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Novel decorin mutation in a Chinese family with congenital stromal corneal dystrophy.
[]
The
aim
of
this
study
was
to
characterize
the
congenital
stromal
corneal
dystrophy
(
CSCD
)
pathological
and
clinical
phenotype
in
a
Chinese
family
with
a
novel
mutation
of
decorin
and
its
possible
molecular
pathogenesis
.
Molecular
genetic
analyses
were
performed
on
5
patients
with
CSCD
.
Clinical
characteristics
,
optical
coherence
tomography
,
and
confocal
microscopic
study
were
evaluated
.
The
corneal
specimens
from
patients
with
CSCD
were
sent
for
light
and
electron
microscopic
evaluation
.
A
protein
modeling
study
was
carried
out
to
assess
the
effect
of
the
mutation
on
the
protein
structure
.
Sequencing
analysis
of
DCN
revealed
that
all
patients
with
CSCD
were
heterozygous
for
a
1
-
bp
deletion
at
nucleotide
962
(
c
.
962
delA
)
in
exon
8
.
This
causes
a
premature
termination
of
the
decorin
protein
by
frameshift
,
causing
the
deletion
of
33
amino
acids
in
the
C-
terminal
end
of
the
decorin
protein
.
Optical
coherence
tomography
and
confocal
microscopic
study
demonstrated
that
the
corneal
lamellar
structure
was
disrupted
and
that
this
is
more
severe
in
the
anterior
and
posterior
central
stroma
.
Histopathological
study
showed
that
electron-lucent
zones
were
present
between
the
normal-appearing
collagen
lamellae
in
the
patients
with
CSCD
.
Abnormally
thinned
collagen
filaments
were
identified
in
the
electron-lucent
zones
,
which
could
be
due
to
abnormal
decorin
binding
to
the
collagen
microfibrils
.
Protein
modeling
studies
involving
wild-
type
and
mutant
protein
indicated
that
mutant
decorin
might
be
unable
to
bind
to
all
4
collagen
microfibrils
as
the
normal
decorin
would
.
We
present
the
clinical
,
histopathological
,
and
molecular
genetic
assessment
of
a
Chinese
family
with
CSCD
in
which
a
novel
DCN
mutation
was
identified
.
Our
findings
add
to
the
allelic
heterogeneity
of
this
rare
form
of
inherited
corneal
disease
.
