Purinergic signalling – a possible mechanism for <scp>KCNQ</scp>1 channel response to cell volume challenges

Hammami, Sofia; Willumsen, Niels J.; Meinild, Anne‐Kristine; Klærke, Dan A.; Novak, Ivana

doi:10.1111/j.1748-1716.2012.02460.x

Cited by 8 publications

(7 citation statements)

References 49 publications

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“…K v 7.1 resides in the tubulovesicular and canalicular membranes of gastric parietal cells together with H + –K + -pumps and participates in gastric acid secretion 71 , 74 , 75 . K v 7.1 was localized in the luminal membrane of pancreatic duct cells, 13 and may be involved in cell volume regulation during purinergic stimulation in epithelial transport, 76 , 77 and/or may potentially be associated with H + –K + -pumps expressed by pancreatic ducts 4 …”

Section: Kcnq1 (Kv71 Kvlqt1) and Kcne1 (Mink)mentioning

confidence: 99%

Molecular basis of potassium channels in pancreatic duct epithelial cells

Hayashi

Novak

2013

Channels

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Potassium channels regulate excitability, epithelial ion transport, proliferation, and apoptosis. In pancreatic ducts, K+ channels hyperpolarize the membrane potential and provide the driving force for anion secretion. This review focuses on the molecular candidates of functional K+ channels in pancreatic duct cells, including KCNN4 (KCa3.1), KCNMA1 (KCa1.1), KCNQ1 (Kv7.1), KCNH2 (Kv11.1), KCNH5 (Kv10.2), KCNT1 (KCa4.1), KCNT2 (KCa4.2), and KCNK5 (K2P5.1). We will give an overview of K+ channels with respect to their electrophysiological and pharmacological characteristics and regulation, which we know from other cell types, preferably in epithelia, and, where known, their identification and functions in pancreatic ducts and in adenocarcinoma cells. We conclude by pointing out some outstanding questions and future directions in pancreatic K+ channel research with respect to the physiology of secretion and pancreatic pathologies, including pancreatitis, cystic fibrosis, and cancer, in which the dysregulation or altered expression of K+ channels may be of importance.

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Section: Kcnq1 (Kv71 Kvlqt1) and Kcne1 (Mink)mentioning

confidence: 99%

Molecular basis of potassium channels in pancreatic duct epithelial cells

Hayashi

Novak

2013

Channels

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“…Direct and specific stretch of α 1 integrin elicits Cl − channels functioning in ventricular myocytes, involving angiotensin II release, engagement of AT1 receptors, NADPH oxidase activation, and ROS production [51]. In this context, purinergic P2 and P1 receptors confer some of the KCNQ1 channel volume sensitivity in oocytes, although endogenous adenosine receptors and expressed P2Y2 receptors do so in the negative direction, as responses to cell volume changes [52]. Actually, adenosine restores desensitized angiotensin II-induced contractions in the renal arterioles via intracellular, receptor-independent mechanisms including the p38 mitogen-activated protein kinase (MAPK).…”

Section: Discussionmentioning

confidence: 99%

Rat Liver Enzyme Release Depends on Blood Flow‐Bearing Physical Forces Acting in Endothelium Glycocalyx rather than on Liver Damage

Díaz-Juárez

Hernández‐Muñoz

2017

Oxidative Medicine and Cellular Longevity

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We have found selective elevation of serum enzyme activities in rats subjected to partial hepatectomy (PH), apparently controlled by hemodynamic flow-bearing physical forces. Here, we assess the involvement of stretch-sensitive calcium channels and calcium mobilization in isolated livers, after chemical modifications of the endothelial glycocalyx and changing perfusion directionality. Inhibiting in vivo protein synthesis, we found that liver enzyme release is influenced by de novo synthesis of endothelial glycocalyx components, and released enzymes are confined into a liver “pool.” Moreover, liver enzyme release depended on extracellular calcium entry possibly mediated by stretch-sensitive calcium channels, and this endothelial-mediated mechanotransduction in liver enzyme release was also evidenced by modifying the glycocalyx carbohydrate components, directionality of perfusing flow rate, and the participation of nitric oxide (NO) and malondialdehyde (MDA), leading to modifications in the intracellular distribution of these enzymes mainly as nuclear enrichment of “mitochondrial” enzymes. In conclusion, the flow-induced shear stress may provide fine-tuned control of released hepatic enzymes through mediation by the endothelium glycocalyx, which provides evidence of a biological role of the enzyme release rather to be merely a biomarker for evaluating hepatotoxicity and liver damage, actually positively influencing progression of liver regeneration in mammals.

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“…ATP in the extracellular milieu of maturing follicles is derived from the follicular cells and the oocyte (Aleu et al, 2003;Bodas et al, 2000;Hammami et al, 2013;Maroto and Hamill, 2001), and is controlled by the actions of ectonucleotidases. The activity of ecto-5′nucleotidase in corpora lutea of mice changes during the estrous cycle, being maximal at the pre-estrous phase .…”

Section: Oocytes and Ovarian Folliclesmentioning

confidence: 99%