TY  - JOUR
AU  - Bjelobaba, Ivana
AU  - Li, Shuo
AU  - Stojilković, Stanko S.
PY  - 2018
UR  - http://linkinghub.elsevier.com/retrieve/pii/S0005273617301098
UR  - https://radar.ibiss.bg.ac.rs/handle/123456789/2745
AB  - Pannexins are a three-member family of vertebrate plasma membrane spanning molecules that have homology to the invertebrate gap junction forming proteins, the innexins. However, pannexins do not form gap junctions but operate as plasma membrane channels. The best-characterized member of these proteins, Pannexin1 (Panx1) was suggested to be functionally associated with purinergic P2X and N-methyl-D-aspartate (NMDA) receptor channels. Activation of these receptor channels by their endogenous ligands leads to cross-activation of Panx1 channels. This in turn potentiates P2X and NMDA receptor channel signaling. Two potentiation concepts have been suggested: enhancement of the current responses and/or sustained receptor channel activation by ATP released through Panx1 pore and adenosine generated by ectonucleotidase-dependent dephosphorylation of ATP. Here we summarize the current knowledge and hypotheses about interactions of Panx1 channels with P2X and NMDA receptor channels. This article is part of a Special Issue entitled: Gap Junction Proteins edited by Jean Claude Herve.
T2  - Biochimica et Biophysica Acta (BBA) - Biomembranes
T1  - Interactions of Pannexin1 channels with purinergic and NMDA receptor channels
IS  - 1
VL  - 1860
DO  - 10.1016/j.bbamem.2017.03.025
SP  - 166
EP  - 173
ER  - 

@article{
author = "Bjelobaba, Ivana and Li, Shuo and Stojilković, Stanko S.",
year = "2018",
abstract = "Pannexins are a three-member family of vertebrate plasma membrane spanning molecules that have homology to the invertebrate gap junction forming proteins, the innexins. However, pannexins do not form gap junctions but operate as plasma membrane channels. The best-characterized member of these proteins, Pannexin1 (Panx1) was suggested to be functionally associated with purinergic P2X and N-methyl-D-aspartate (NMDA) receptor channels. Activation of these receptor channels by their endogenous ligands leads to cross-activation of Panx1 channels. This in turn potentiates P2X and NMDA receptor channel signaling. Two potentiation concepts have been suggested: enhancement of the current responses and/or sustained receptor channel activation by ATP released through Panx1 pore and adenosine generated by ectonucleotidase-dependent dephosphorylation of ATP. Here we summarize the current knowledge and hypotheses about interactions of Panx1 channels with P2X and NMDA receptor channels. This article is part of a Special Issue entitled: Gap Junction Proteins edited by Jean Claude Herve.",
journal = "Biochimica et Biophysica Acta (BBA) - Biomembranes",
title = "Interactions of Pannexin1 channels with purinergic and NMDA receptor channels",
number = "1",
volume = "1860",
doi = "10.1016/j.bbamem.2017.03.025",
pages = "166-173"
}

Bjelobaba, I., Li, S.,& Stojilković, S. S.. (2018). Interactions of Pannexin1 channels with purinergic and NMDA receptor channels. in Biochimica et Biophysica Acta (BBA) - Biomembranes, 1860(1), 166-173.
https://doi.org/10.1016/j.bbamem.2017.03.025

Bjelobaba I, Li S, Stojilković SS. Interactions of Pannexin1 channels with purinergic and NMDA receptor channels. in Biochimica et Biophysica Acta (BBA) - Biomembranes. 2018;1860(1):166-173.
doi:10.1016/j.bbamem.2017.03.025 .

Bjelobaba, Ivana, Li, Shuo, Stojilković, Stanko S., "Interactions of Pannexin1 channels with purinergic and NMDA receptor channels" in Biochimica et Biophysica Acta (BBA) - Biomembranes, 1860, no. 1 (2018):166-173,
https://doi.org/10.1016/j.bbamem.2017.03.025 . .