Epithelial sodium

channel

The epithelial sodium channel (short: ENaC, also: amiloride-sensitive sodium channel) is a
+

membrane-bound ion channel that is selectively permeable to the ions of sodium (Na ) and that
is assembled as a heterotrimer composed of three homologous subunits α or δ, β, and γ,[2]
These subunits are encoded by four genes: SCNN1A, SCNN1B, SCNN1G, and SCNN1D. It is
involved primarily in the reabsorption of sodium ions at the collecting ducts of the kidney's
nephrons. In addition to being implicated in diseases where fluid balance across epithelial
membranes is perturbed, including pulmonary edema, cystic fibrosis, COPD and COVID-19,
proteolyzed forms of ENaC function as the human salt taste receptor.[3]
 Amiloride-sensitive sodium channel

Structure of human ENaC.[1]

Identifiers

Symbol ASC

Pfam PF00858 (http://pfam.xfam.org/family?acc=PF00

858)

InterPro IPR001873 (https://www.ebi.ac.uk/interpro/entry/

IPR001873)

PROSITE PDOC00926 (https://prosite.expasy.org/PDOC009

26)

SCOP2 6BQN (http://scop2.mrc-lmb.cam.ac.uk/search?t=

txt;q=6BQN) / SCOPe (https://scop.berkeley.ed
u/pdb/code=6BQN) / SUPFAM (http://supfam.or
g/SUPERFAMILY/cgi-bin/search.cgi?search_field=
6BQN)

TCDB 1.A.6 (http://www.tcdb.org/search/result.php?tc=

1.A.6)

OPM superfamily 181 (https://opm.phar.umich.edu/protein_superfa

milies/181)

OPM protein 4fz1 (https://opm.phar.umich.edu/proteins?searc

h=4fz1)

Available protein structures:

Pfam
  structures (http://pfam.xfam.org/family/PF00858?ta
b=pdbBlock) / ECOD (http://prodata.swmed.edu/ec
od/complete/search?kw=PF00858)
 
 PDB RCSB PDB (https://www.rcsb.org/search?q=rcsb_poly
mer_entity_annotation.annotation_id:PF00858%20AN
D%20rcsb_polymer_entity_annotation.type:Pfam) ;
PDBe (https://www.ebi.ac.uk/pdbe/entry/search/inde
x?pfam_accession:PF00858) ; PDBj (https://pdbj.or
g/searchFor?query=PF00858)
PDBsum structure summary (https://www.ebi.ac.uk/thornton-s
rv/databases/cgi-bin/pdbsum/GetPfamStr.pl?pfam_i
d=PF00858)

PDB 6BQN

The apical membranes of many tight epithelia contain sodium channels that are characterized
primarily by their high affinity for the diuretic blocker amiloride.[2][4][5][6] These channels mediate
the first step of active sodium reabsorption essential for the maintenance of body salt and water
homeostasis.[4] In vertebrates, the channels control reabsorption of sodium in kidney, colon, lung
and sweat glands; they also play a role in taste perception.

The epithelial sodium channels are structurally and probably evolutionary related to P2X
purinoreceptors, pain receptors that activate when they detect ATP.

Location and function

ENaC is located in the apical membrane of polarized epithelial cells in particular in the kidney
(primarily in the collecting tubule), the lung, the skin,[7] the male and female reproductive tracts
and the colon.[2][8][9] Epithelial sodium channels facilitate Na⁺ reabsorption across the apical
membranes of epithelia in the distal nephron, respiratory and reproductive tracts and exocrine
glands. Since Na⁺ ion concentration is a major determinant of extracellular fluid osmolarity,
changes in Na⁺ concentration affect the movement of fluids and consequently fluid volume and
blood pressure. The activity of ENaC in the colon and kidney is modulated by the
mineralcorticoid aldosterone. It can be blocked by either triamterene or amiloride, which are
used medically to serve as diuretics. In the kidney, it is inhibited by atrial natriuretic peptide,
causing natriuresis and diuresis.

Epithelial Na+ channels (ENaCs) in the brain play a significant role in the regulation of blood
pressure.[10] Vasopressin (VP) neurons play a pivotal role in coordinating neuroendocrine and
autonomic responses to maintain cardiovascular homeostasis. High dietary salt intake causes
an increase in the expression and activity of ENaC which results in the steady state
depolarization of VP neurons.[10] This is one of the mechanisms underlying how dietary salt
intake affects the activity of VP neurons via ENaC activity. ENaC channels in the brain are
involved in blood pressure response to dietary sodium.

