Results 11 to 20 of about 22,476 (217)
Acta Physiologica, 2022 AbstractProteases are fundamental for a plethora of biological processes, including signalling and tissue remodelling, and dysregulated proteolytic activity can result in pathogenesis. In this review, we focus on a subclass of membrane‐bound and soluble proteases that are defined as channel‐activating proteases (CAPs), since they induce Na+ ion ...
Deepika Anand +2 more
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The N terminus of α-ENaC mediates ENaC cleavage and activation by furin [PDF]
Journal of General Physiology, 2018 Epithelial Na+ channels comprise three homologous subunits (α, β, and γ) that are regulated by alternative splicing and proteolytic cleavage. Here, we determine the basis of the reduced Na+ current (INa) that results from expression of a previously identified, naturally occurring splice variant of the α subunit (α-ENaC), in which residues 34–82 are ...
Pradeep Kota +4 more
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Biochemistry, 1998 Liddle's disease is an autosomal dominant form of human hypertension resulting from a basal activation of amiloride-sensitive Na+ channels (ENaC). This channel activation is produced by mutations in the beta- and/or gamma-carboxy-terminal cytoplasmic tails, in many cases causing a truncation of the last 45-76 amino acids.
Ismailov, I I +7 more
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ENaC in Cholinergic Brush Cells [PDF]
Frontiers in Cell and Developmental Biology, 2018 Cholinergic polymodal chemosensory cells in the mammalian urethra (urethral brush cells = UBC) functionally express the canonical bitter and umami taste transduction signaling cascade. Here, we aimed to determine whether UBC are functionally equipped for the perception of salt through ENaC (epithelial sodium channel). Cholinergic UBC were isolated from
Kandel C +8 more
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CFTR stabilizes ENaC at the plasma membrane [PDF]
Journal of Cystic Fibrosis, 2007 CFTR was reported to regulate ENaC channel opening, decreasing ENaC activity in airways and increasing it in sweat ducts. We generated MDCK-I cell lines stably expressing tagged alphabetagammaENaC+CFTR or ENaC alone, and developed an assay to quantify cell-surface half-life of ENaC.
Lu, C. +3 more
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Trafficking and cell surface stability of ENaC
American Journal of Physiology-Renal Physiology, 2001 The epithelial Na+channel (ENaC) plays a key role in the regulation of Na+and water absorption in several epithelia, including those of the distal nephron, distal colon, and lung. Accordingly, mutations in ENaC leading to reduced or increased channel activity cause human diseases such as pseudohypoaldosteronism type I or Liddle's syndrome, respectively.
D, Rotin, V, Kanelis, L, Schild
core +4 more sources
Hyperaldosteronism in Mice Lacking the Distal Polybasic Tract of the γ-Subunit of the Epithelial Sodium Channel During Sodium Restriction. [PDF]
Acta Physiol (Oxf)ABSTRACT Aims The epithelial sodium channel ENaC consists of the subunits α, β, and γ and is activated at an individual channel level by proteolytic processing. Murine γENaC contains a distal polybasic tract 186RKRK mediating proteolytic ENaC activation by serine proteases in vitro.
Essigke D +8 more
europepmc +2 more sources
Expression of ENaC subunits in epithelia
Journal of General Physiology, 2022 The epithelial Na+ channel (ENaC) is a heterotrimeric protein whose assembly, trafficking, and function are highly regulated. To better understand the biogenesis and activation of the channel, we quantified the expression of individual subunits of ENaC in rat kidneys and colon using calibrated Western blots.
Gustavo Frindt +4 more
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American Journal of Physiology-Cell Physiology, 2020 Epithelial Na+ channels (ENaCs) are members of a family of cation channels that function as sensors of the extracellular environment. ENaCs are activated by specific proteases in the biosynthetic pathway and at the cell surface and remove embedded inhibitory tracts, which allows channels to transition to higher open-probability states.
Thomas R. Kleyman, Douglas C. Eaton
openaire +3 more sources
Frontiers in Physiology, 2020 Canonical epithelial sodium channels (ENaCs) are heterotrimers formed by α, β, and γ ENaC subunits in vertebrates and belong to the Degenerin/ENaC family of proteins. Proteins from this family form mechanosensitive channels throughout the animal kingdom.
Jan-Peter Baldin +3 more
doaj +1 more source