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Reduced glutathione disrupts the intracellular trafficking of tyrosinase and tyrosinase-related protein-1 but not dopachrome tautomerase and Pmel17 to melanosomes, which results in the attenuation of melanization.
[oculocutaneous albinism]
We
previously
reported
that
treatment
of
B
16
melanotic
melanoma
cells
with
reduced
glutathione
(
GSH
)
converts
them
to
amelanotic
cells
without
any
significant
down-regulation
of
tyrosinase
activity
.
To
characterize
the
cellular
mechanism
(
s
)
involved
,
we
determined
the
intracellular
distribution
of
melanocyte-
specific
proteins
,
especially
in
melanin
synthesis-
specific
organelles
,
termed
melanosomes
by
subcellular
fractionation
followed
by
Western
blotting
and
confocal
laser
microscopy
(
CFLM
)
.
In
the
melanosome-rich
large
granule
fraction
and
in
highly
purified
melanosome
fractions
,
while
GSH-induced
amelanotic
B
16
cells
have
significantly
diminished
levels
of
protein
/
activity
of
tyrosinase
and
tyrosinase
-related
protein-
1
compared
with
control
melanized
B
16
cells
,
there
was
substantially
no
difference
in
the
distribution
and
levels
of
dopachrome
tautomerase
and
the
processed
isoform
of
Pmel
17
(
HMB
45
)
between
control
melanized
and
GSH-induced
amelanotic
B
16
cells
.
Analysis
of
merged
images
obtained
by
CFLM
revealed
that
whereas
tyrosinase
,
Pmel
17
and
dopachrome
tautomerase
colocalize
with
each
other
in
the
control
melanized
B
16
cells
,
tyrosinase
does
not
colocalize
with
Pmel
17
or
its
processed
isoform
and
with
dopachrome
tautomerase
in
GSH-induced
amelanotic
B
16
cells
.
The
sum
of
these
findings
suggests
that
reduced
glutathione
selectively
disrupts
the
intracellular
trafficking
of
tyrosinase
and
tyrosinase
-related
protein-
1
but
not
dopachrome
tautomerase
and
Pmel
17
to
melanosomes
,
which
results
in
the
attenuation
of
melanization
,
probably
serving
as
a
putative
model
for
oculocutaneous
albinism
type
4
.
