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Ultrastructural evidence of early non-fibrillar Abeta42 in the capillary basement membrane of patients with hereditary cerebral hemorrhage with amyloidosis, Dutch type.
[hereditary cerebral hemorrhage with amyloidosis]
The
C-
terminal
profile
and
ultrastructure
of
small
and
presumably
early
capillary
amyloid
beta
protein
(
Abeta
)
deposits
were
investigated
in
four
patients
with
hereditary
cerebral
hemorrhage
with
amyloidosis
,
Dutch
type
.
The
C
terminus
of
the
40
(
Abeta
40
)
or
the
42
(
Abeta
42
)
amino
acid
form
of
Abeta
was
gold
labeled
in
serial
,
ultrathin
sections
on
glass
slides
for
reflection
contrast
microscopy
and
on
grids
for
electron
microscopy
.
In
all
studied
subjects
,
reflection
contrast
microscopy
revealed
capillaries
with
focal
Abeta
42
immunolabeling
in
the
absence
of
Abeta
40
labeling
.
In
the
adjacent
electron
microscopic
section
,
Abeta
42
labeling
was
confined
to
the
capillary
basement
membrane
.
The
majority
of
Abeta
42
(
+
)
40
(
-
)
deposits
showed
no
amyloid
fibrils
.
Abeta
42
(
+
)
40
(
-
)
deposits
were
sometimes
observed
in
an
unremarkable
basement
membrane
but
usually
showed
increased
electron
density
and
reticular
structures
.
A
small
subset
of
Abeta
42
(
+
)
40
(
-
)
deposits
with
basement
membrane
changes
showed
few
amyloid
fibrils
.
Abeta
42
(
+
)
40
(
+
)
capillary
deposits
always
showed
definite
fibrils
and
were
larger
than
Abeta
42
(
+
)
40
(
-
)
capillary
deposits
.
The
present
findings
suggest
that
in
capillaries
the
accumulation
and
subsequent
polymerization
of
Abeta
42
,
possibly
in
conjunction
with
basement
membrane
changes
,
precedes
the
definite
fibril
formation
with
Abeta
40
.
Diseases
Validation
Diseases presenting
"deposits"
symptom
hereditary cerebral hemorrhage with amyloidosis
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