2011
DOI: 10.1210/en.2010-1216
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Expression and Roles of Pannexins in ATP Release in the Pituitary Gland

Abstract: Pannexins are a newly discovered three-member family of proteins expressed in the brain and peripheral tissues that belong to the superfamily of gap junction proteins. However, in mammals pannexins do not form gap junctions, and their expression and function in the pituitary gland have not been studied. Here we show that the rat pituitary gland expresses mRNA and protein transcripts of pannexins 1 and 2 but not pannexin 3. Pannexin 1 was more abundantly expressed in the anterior lobe, whereas pannexin 2 was mo… Show more

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Cited by 52 publications
(61 citation statements)
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References 49 publications
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“…In other cases of ball-and-chain inhibition, there has been no physiological mechanism described for cutting the chain to permanently remove channel inhibition, as we have found for caspase-mediated cleavage and activation of hPANX1. Although this cleavage-based mechanism seems appropriate for a terminal process such as apoptosis, we expect that more subtle mechanisms will account for other forms of PANX1 activation associated with different physiological conditions (10,26,27). Nevertheless, because C-terminal inhibition in the intact channel depends on its association with the pore, our data suggest that these other PANX1 activation mechanisms will also require some disruption of the C terminus from its inhibitory interaction site within the channel pore.…”
Section: Discussionmentioning
confidence: 88%
“…In other cases of ball-and-chain inhibition, there has been no physiological mechanism described for cutting the chain to permanently remove channel inhibition, as we have found for caspase-mediated cleavage and activation of hPANX1. Although this cleavage-based mechanism seems appropriate for a terminal process such as apoptosis, we expect that more subtle mechanisms will account for other forms of PANX1 activation associated with different physiological conditions (10,26,27). Nevertheless, because C-terminal inhibition in the intact channel depends on its association with the pore, our data suggest that these other PANX1 activation mechanisms will also require some disruption of the C terminus from its inhibitory interaction site within the channel pore.…”
Section: Discussionmentioning
confidence: 88%
“…Since their identification in 2000, Panx1 channels have been characterized as ATP release channels that may play a pivotal role in supporting purinergic signaling in a multitude of cell types (2)(3)(4)(5)(6)(7)(8)(9)(10)(11)(12)(13)(14). Importantly, Panx1 channels mediate ATP release from vascular smooth muscle and endothelial cells (7,14), circulating erythrocytes (11,15), airway epithelial cells (13), astrocytes (5,16,17) and T-cells (6,8).…”
Section: S-nitrosylationmentioning
confidence: 99%
“…Instead, recent evidence suggests that Panx1 channels primarily facilitate the release of ATP, which then binds to purinergic receptors (26). The expression of Panx1 in Xenopus oocytes (36) has been found to increase ATP release, whereas siRNA directed against Panx1 suppresses basal ATP release in mouse pituitary At-t20 cells (37).…”
Section: Journal Of Biological Chemistrymentioning
confidence: 99%