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Crystallin proteins and amyloid fibrils.
[alexander disease]
Improper
protein
folding
(
misfolding
)
can
lead
to
the
formation
of
disordered
(
amorphous
)
or
ordered
(
amyloid
fibril
)
aggregates
.
The
major
lens
protein
,
alpha-crystallin
,
is
a
member
of
the
small
heat-shock
protein
(
sHsp
)
family
of
intracellular
molecular
chaperone
proteins
that
prevent
protein
aggregation
.
Whilst
the
chaperone
activity
of
sHsps
against
amorphously
aggregating
proteins
has
been
well
studied
,
its
action
against
fibril-forming
proteins
has
received
less
attention
despite
the
presence
of
sHsps
in
deposits
found
in
fibril-associated
diseases
(
e
.
g
.
Alzheimer
's
and
Parkinson
's
)
.
In
this
review
,
the
literature
on
the
interaction
of
alphaB-crystallin
and
other
sHsps
with
fibril-forming
proteins
is
summarized
.
In
particular
,
the
ability
of
sHsps
to
prevent
fibril
formation
,
their
mechanisms
of
action
and
the
possible
in
vivo
consequences
of
such
associations
are
discussed
.
Finally
,
the
fibril-forming
propensity
of
the
crystallin
proteins
and
its
implications
for
cataract
formation
are
described
along
with
the
potential
use
of
fibrillar
crystallin
proteins
as
bionanomaterials
.
Diseases
Validation
Diseases presenting
"attention despite the presence of shsps in deposits"
symptom
alexander disease
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