Výsledky vyhledávání - "A. V. Ilyaskin"

Contributions of bile acids to gastrointestinal physiology as receptor agonists and modifiers of ion channels

Autor: Simona E. Carbone, Stephen J. Keely, Andreacarola Urso, Daniel P. Poole, Christoph Korbmacher, Alexandr V. Ilyaskin, Nigel W. Bunnett

Publikováno v: Am J Physiol Gastrointest Liver Physiol

Bile acids (BAs) are known to be important regulators of intestinal motility and epithelial fluid and electrolyte transport. Over the past two decades, significant advances in identifying and characterizing the receptors, transporters, and ion channe

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e40a183749b54aa29b895cd18516e775
https://pubmed.ncbi.nlm.nih.gov/34755536

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Akademický článek

The Water Permeability Reduction After Successive Hypo-Osmotic Shocks in Kidney Principal Cells is Apically Regulated

Autor: Liubov E. Katkova, Galina S. Baturina, Alexander V. Ilyaskin, Sotirios G. Zarogiannis, Evgeniy I. Solenov

Publikováno v: Cellular Physiology and Biochemistry, Vol 34, Iss 5, Pp 1802-1811 (2014)

Background/Aims: Renal principal cells maintain their intracellular water and electrolyte content despite significant fluctuations of the extracellular water and salt concentrations. Their water permeability decreases rapidly (within a few seconds) a

Externí odkaz: https://doaj.org/article/28c3ec8c25be4129a364f726e2564d9b

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Transmembrane serine protease 2 (TMPRSS2) proteolytically activates the epithelial sodium channel (ENaC) by cleaving the channel’s γ-subunit

Autor: Florian Sure, Marko Bertog, Sara Afonso, Alexei Diakov, Ralf Rinke, M. Gregor Madej, Sabine Wittmann, Thomas Gramberg, Christoph Korbmacher, Alexandr V. Ilyaskin

The epithelial sodium channel (ENaC) is a heterotrimer consisting of α-, β-, and γ-subunits. Channel activation requires proteolytic release of inhibitory tracts from the extracellular domains of α-ENaC and γ-ENaC; however, the proteases involve

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d1647ad897ede0e49595e59a2dbc68df
https://epub.uni-regensburg.de/52234/

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A polycystin-2 protein with modified channel properties leads to an increased diameter of renal tubules and to renal cysts

Publikováno v: Journal of Cell Science
article-version (VoR) Version of Record

Mutations in the PKD2 gene cause autosomal-dominant polycystic kidney disease but the physiological role of polycystin-2, the protein product of PKD2, remains elusive. Polycystin-2 belongs to the transient receptor potential (TRP) family of non-selec

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6b4fd48c1c766e87d3fe6f1f0fe1a9ce
http://europepmc.org/articles/PMC8435292

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Bile acids inhibit human purinergic receptor P2X4 in a heterologous expression system

Autor: Silke Haerteis, Christoph Korbmacher, Viatcheslav Nesterov, Alexandr V. Ilyaskin, Florian Sure

Publikováno v: The Journal of General Physiology

The human purinergic receptor P2X4 is an ATP-gated nonselective cation channel expressed in a variety of cells, including hepatocytes and cholangiocytes. Ilyaskin et al. find that the bile acids inhibit P2X4 by stabilizing the channel's closed state,

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8c2e9f076bb662339288ba0d0b01edb0
http://europepmc.org/articles/PMC6572003

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Zymogen-locked mutant prostasin (Prss8) leads to incomplete proteolytic activation of the epithelial sodium channel (ENaC) and severely compromises triamterene tolerance in mice

Autor: Daniel Essigke, Kerstin Amann, Thomas H. Bugge, Ferruh Artunc, Roman Szabo, Matthias Wörn, Andreas L. Birkenfeld, Bernhard N. Bohnert, Mengyun Xiao, Christoph Korbmacher, Christoph Daniel, Alexandr V. Ilyaskin

Publikováno v: Acta Physiol. 232:e13640 (2021)
Acta Physiol (Oxf)

Aim The serine protease prostasin (Prss8) is expressed in the distal tubule and stimulates proteolytic activation of the epithelial sodium channel (ENaC) in co-expression experiments in vitro. The aim of this study was to explore the role of prostasi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::39dc782ab0453a3ed5733647de3f1fed
https://pubmed.ncbi.nlm.nih.gov/33721422

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Inhibition of the epithelial sodium channel (ENaC) by connexin 30 involves stimulation of clathrin-mediated endocytosis

Autor: Alexei Diakov, Alexandr V. Ilyaskin, Christoph Korbmacher

Publikováno v: The Journal of Biological Chemistry

Mice lacking connexin 30 (Cx30) display increased epithelial sodium channel (ENaC) activity in the distal nephron and develop salt-sensitive hypertension. This indicates a functional link between Cx30 and ENaC, which remains incompletely understood.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ba8597f1fb62923ac7ca334cd47594cf
https://pubmed.ncbi.nlm.nih.gov/33577799

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Proteolytic activation of the epithelial sodium channel (ENaC) by factor VII activating protease (FSAP) and its relevance for sodium retention in nephrotic mice

Autor: Ferruh Artunc, Bernhard N. Bohnert, Jonas C. Schneider, Tobias Staudner, Florian Sure, Alexandr V. Ilyaskin, Matthias Wörn, Daniel Essigke, Andrea Janessa, Nis V. Nielsen, Andreas L. Birkenfeld, Michael Etscheid, Silke Haerteis, Christoph Korbmacher, Sandip M. Kanse

Publikováno v: Pflügers Archiv, 2022(474):217-229
Pflugers Archiv
Pflugers Arch. 474, 217-229 (2022)

Proteolytic activation of the epithelial sodium channel (ENaC) by aberrantly filtered serine proteases is thought to contribute to renal sodium retention in nephrotic syndrome. However, the identity of the responsible proteases remains elusive. This

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f45650f55637d2b812841cb6d95a7372
https://repository.publisso.de/resource/frl:6431670

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Urokinase‐type plasminogen activator (uPA) is not essential for epithelial sodium channel (ENaC)‐mediated sodium retention in experimental nephrotic syndrome

Autor: Ferruh Artunc, Sophie Daiminger, Tobias Staudner, Daniel Essigke, Matthias Wörn, Christoph Korbmacher, Florian Sure, Firas Batbouta, Bernhard N. Bohnert, Sandip M. Kanse, Andrea Janessa, Jonas C Schneider, Alexandr V. Ilyaskin, Silke Haerteis

Publikováno v: Acta Physiol. 227:e13286 (2019)

Aim In nephrotic syndrome, aberrantly filtered plasminogen (plg) is converted to active plasmin by tubular urokinase-type plasminogen activator (uPA) and thought to lead to sodium retention by proteolytic activation of the epithelial sodium channel (

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::69136e8b6141da5f996c3c2e93879ee5
https://doi.org/10.1111/apha.13286

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