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Vitamin E but not 17beta-estradiol protects against vascular toxicity induced by beta-amyloid wild type and the Dutch amyloid variant.
[hereditary cerebral hemorrhage with amyloidosis]
Amyloid
beta
-peptide
(
Abeta
)
fibril
deposition
on
cerebral
vessels
produces
cerebral
amyloid
angiopathy
that
appears
in
the
majority
of
Alzheimer
's
disease
patients
.
An
early
onset
of
a
cerebral
amyloid
angiopathy
variant
called
hereditary
cerebral
hemorrhage
with
amyloidosis
of
the
Dutch
type
is
caused
by
a
point
mutation
in
Abeta
yielding
Abeta
(
Glu
22
-
-
>
Gln
)
.
The
present
study
addresses
the
effect
of
amyloid
fibrils
from
both
wild-
type
and
mutated
Abeta
on
vascular
cells
,
as
well
as
the
putative
protective
role
of
antioxidants
on
amyloid
angiopathy
.
For
this
purpose
,
we
studied
the
cytotoxicity
induced
by
Abeta
(
1
-
40
Glu
22
-
-
>
Gln
)
and
Abeta
(
1
-
40
wild-
type
)
fibrils
on
human
venule
endothelial
cells
and
rat
aorta
smooth
muscle
cells
.
We
observed
that
Abeta
(
Glu
22
-
-
>
Gln
)
fibrils
are
more
toxic
for
vascular
cells
than
the
wild-
type
fibrils
.
We
also
evaluated
the
cytotoxicity
of
Abeta
fibrils
bound
with
acetylcholinesterase
(
AChE
)
,
a
common
component
of
amyloid
deposits
.
Abeta
(
1
-
40
wild-
type
)
-
AChE
fibrillar
complexes
,
similar
to
neuronal
cells
,
resulted
in
an
increased
toxicity
on
vascular
cells
.
Previous
reports
showing
that
antioxidants
are
able
to
reduce
the
toxicity
of
Abeta
fibrils
on
neuronal
cells
prompted
us
to
test
the
effect
of
vitamin
E
,
vitamin
C
,
and
17
beta
-estradiol
on
vascular
damage
induced
by
Abeta
(
wild-
type
)
and
Abeta
(
Glu
22
-
-
>
Gln
)
.
Our
data
indicate
that
vitamin
E
attenuated
significantly
the
Abeta-mediated
cytotoxicity
on
vascular
cells
,
although
17
beta
-estradiol
and
vitamin
C
failed
to
inhibit
the
cytotoxicity
induced
by
Abeta
fibrils
.
Diseases
Validation
Diseases presenting
"vascular damage"
symptom
cadasil
erythropoietic protoporphyria
hereditary cerebral hemorrhage with amyloidosis
waldenström macroglobulinemia
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