High-resolution immunofluorescence studies revealed that in the respiratory tract and the
female reproductive tract, ENaC is located along the entire length of cilia that cover the surface
of multi-ciliated cells.[8] Hence, in these epithelia with motile cilia, ENaC functions as a regulator
of the osmolarity of the periciliary fluid, and its function is essential to maintain fluid volume at a
depth necessary for the motility of the cilia. In the respiratory tract this movement is essential
for clearing mucosal surface, and in the female reproductive tract, motility of the cilia is
essential for the movement of oocytes.[8]

In contrast to ENaC, CFTR that regulates chloride ion transport is not found on cilia. These
findings contradict a previous hypothesis that ENaC is downregulated by direct interaction with
CFTR. In patients with cystic fibrosis (CF), CFTR cannot downregulate ENaC, causing hyper-
absorption in the lungs and recurrent lung infections. It has been suggested that it may be a
ligand-gated ion channel.[11]

In the skin epidermal layers, ENaC is expressed in the keratinocytes, sebaceous glands, and
smooth muscle cells.[7] In these cells ENaC is mostly located in the cytoplasm.[7] In the eccrine
sweat glands, ENaC is predominantly located in the apical membrane facing the lumen of the
sweat ducts.[7] The major function of ENaC in these ducts is the re-uptake of Na⁺ ions that are
excreted in sweat. In patients with ENaC mutations that cause systemic
pseudohypoaldosteronism type I, the patients can lose a significant amount of Na⁺ ions,
especially under hot climates.

ENaC is also found in taste receptors, where it plays an important role in saltiness perception. In
rodents, virtually the entire salt taste is mediated by ENaC, whereas it seems to play a less
significant role in humans: About 20 percent can be accredited to the epithelial sodium channel.

Protoelyzed variants of ENaC also function as human salt taste receptors. This role was first
confirmed using human sensory studies to evaluate the effect of 4-propylphenyl 2-furoate on the
perception of the salty taste of table salt, sodium chloride (NaCl). 4-propylphenyl 2-furoate is a
compound that was discovered to activate proteolyzed ENaC.[12]

Ion selectivity
 +
+

Studies show that the ENaC channel is permeable to Na and Li ions, but has very little
+
+
+

permeability to K , Cs or Rb ions.[13][14]

Transport reaction
+

The generalized transport reaction for Na channels is:

+
+

Na (out) → Na (in)

That for the degenerins is:

Cation (out) → cation (in)

Structure

A diagram demonstrating the arrangement of the subunits

ENaC consists of three different subunits: α, β, γ.[2][15] All three subunits are essential for
transport to the membrane assembly of functional channels on the membrane.[16] The C-
terminus of each ENaC subunit contains a PPXY motif which when mutated or deleted in either
the β- or γ-ENaC subunit leads to Liddle's syndrome, a human autosomal dominant form of
hypertension. The cryoEM structure of ENaC indicates that the channel is a heterotrimeric
protein like the acid-sensing ion channel 1 (ASIC1), which belongs to the same family.[17][18] Each
of the subunits consists of two transmembrane helices and an extracellular loop. The amino-
and carboxy-termini of all three polypeptides are located in the cytosol.
Crystal structure of ASIC1 and site-directed mutagenesis studies suggest that ENaC has a
central ion channel located along the central symmetry axis in between the three subunits.[14][19]

In terms of structure, the proteins that belong to this family consist of about 510 to 920 amino
acid residues. They are made of an intracellular N-terminus region followed by a transmembrane
domain, a large extracellular loop, a second transmembrane segment, and a C-terminal
intracellular tail.[20]

δ-subunit

In addition there is a fourth, so-called δ-subunit, that shares considerable sequence similarity
with the α-subunit and can form a functional ion-channel together with the β- and γ-subunits.
Such δ-, β-, γ-ENaC appear in pancreas, testes, lung, and ovaries. Their function is yet unknown.

