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Distinct 3-O-sulfated heparan sulfate modification patterns are required for kal-1-dependent neurite branching in a context-dependent manner in Caenorhabditis elegans.
[kallmann syndrome]
Heparan
sulfate
(
HS
)
is
an
unbranched
glycosaminoglycan
exhibiting
substantial
molecular
diversity
due
to
multiple
,
nonuniformly
introduced
modifications
,
including
sulfations
,
epimerization
,
and
acetylation
.
HS
modifications
serve
specific
and
instructive
roles
in
neuronal
development
,
leading
to
the
hypothesis
of
a
HS
code
that
regulates
nervous
system
patterning
.
Although
the
in
vivo
roles
of
many
of
the
HS
modifications
have
been
investigated
,
very
little
is
known
about
the
function
of
HS
3
-
O-
sulfation
in
vivo
.
By
examining
patterning
of
the
Caenorhabditis
elegans
nervous
system
in
loss
of
function
mutants
of
the
two
3
-
O-
sulfotransferases
,
hst-
3
.
1
and
hst-
3
.
2
,
we
found
HS
3
-
O-
sulfation
to
be
largely
dispensable
for
overall
neural
development
.
However
,
generation
of
stereotypical
neurite
branches
in
hermaphroditic-
specific
neurons
required
hst-
3
.
1
,
hst-
3
.
2
,
as
well
as
an
extracellular
cell
adhesion
molecule
encoded
by
kal-
1
,
the
homolog
of
Kallmann
Syndrome
associated
gene
1
/
anosmin-
1
.
In
contrast
,
kal-
1
-
dependent
neurite
branching
in
AIY
neurons
required
catalytic
activity
of
hst-
3
.
2
but
not
hst-
3
.
1
.
The
context-dependent
requirement
for
hst-
3
.
2
and
hst-
3
.
1
indicates
that
both
enzymes
generate
distinct
types
of
HS
modification
patterns
in
different
cell
types
,
which
regulate
kal-
1
to
promote
neurite
branching
.
We
conclude
that
HS
3
-
O-
sulfation
does
not
play
a
general
role
in
establishing
the
HS
code
in
C
.
elegans
but
rather
plays
a
specialized
role
in
a
context-dependent
manner
to
establish
defined
aspects
of
neuronal
circuits
.
Diseases
Validation
Diseases presenting
"loss of function mutants"
symptom
kallmann syndrome
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