Zobrazeno 1 - 10
of 48
pro vyhledávání: '"Ivan Gautschi"'
Autor:
Sophie Roy, Niklaus Johner, Viktor Trendafilov, Ivan Gautschi, Olivier Bignucolo, Ophélie Molton, Simon Bernèche, Stephan Kellenberger
Publikováno v:
Open Biology, Vol 12, Iss 12 (2022)
The extracellular Ca2+ concentration changes locally under certain physiological and pathological conditions. Such variations affect the function of ion channels of the nervous system and consequently also neuronal signalling. We investigated here th
Externí odkaz:
https://doaj.org/article/555c8ce8e3da400bb0f217a5277dac57
Publikováno v:
Frontiers in Molecular Biosciences, Vol 7 (2020)
Acid-sensing ion channels (ASICs) act as pH sensors in neurons. ASICs contribute to pain sensation, learning, fear behavior and to neuronal death after ischemic stroke. Extracellular acidification induces a transient activation and subsequent desensi
Externí odkaz:
https://doaj.org/article/f4313c1db3b44327941672b517f72f2a
Publikováno v:
Frontiers in Physiology, Vol 9 (2018)
SLC2A9 or Glut9 is a voltage sensitive urate transporter, mainly expressed in the kidneys, the liver, and the intestine. Human Glut9 loss-of-function mutations were identified in familial hypouricemia, and several single nucleotide polymorphisms (SNP
Externí odkaz:
https://doaj.org/article/d6c00967366a4b14a3576735bade4fa4
Publikováno v:
PLoS ONE, Vol 12, Iss 4, p e0175293 (2017)
The Acid-Sensing Ion Channels (ASIC) exhibit a fast desensitizing current when activated by pH values below 7.0. By contrast, non-proton ligands are able to trigger sustained ASIC currents at physiological pHs. To analyze the functional basis of the
Externí odkaz:
https://doaj.org/article/524f60438fe34c97893bb3ab75180f56
Publikováno v:
PLoS ONE, Vol 10, Iss 8, p e0135191 (2015)
The chicken acid-sensing ion channel ASIC1 has been crystallized as a homotrimer. We address here the oligomeric state of the functional ASIC1 in situ at the cell surface. The oligomeric states of functional ASIC1a and mutants with additional cystein
Externí odkaz:
https://doaj.org/article/15b7c4e0f6b7422187e470be9dc57879
Publikováno v:
PLoS ONE, Vol 9, Iss 4, p e94267 (2014)
Membrane-bound serine proteases play important roles in different biological processes. Their regulation by endogenous inhibitors is poorly understood. A Y163C mutation in the SPINT2 gene encoding the serine protease inhibitor Hepatocyte Growth Facto
Externí odkaz:
https://doaj.org/article/02e7089b27bd4b1a993b62bf096c9aac
Autor:
Alexandra Eythymiadou, Ivan Gautschi, Miguel Xavier van Bemmelen, Amalia Sertedaki, Aristeidis Giannakopoulos, George Chrousos, Laurent Schild, Dionisios Chrysis
Publikováno v:
American Journal of Physiology-Endocrinology and Metabolism.
Objective: To investigate the genetic etiology in a cohort of patients with a clinical, biochemical, and hormonal profile suggestive of a mild and transient form of PHA1. Patients - Methods: Twelve PHA1 patients with clinical and biochemical data wer
Publikováno v:
Journal of Molecular and Cellular Cardiology. 173:157-158
Publikováno v:
The FASEB Journal. 36
Autor:
Elodie Ehret, Yannick Jäger, Chloé Sergi, Anne-Marie Mérillat, Thibaud Peyrollaz, Deepika Anand, Qing Wang, Fréderique Ino, Marc Maillard, Stephan Kellenberger, Ivan Gautschi, Roman Szabo, Thomas H. Bugge, Lotte K. Vogel, Edith Hummler, Simona Frateschi
Publikováno v:
Ehret, E, Jäger, Y, Sergi, C, Mérillat, A M, Peyrollaz, T, Anand, D, Wang, Q, Ino, F, Maillard, M, Kellenberger, S, Gautschi, I, Szabo, R, Bugge, T H, Vogel, L K, Hummler, E & Frateschi, S 2022, ' Kidney-Specific CAP1/Prss8-Deficient Mice Maintain ENaC-Mediated Sodium Balance through an Aldosterone Independent Pathway ', International Journal of Molecular Sciences, vol. 23, no. 12, 6745 . https://doi.org/10.3390/ijms23126745
International journal of molecular sciences, vol. 23, no. 12, pp. 6745
International Journal of Molecular Sciences; Volume 23; Issue 12; Pages: 6745
International journal of molecular sciences, vol. 23, no. 12, pp. 6745
International Journal of Molecular Sciences; Volume 23; Issue 12; Pages: 6745
The serine protease prostasin (CAP1/Prss8, channel-activating protease-1) is a confirmed in vitro and in vivo activator of the epithelial sodium channel ENaC. To test whether proteolytic activity or CAP1/Prss8 abundance itself are required for ENaC a