Activation of the amiloride-sensitive epithelial sodium channel by the serine protease mCAP1 expressed in a mouse cortical collecting duct cell line

Détails

ID Serval
serval:BIB_58082E4DD25F
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Activation of the amiloride-sensitive epithelial sodium channel by the serine protease mCAP1 expressed in a mouse cortical collecting duct cell line
Périodique
Journal of the American Society of Nephrology
Auteur(s)
Vuagniaux  G., Vallet  V., Jaeger  N. F., Pfister  C., Bens  M., Farman  N., Courtois-Coutry  N., Vandewalle  A., Rossier  B. C., Hummler  E.
ISSN
1046-6673
Statut éditorial
Publié
Date de publication
05/2000
Peer-reviewed
Oui
Volume
11
Numéro
5
Pages
828-34
Notes
Journal Article
Research Support, Non-U.S. Gov't --- Old month value: May
Résumé
This study examines whether serine proteases can activate the amiloride-sensitive sodium channel (ENaC) in mammalian kidney epithelial cells. The transepithelial sodium transport assessed by amiloride-sensitive short-circuit current appears to be sensitive to aprotinin, a protease inhibitor in a mouse cortical collecting duct cell line (mpkCCD(c14)). This result indicated that serine proteases may be implicated in the regulation of ENaC-mediated sodium transport. Using degenerated oligonucleotides to a previously isolated serine protease from Xenopus, xCAP1 (channel activating protease), a novel full-length serine protease (mCAP1), has been isolated and characterized. RNA analysis showed a broad pattern of expression in tissues (kidney, lung, colon, and salivary glands) expressing ENaC. Reverse transcription-PCR experiments also showed that mCAP1 was abundantly expressed in proximal tubule cells and was also expressed in intact and cultured collecting duct cells. Coexpression of the Xenopus, rat, or human alpha-, beta-, and gamma-ENaC subunits in Xenopus oocytes also showed that mCAP1 induces a significant increase in ENaC-mediated current accompanied by a decrease of channel molecules at the cell surface. It is proposed that this novel mouse channel activating protease may act as a regulator of ENaC within the kidney.
Mots-clé
Amiloride/*pharmacology Amino Acid Sequence Animals Aprotinin/pharmacology Blotting, Northern Cell Line DNA, Complementary Diuretics/*pharmacology Electrophysiology Humans Kidney Tubules, Collecting/cytology/*metabolism Mice Molecular Sequence Data Oocytes/drug effects RNA, Messenger/metabolism Rats Reverse Transcriptase Polymerase Chain Reaction Sequence Homology, Amino Acid Serine Endopeptidases/genetics/*metabolism Serine Proteinase Inhibitors/pharmacology Sodium/metabolism Sodium Channels/*drug effects/*metabolism Xenopus *Xenopus Proteins
Pubmed
Web of science
Création de la notice
24/01/2008 14:00
Dernière modification de la notice
20/08/2019 15:11
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