Families
+

Members of the epithelial Na channel (ENaC) family fall into four subfamilies, termed alpha,
beta, gamma and delta.[5] The proteins exhibit the same apparent topology, each with two
transmembrane (TM)-spanning segments (TMS), separated by a large extracellular loop. In most
ENaC proteins studied to date, the extracellular domains are highly conserved and contain
numerous cysteine residues, with flanking C-terminal amphipathic TM regions, postulated to
contribute to the formation of the hydrophilic pores of the oligomeric channel protein
complexes. It is thought that the well-conserved extracellular domains serve as receptors to
control the activities of the channels.

The vertebrate ENaC proteins from epithelial cells cluster tightly together on the phylogenetic
tree; voltage-insensitive ENaC homologues are also found in the brain. The many sequenced C.
elegans proteins, including the worm degenerins, are distantly related to the vertebrate proteins
as well as to each other. Vertebrate ENaC proteins are similar to degenerins of Caenorhabditis
elegans:[20] deg-1, del-1, mec-4, mec-10 and unc-8. These proteins can be mutated to cause
neuronal degradation, and are also thought to form sodium channels.

Superfamily
+

The epithelial sodium (Na ) channel (ENaC) family belongs to the ENaC/P2X superfamily.[21]
ENaC and P2X receptors have similar 3-d structures and are homologous.[22]
 Genes

The exon–intron architecture of the three genes encoding the three subunits of ENaC have
remained highly conserved despite the divergence of their sequences.[23]

SCNN1A, SCNN1B, SCNN1G, SCNN1D

There are four related amiloride sensitive sodium channels:

ACCN1, ACCN2, ACCN3, ACCN4

Stable ENaC Cell Line

Expression of ENaC in mammalian cell cultures is cytotoxic, resulting in sodium uptake, cell
swelling and cell death, complicating production of stable cell lines to study ENaC. Chromovert
technology enabled the production of a stable ENaC cell line using fluorogenic signaling probes
and flow cytometry to scan numerous cells to isolate rare clones capable of functional, stable
and viable expression of ENaC.[24]

Clinical significance

Structure of amiloride, a channel blocker

ENaC interaction with CFTR is of important pathophysiological relevance in cystic fibrosis. CFTR
is a transmembrane channel responsible for chloride transport and defects in this protein cause
cystic fibrosis, partly through upregulation of the ENaC channel in the absence of functional
CFTR.
In the airways, CFTR allows for the secretion of chloride, and sodium ions and water follow
passively. However, in the absence of functional CFTR, the ENaC channel is upregulated, and
further decreases salt and water secretion by reabsorbing sodium ions. As such, the respiratory
complications in cystic fibrosis are not solely caused by the lack of chloride secretion but
instead by the increase in sodium and water reabsorption. This results in the deposition of thick,
dehydrated mucus, which collects in the respiratory tract, interfering with gas exchange and
allowing for the collection of bacteria.[25] Nevertheless, an upregulation of CFTR does not
correct the influence of high-activity ENaC.[26] Probably other interacting proteins are necessary
to maintain a functional ion homeostasis in epithelial tissue of the lung, like potassium channels,
aquaporins or Na/K-ATPase.[27]

In sweat glands, CFTR is responsible for the reabsorption of chloride in the sweat duct. Sodium
ions follow passively through ENaC as a result of the electrochemical gradient caused by
chloride flow. This reduces salt and water loss. In the absence of chloride flow in cystic fibrosis,
sodium ions do not flow through ENaC, leading to greater salt and water loss. (This is true
despite upregulation of the ENaC channel, as flow in the sweat ducts is limited by the
electrochemical gradient set up by chloride flow through CFTR.) As such, patients' skin tastes
salty, and this is commonly used to help diagnose the disease, both in the past and today by
modern electrical tests.[28]

Gain of function mutations to the β and γ subunits are associated with Liddle's syndrome.[29]

Amiloride and triamterene are potassium-sparing diuretics that act as epithelial sodium channel
blockers.

References

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muscular/mother/chan.html#nachnvg)

External links

Epithelial+sodium+channel (https://meshb.nlm.nih.gov/record/ui?name=Epithelial%20sodiu
m%20channel) at the US National Library of Medicine Medical Subject Headings (MeSH)
This article incorporates text from the public domain Pfam and InterPro: IPR001873 (https://www.e
bi.ac.uk/interpro/entry/IPR001873)

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