Plasma kallikrein activates the epithelial sodium channel in vitro but is not essential for volume retention in nephrotic mice-Reference-Cited by-同舟云学术

Plasma kallikrein activates the epithelial sodium channel in vitro but is not essential for volume retention in nephrotic mice

Published:2018-03-25 Issue:1 Volume:224 Page:e13060
ISSN:1748-1708
Container-title:Acta Physiologica
language:en
Short-container-title:Acta Physiol

Author:

Haerteis S.¹,Schork A.²³⁴,Dörffel T.²,Bohnert B. N.²³⁴,Nacken R.¹,Wörn M.²,Xiao M.²,Essigke D.²,Janessa A.²,Schmaier A. H.⁵⁶,Feener E. P.⁷,Häring H.-U.²³⁴,Bertog M.¹,Korbmacher C.¹,Artunc F.²³⁴^ORCID

Affiliation:

1. Institute of Cellular and Molecular Physiology; Friedrich-Alexander University Erlangen-Nürnberg; Erlangen Germany

2. Division of Endocrinology, Diabetology, Vascular Disease, Nephrology and Clinical Chemistry; Department of Internal Medicine; University Hospital Tübingen; Tübingen Germany

3. Institute of Diabetes Research and Metabolic Diseases (IDM) of the Helmholtz Center Munich; University of Tübingen; Tübingen Germany

4. German Center for Diabetes Research (DZD); University of Tübingen; Tübingen Germany

5. Division of Hematology and Oncology; University Hospitals Cleveland Medical Center; Cleveland OH USA

6. Case Western Reserve University; Cleveland OH USA

7. Joslin Diabetes Center; Boston MA USA

Funder

Deutsche Forschungsgemeinschaft

Publisher

Wiley

Subject

Physiology

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1111/apha.13060/fullpdf

Reference35 articles.

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2. ENaC at the cutting edge: regulation of epithelial sodium channels by proteases;Kleyman;J Biol Chem,2009

3. An inhibitory peptide derived from the α-subunit of the epithelial sodium channel (ENaC) shows a helical conformation;Haerteis;Cell Physiol Biochem,2012

4. Cleavage in the {gamma}-subunit of the epithelial sodium channel (ENaC) plays an important role in the proteolytic activation of near-silent channels;Diakov;J Physiol,2008

5. Proteolytic activation of the human epithelial sodium channel by trypsin IV and trypsin I involves distinct cleavage sites;Haerteis;J Biol Chem,2014

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