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Cell and Transport Physiology
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Cell-Surface Expression of the Channel Activating Protease xCAP-1 Is Required for Activation of ENaC in the Xenopus Oocyte

Véronique Vallet, Corinne Pfister, Johannes Loffing and Bernard C. Rossier
JASN March 2002, 13 (3) 588-594;
Véronique Vallet
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Corinne Pfister
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Johannes Loffing
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Bernard C. Rossier
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Article Information

vol. 13 no. 3 588-594
PubMed 
11856761

Published By 
American Society of Nephrology
Print ISSN 
1046-6673
Online ISSN 
1533-3450
History 
  • Received for publication October 17, 2001
  • Accepted for publication November 15, 2001
  • Published online March 1, 2002.

Copyright & Usage 
© 2002 American Society of Nephrology

Author Information

  1. Véronique Vallet*,
  2. Corinne Pfister*,
  3. Johannes Loffing† and
  4. Bernard C. Rossier*
  1. *Institute of Pharmacology and Toxicology, University of Lausanne, Lausanne, Switzerland; and †Institute of Anatomy, University of Zurich, Zurich, Switzerland.
  1. Correspondence to: Prof. Bernard C. Rossier, Institut de Pharmacologie et de Toxicologie, Rue du Bugnon 27, CH-1005 Lausanne, Switzerland. Phone: +4121-692-5351; Fax: +4121-692-5355; E-mail: Bernard.Rossier{at}ipharm.unil.ch
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Journal of the American Society of Nephrology: 13 (3)
Journal of the American Society of Nephrology
Vol. 13, Issue 3
1 Mar 2002
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Cell-Surface Expression of the Channel Activating Protease xCAP-1 Is Required for Activation of ENaC in the Xenopus Oocyte
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Cell-Surface Expression of the Channel Activating Protease xCAP-1 Is Required for Activation of ENaC in the Xenopus Oocyte
Véronique Vallet, Corinne Pfister, Johannes Loffing, Bernard C. Rossier
JASN Mar 2002, 13 (3) 588-594;

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Cell-Surface Expression of the Channel Activating Protease xCAP-1 Is Required for Activation of ENaC in the Xenopus Oocyte
Véronique Vallet, Corinne Pfister, Johannes Loffing, Bernard C. Rossier
JASN Mar 2002, 13 (3) 588-594;
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More in this TOC Section

  • Acute Regulation of the Epithelial Na+ Channel by Phosphatidylinositide 3-OH Kinase Signaling in Native Collecting Duct Principal Cells
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  • Increased Renal Responsiveness to Vasopressin and Enhanced V2 Receptor Signaling in RGS2−/− Mice
Show more Cell and Transport Physiology

Cited By...

  • GPI-anchored carbonic anhydrase IV displays both intra- and extracellular activity in cRNA-injected oocytes and in mouse neurons
  • Cathepsin B Is Secreted Apically from Xenopus 2F3 Cells and Cleaves the Epithelial Sodium Channel (ENaC) to Increase Its Activity
  • The cutting edge: membrane-anchored serine protease activities in the pericellular microenvironment
  • ENaC-mediated alveolar fluid clearance and lung fluid balance depend on the channel-activating protease 1
  • Alternative Mechanism of Activation of the Epithelial Na+ Channel by Cleavage
  • ENaC Proteolytic Regulation by Channel-activating Protease 2
  • MEC-2 and MEC-6 in the Caenorhabditis elegans Sensory Mechanotransduction Complex: Auxiliary Subunits that Enable Channel Activity
  • Defective ENaC Processing and Function in Tissue Kallikrein-deficient Mice
  • Indirect Activation of the Epithelial Na+ Channel by Trypsin
  • Acute Downregulation of ENaC by EGF Involves the PY Motif and Putative ERK Phosphorylation Site
  • Epithelial Na+ Channels Are Fully Activated by Furin- and Prostasin-dependent Release of an Inhibitory Peptide from the {gamma}-Subunit
  • Activation of Epithelial Sodium Channels by Mouse Channel Activating Proteases (mCAP) Expressed in Xenopus Oocytes Requires Catalytic Activity of mCAP3 and mCAP2 but not mCAP1
  • Trypsin Cleaves Acid-sensing Ion Channel 1a in a Domain That Is Critical for Channel Gating
  • Endogenous Protease Activation of ENaC: Effect of Serine Protease Inhibition on ENaC Single Channel Properties
  • Maturation of the Epithelial Na+ Channel Involves Proteolytic Processing of the {alpha}- and {gamma}-Subunits
  • Structure and Activity of Human Pancreasin, a Novel Tryptic Serine Peptidase Expressed Primarily by the Pancreas
  • Inhibition of Prostasin Secretion by Serine Protease Inhibitors in the Kidney
  • Synergistic Activation of ENaC by Three Membrane-bound Channel-activating Serine Proteases (mCAP1, mCAP2, and mCAP3) and Serum- and Glucocorticoid-regulated Kinase (Sgk1) in Xenopus Oocytes
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