PMID- 24611056
OWN - NLM
STAT- PubMed-not-MEDLINE
DCOM- 20140624
LR  - 20211021
IS  - 1664-042X (Print)
IS  - 1664-042X (Electronic)
IS  - 1664-042X (Linking)
VI  - 5
DP  - 2014
TI  - Connexin and Pannexin hemichannels are regulated by redox potential.
PG  - 80
LID - 10.3389/fphys.2014.00080 [doi]
LID - 80
AB  - Connexins (Cxs) and Pannexins (Panxs) are two non-related protein families, 
      having both the property to form hemichannels at the plasma membrane. There are 
      21 genes coding for different Cx based proteins and only 3 for Panx. Under 
      physiological conditions, these hemichannels (Cxs and Panxs) present a low open 
      probability, but when open, they allow the release of signaling molecules to the 
      extracellular space. However, under pathological conditions, these hemichannels 
      increase their open probability, inducing important lysis of metabolites, and 
      ionic imbalance, which in turn induce the massive entry of Ca(+2) to the cell. 
      Actually, it is well recognized that Cxs and Panxs based channels play an 
      important role in several diseases and -in many cases- this is associated with an 
      aberrant hemichannel opening. Hemichannel opening and closing are controlled by a 
      plethora of signaling including changes of the voltage plasma membrane, 
      protein-protein interactions, and several posttranslational modifications, 
      including protein cleavage, phosphorylation, glycosylation, hydroxylation and 
      S-nitrosylation, among others. In particular, it has been recently shown that the 
      cellular redox status modulates the opening/closing and permeability of at least 
      Cx43, Cx46, and Panx1 hemichannels. Thus, for example, the gaseous transmitter 
      nitric oxide (NO) can induce the S-nitrosylation of these proteins modulating in 
      turn several of their properties. The reason is that the redox status of a cell 
      is fundamental to set their response to the environment and also plays an 
      important role in several pathologies. In this review, I will discuss how NO and 
      other molecules associated with redox signaling modulate Cxs and Panx 
      hemichannels properties.
FAU - Retamal, Mauricio A
AU  - Retamal MA
AD  - Facultad de Medicina Clinica Alemana, Centro de Fisiologia Celular e Integrativa, 
      Universidad del Desarrollo Santiago, Chile.
LA  - eng
PT  - Journal Article
PT  - Review
DEP - 20140225
PL  - Switzerland
TA  - Front Physiol
JT  - Frontiers in physiology
JID - 101549006
PMC - PMC3933782
OTO - NOTNLM
OT  - S-Nitrosylation
OT  - carbon monoxide
OT  - connexin
OT  - nitric oxide
OT  - redox signaling
EDAT- 2014/03/13 06:00
MHDA- 2014/03/13 06:01
PMCR- 2014/02/25
CRDT- 2014/03/11 06:00
PHST- 2013/11/14 00:00 [received]
PHST- 2014/02/08 00:00 [accepted]
PHST- 2014/03/11 06:00 [entrez]
PHST- 2014/03/13 06:00 [pubmed]
PHST- 2014/03/13 06:01 [medline]
PHST- 2014/02/25 00:00 [pmc-release]
AID - 10.3389/fphys.2014.00080 [doi]
PST - epublish
SO  - Front Physiol. 2014 Feb 25;5:80. doi: 10.3389/fphys.2014.00080. eCollection 2014.