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Regulation of pendrin by pH: dependence on glycosylation.
[pendred syndrome]
Mutations
in
the
anion
exchanger
pendrin
are
responsible
for
Pendred
syndrome
,
an
autosomal
recessive
disease
characterized
by
deafness
and
goitre
.
Pendrin
is
highly
expressed
in
kidney
collecting
ducts
,
where
it
acts
as
a
chloride
/
bicarbonate
exchanger
and
thereby
contributes
to
the
regulation
of
acid-base
homoeostasis
and
blood
pressure
.
The
present
study
aimed
to
characterize
the
intrinsic
properties
of
pendrin
.
Mouse
pendrin
was
transfected
in
HEK
(
human
embryonic
kidney
)
293
and
OKP
(
opossum
kidney
proximal
tubule
)
cells
and
its
activity
was
determined
by
monitoring
changes
in
the
intracellular
pH
induced
by
variations
of
transmembrane
anion
gradients
.
Combining
measurements
of
pendrin
activity
with
mathematical
modelling
we
found
that
its
affinity
for
Cl-
,
HCO
3
-
and
OH
-
varies
with
intracellular
pH
,
with
increased
activity
at
low
intracellular
pH
.
Maximal
pendrin
activity
was
also
stimulated
at
low
extracellular
pH
,
suggesting
the
presence
of
both
intracellular
and
extracellular
proton
regulatory
sites
.
We
identified
five
putative
pendrin
glycosylation
sites
,
only
two
of
which
are
used
.
Mutagenesis-induced
disruption
of
pendrin
glycosylation
did
not
alter
its
cell-surface
expression
or
polarized
targeting
to
the
apical
membrane
and
basal
activity
,
but
fully
abrogated
its
sensitivity
to
extracellular
pH
.
The
hither
to
unknown
regulation
of
pendrin
by
external
pH
may
constitute
a
key
mechanism
in
controlling
ionic
exchanges
across
the
collecting
duct
and
inner
ear
.
Diseases
Validation
Diseases presenting
"increased activity at low intracellular ph"
symptom
pendred syndrome
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