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Lipid rafts mediate amyloid-induced calcium dyshomeostasis and oxidative stress in Alzheimer's disease.
[gm1 gangliosidosis]
Several
lines
of
evidence
suggest
that
the
initial
events
of
amyloid-β
peptide
(
Aβ
)
oligomerization
and
deposition
in
Alzheimer
's
disease
(
AD
)
involve
the
interaction
of
soluble
oligomers
with
neuronal
membranes
.
In
this
study
,
we
show
that
Aβ
42
oligomers
are
recruited
to
lipid
rafts
,
which
are
ordered
membrane
microdomains
rich
in
cholesterol
and
gangliosides
,
resulting
in
lipid
peroxidation
,
Ca
(
2
+
)
dyshomeostasis
and
membrane
permeabilization
in
primary
fibroblasts
from
familial
AD
patients
(
FAD
)
bearing
APPVal
717
I
le
,
PS-
1
Leu
392
V
al
or
PS-
1
Met
146
Leu
gene
mutations
.
Moreover
,
the
presence
of
significantly
higher
levels
of
lipid
peroxidation
correlated
with
greater
structural
modification
in
detergent
resistant
domains
(
DRMs
)
isolated
from
APP
and
PS-
1
fibroblasts
,
compared
to
WT
fibroblasts
from
healthy
subjects
.
Modulation
of
raft
GM
1
,
including
modest
depletion
of
GM
1
content
and
interference
with
GM
1
exposure
or
negative
charge
,
precluded
the
interaction
of
amyloid
aggregates
with
the
plasma
membrane
and
the
resulting
cell
damage
in
FAD
fibroblasts
and
rat
brains
cortical
neurons
.
These
findings
suggest
a
specific
role
for
raft
domains
as
primary
mediators
of
amyloid
toxicity
in
AD
neurons
.
Diseases
Validation
Diseases presenting
"ordered membrane microdomains rich in cholesterol and gangliosides"
symptom
gm1 gangliosidosis
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