Pannexin-1 (Panx1) forms anion-selective channels with a permeability up to 1 kDa and represents a pathway for the release of cytosolic ATP. Several structurally similar connexin (Cx) proteins have been identified in platelets and shown to play roles in haemostasis and thrombosis. More recently, functional Panx1 channels have been demonstrated on the surface of human platelets [Taylor et al. (2014) J. Thromb. Haemost. 12, 987–998]. Since their identification in the year 2000, several mechanisms have been reported to activate Panx1 channels, including mechanical stimulation, oxygen-glucose deprivation, a rise of [Ca2+]i, caspase cleavage and phosphorylation. Within this review, the regulation of Panx1 channels is discussed, with a focus on how they may contribute to platelet function.
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June 2015
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Conference Article|
June 01 2015
Regulation of Pannexin-1 channel activity
Kirk A. Taylor;
*Department of Cell Physiology and Pharmacology, University of Leicester, Leicester, U.K.
†Department of Biomedical and Forensic Sciences, Anglia Ruskin University, Cambridge, U.K.
2To whom correspondence should be addressed (emailkirk.taylor@anglia.ac.uk).
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Joy R. Wright;
Joy R. Wright
1
*Department of Cell Physiology and Pharmacology, University of Leicester, Leicester, U.K.
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Martyn P. Mahaut-Smith
Martyn P. Mahaut-Smith
*Department of Cell Physiology and Pharmacology, University of Leicester, Leicester, U.K.
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Publisher: Portland Press Ltd
Received:
February 09 2015
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© The Authors Journal compilation © 2015 Biochemical Society
2015
Biochem Soc Trans (2015) 43 (3): 502–507.
Article history
Received:
February 09 2015
Citation
Kirk A. Taylor, Joy R. Wright, Martyn P. Mahaut-Smith; Regulation of Pannexin-1 channel activity. Biochem Soc Trans 1 June 2015; 43 (3): 502–507. doi: https://doi.org/10.1042/BST20150042
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