributing to the wider cytoplasmic opening of the channel. Additional mapping of a close association between M3 and M4 allowed the helices of the low resolution map (Unger et al., 1999. Science. 283:1176–1180) to be tentatively assigned to the connexin transmembrane domains. Contrary to previous conceptions of the gap junction channel, the residues lining the pore are largely hydrophobic. This indicates that the selective permeabilities of this unique channel class may result from novel mechanisms, including complex van der Waals interactions of permeants with the pore wall, rather than mechanisms involving fixed charges or chelation chemistry as reported for other ion channels.

Innexin-3 forms connexin-like intercellular channels

1999 ◽  
Vol 112 (14) ◽  
pp. 2391-2396 ◽  
Author(s):  
Y. Landesman ◽  
T.W. White ◽  
T.A. Starich ◽  
J.E. Shaw ◽  
D.A. Goodenough ◽  
...  
Keyword(s):  
Caenorhabditis Elegans ◽  
Gap Junction ◽  
Functional Properties ◽  
Xenopus Oocytes ◽  
Family Members ◽  
Electrical Coupling ◽  
Large Family ◽  
Gap Junction Channel ◽  
Intercellular Channels

Innexins comprise a large family of genes that are believed to encode invertebrate gap junction channel-forming proteins. However, only two Drosophila innexins have been directly tested for the ability to form intercellular channels and only one of those was active. Here we tested the ability of Caenorhabditis elegans family members INX-3 and EAT-5 to form intercellular channels between paired Xenopus oocytes. We show that expression of INX-3 but not EAT-5, induces electrical coupling between the oocyte pairs. In addition, analysis of INX-3 voltage and pH gating reveals a striking degree of conservation in the functional properties of connexin and innnexin channels. These data strongly support the idea that innexin genes encode intercellular channels.

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