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J. Biol. Chem., Vol. 277, Issue 10, 8338-8345, March 8, 2002
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From the The epithelial sodium channel (ENaC) constitutes
the rate-limiting step for sodium absorption across airway epithelia,
which in turn regulates airway surface liquid (ASL) volume and the
efficiency of mucociliary clearance. This role in ASL volume regulation
suggests that ENaC activity is influenced by local factors rather than systemic signals indicative of total body volume homeostasis. Based on
reports that ENaC may be regulated by extracellular serine protease
activity in Xenopus and mouse renal epithelia, we sought to
identify proteases that serve similar functions in human airway epithelia. Homology screening of a human airway epithelial cDNA library identified two trypsin-like serine proteases (prostasin and
TMPRSS2) that, as revealed by in situ hybridization, are
expressed in airway epithelia. Functional studies in the
Xenopus oocyte expression system demonstrated that
prostasin increased ENaC currents 60-80%, whereas TMPRSS2 markedly
decreased ENaC currents and protein levels. Studies of primary nasal
epithelial cultures in Ussing chambers revealed that inhibition of
endogenous serine protease activity with aprotinin markedly decreased
ENaC-mediated currents and sensitized the epithelia to subsequent
channel activation by exogenous trypsin. These data, therefore, suggest
that protease-mediated regulation of sodium absorption is a function of
human airway epithelia, and prostasin is a likely candidate for this activity.
Regulation of the Epithelial Sodium Channel by Serine Proteases
in Human Airways*
§¶,,,,
,§, and**
Cystic Fibrosis Research and Treatment
Center, § Department of Medicine, and
** Department of Pediatrics, University of North Carolina at
Chapel Hill, Chapel Hill, North Carolina 27599 and the
Department of Biochemistry and Molecular Biology, Medical
University of South Carolina, Charleston, South Carolina 29425
*
This work was supported by Grants L543 (to S. H. D.) and
R026 (to R. C. B., S. H. D.) from the Cystic Fibrosis Foundation, and Grant HL62564 from the National Institutes of Health (to
S. E. G.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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