scholarly journals Possible Role of Gap Junction Channels and Non-Junctional Channels in the Infection Caused by Trypanosoma cruzi

Author(s):  
José Luis Vega ◽  
Camilo Juyumaya ◽  
Luis Rodríguez ◽  
Juan Güiza ◽  
Camila Gutíerrez ◽  
...  
2013 ◽  
Vol 2013 ◽  
pp. 1-17 ◽  
Author(s):  
José Luis Vega ◽  
Mario Subiabre ◽  
Felipe Figueroa ◽  
Kurt Alex Schalper ◽  
Luis Osorio ◽  
...  

In vertebrates, connexins (Cxs) and pannexins (Panxs) are proteins that form gap junction channels and/or hemichannels located at cell-cell interfaces and cell surface, respectively. Similar channel types are formed by innexins in invertebrate cells. These channels serve as pathways for cellular communication that coordinate diverse physiologic processes. However, it is known that many acquired and inherited diseases deregulate Cx and/or Panx channels, condition that frequently worsens the pathological state of vertebrates. Recent evidences suggest that Cx and/or Panx hemichannels play a relevant role in bacterial and viral infections. Nonetheless, little is known about the role of Cx- and Panx-based channels in parasitic infections of vertebrates. In this review, available data on changes in Cx and gap junction channel changes induced by parasitic infections are summarized. Additionally, we describe recent findings that suggest possible roles of hemichannels in parasitic infections. Finally, the possibility of new therapeutic designs based on hemichannel blokers is presented.


Antioxidants ◽  
2021 ◽  
Vol 10 (9) ◽  
pp. 1374
Author(s):  
Yumeng Quan ◽  
Yu Du ◽  
Yuxin Tong ◽  
Sumin Gu ◽  
Jean X. Jiang

The lens is continuously exposed to oxidative stress insults, such as ultraviolet radiation and other oxidative factors, during the aging process. The lens possesses powerful oxidative stress defense systems to maintain its redox homeostasis, one of which employs connexin channels. Connexins are a family of proteins that form: (1) Hemichannels that mediate the communication between the intracellular and extracellular environments, and (2) gap junction channels that mediate cell-cell communication between adjacent cells. The avascular lens transports nutrition and metabolites through an extensive network of connexin channels, which allows the passage of small molecules, including antioxidants and oxidized wastes. Oxidative stress-induced post-translational modifications of connexins, in turn, regulates gap junction and hemichannel permeability. Recent evidence suggests that dysfunction of connexins gap junction channels and hemichannels may induce cataract formation through impaired redox homeostasis. Here, we review the recent advances in the knowledge of connexin channels in lens redox homeostasis and their response to cataract-related oxidative stress by discussing two major aspects: (1) The role of lens connexins and channels in oxidative stress and cataractogenesis, and (2) the impact and underlying mechanism of oxidative stress in regulating connexin channels.


2004 ◽  
Vol 47 (1-3) ◽  
pp. 290-303 ◽  
Author(s):  
Jorge E. Contreras ◽  
Helmuth A. Sánchez ◽  
Loreto P. Véliz ◽  
Feliksas F. Bukauskas ◽  
Michael V.L. Bennett ◽  
...  

2005 ◽  
Vol 16 (7) ◽  
pp. 300-306 ◽  
Author(s):  
Georges Pointis ◽  
Dominique Segretain

2010 ◽  
Vol 90 (1) ◽  
pp. 179-206 ◽  
Author(s):  
Richard T. Mathias ◽  
Thomas W. White ◽  
Xiaohua Gong

The cells of most mammalian organs are connected by groups of cell-to-cell channels called gap junctions. Gap junction channels are made from the connexin (Cx) family of proteins. There are at least 20 isoforms of connexins, and most tissues express more than 1 isoform. The lens is no exception, as it expresses three isoforms: Cx43, Cx46, and Cx50. A common role for all gap junctions, regardless of their Cx composition, is to provide a conduit for ion flow between cells, thus creating a syncytial tissue with regard to intracellular voltage and ion concentrations. Given this rather simple role of gap junctions, a persistent question has been: Why are there so many Cx isoforms and why do tissues express more than one isoform? Recent studies of lens Cx knockout (KO) and knock in (KI) lenses have begun to answer these questions. To understand these roles, one must first understand the physiological requirements of the lens. We therefore first review the development and structure of the lens, its numerous transport systems, how these systems are integrated to generate the lens circulation, the roles of the circulation in lens homeostasis, and finally the roles of lens connexins in growth, development, and the lens circulation.


2018 ◽  
Vol 315 (5) ◽  
pp. C623-C635
Author(s):  
Charles K. Abrams ◽  
Alejandro Peinado ◽  
Rola Mahmoud ◽  
Matan Bocarsly ◽  
Han Zhang ◽  
...  

The connexins are members of a family of integral membrane proteins that form gap junction channels between apposed cells and/or hemichannels across the plasma membranes. The importance of the arginine at position 76 (Arg76) in the structure and/or function of connexin 46 (Cx46) is highlighted by its conservation across the entire connexin family and the occurrence of pathogenic mutations at this (or the corresponding homologous) residue in a number of human diseases. Two mutations at Arg76 in Cx46 are associated with cataracts in humans, highlighting the importance of this residue. We examined the expression levels and macroscopic and single-channel properties of human Cx46 and compared them with those for two pathogenic mutants, namely R76H and R76G. To gain further insight into the role of charge at this position, we generated two additional nonnaturally occurring mutants, R76K (charge conserving) and R76E (charge inverting). We found that, when expressed exogenously in Neuro2a cells, all four mutants formed membrane hemichannels, inducing membrane permeability at levels comparable to those recorded in cells expressing the wild-type Cx46. In contrast, the number of gap-junction plaques and the magnitude of junctional coupling were reduced by all four mutations. To gain further insight into the role of Arg76 in the function of Cx46, we performed homology modeling of Cx46 and in silico mutagenesis of Arg76 to Gly, His, or Glu. Our studies suggest that the loss of interprotomeric interactions has a significant effect on the extracellular domain conformation and dynamics, thus affecting the hemichannel docking required for formation of cell-cell channels.


2008 ◽  
Vol 44 (4) ◽  
pp. 752 ◽  
Author(s):  
M. Gönczi ◽  
R. Papp ◽  
Gy. Seprényi ◽  
Á. Végh

2014 ◽  
Vol 745 ◽  
pp. 196-200 ◽  
Author(s):  
Siamak Beheshti ◽  
Seyyed Akbar Mir Seyyed Hosseini ◽  
Maryam Noorbakhshnia ◽  
Mehdi Eivani

2011 ◽  
Vol 100 (3) ◽  
pp. 438a-439a
Author(s):  
J. Krishnan ◽  
V.S Chakravarthy

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