International Journal of Molecular Sciences,
Год журнала:
2024,
Номер
25(22), С. 11962 - 11962
Опубликована: Ноя. 7, 2024
Glycan
structures
of
glycoproteins
and
glycolipids
on
the
surface
glycocalyx
luminal
sugar
layers
intracellular
membrane
compartments
in
human
cells
constitute
a
key
interface
between
biological
processes
external
environments.
Sialic
acids,
class
alpha-keto
acid
sugars
with
nine-carbon
backbone,
are
frequently
found
as
terminal
residues
these
glycoconjugates,
forming
critical
components
layers.
Changes
status
content
cellular
sialic
acids
closely
linked
to
many
diseases
such
cancer,
cardiovascular,
neurological,
inflammatory,
infectious,
lysosomal
storage
diseases.
The
molecular
machineries
responsible
for
biosynthesis
sialylated
glycans,
along
their
interacting
partners,
important
therapeutic
strategies
targets
drug
development.
purpose
this
article
is
comprehensively
review
recent
literature
provide
new
scientific
insights
into
mechanisms
implications
sialylation
across
various
Recent
advances
clinical
developments
acid-related
therapies
also
summarized
discussed.
Nature Communications,
Год журнала:
2024,
Номер
15(1)
Опубликована: Ноя. 9, 2024
N-glycosylation
is
one
of
the
most
common
protein
modifications
in
eukaryotes,
with
immense
importance
at
molecular,
cellular,
and
organismal
level.
Accurate
reliable
N-glycan
analysis
essential
to
obtain
a
systems-wide
understanding
fundamental
biological
processes.
Due
structural
complexity
glycans,
their
still
highly
challenging.
Here
we
make
publicly
available
consistent
N-glycome
dataset
20
different
mouse
tissues
demonstrate
multimodal
data
workflow
that
allows
for
unprecedented
depth
coverage
features.
This
scalable,
LC-MS/MS
data-driven
method
integrates
automated
identification
spectra,
application
non-targeted
profiling
strategies
isomer-sensitive
glycan
structures.
Our
delineation
critical
sub-structural
determinants
isomers
across
uncovered
tissue-specific
glycosylation
patterns,
expression
non-canonical
structures
highlights
multiple
layers
derive
from
organ-specific
regulations
glycobiological
pathways.
Glycobiology,
Год журнала:
2023,
Номер
33(11), С. 935 - 942
Опубликована: Окт. 4, 2023
Abstract
The
development
and
function
of
the
brain
requires
N-linked
glycosylation
proteins,
which
is
a
ubiquitous
modification
in
secretory
pathway.
N-glycans
have
distinct
composition
undergo
tight
regulation
brain,
but
spatial
distribution
these
structures
remains
relatively
unexplored.
Here,
we
systematically
employed
carbohydrate
binding
lectins
with
differing
specificities
to
various
classes
appropriate
controls
identify
glycan
expression
multiple
regions
mouse
brain.
Lectins
high-mannose-type
N-glycans,
most
abundant
class
showed
diffuse
staining
some
punctate
observed
on
high
magnification.
specific
motifs
complex
including
fucose
bisecting
GlcNAc,
more
partitioned
labeling,
synapse-rich
molecular
layer
cerebellum.
Understanding
across
will
aid
future
studies
critical
protein
modifications
disease
bioRxiv (Cold Spring Harbor Laboratory),
Год журнала:
2023,
Номер
unknown
Опубликована: Сен. 22, 2023
Abstract
In
addition
to
the
backbone
molecules
of
proteins
and
lipids,
RNAs
have
recently
been
found
be
N-glycosylated
as
well
in
cell
models.
Some
overlap
N-glycans
between
RNA
protein
exist
terms
monosaccharide
composition.
Here
we
report
a
draft
human
tissue
glycoRNA
covering
12
typical
organs
characterized
by
mass
spectrometry-based
N-glycomics.
were
first
prepared,
then
enzymatically
released,
hydrophilically
enriched,
permethylated,
analyzed
RPLC-MS/MS,
finally
identified
N-glycan
search
engine
GlySeeker.
A
total
676
putative
sequence
structures
with
236
compositions
across
organs.
Organ-specific
similarity
heterogeneity
N-glycosylation
glycoRNAs
annotated.
This
comprehensive
serves
foundation
for
future
structural
functional
studies.
TOC
Graphic
Neural Regeneration Research,
Год журнала:
2023,
Номер
19(3), С. 489 - 490
Опубликована: Июль 20, 2023
Center
for
Cognition
and
Sociality,
Institute
Basic
Science
(IBS),
Daejeon,
South
Korea
(Lee
B)
Asia-Pacific
Glycomics
Reference
Site,
(An
HJ)
Graduate
School
of
Analytical
&
Technology,
Chungnam
National
University,
Correspondence
to:
Hyun
Joo
An,
PhD,
[email
protected].
Received
April
5,
2023
in
revised
form
28,
Accepted
May
15,
This
is
an
open-access
article
distributed
under
the
terms
Creative
Commons
Attribution-Noncommercial-Share
Alike
4.0
Unported,
which
permits
unrestricted
use,
distribution,
reproduction
any
medium,
provided
original
work
properly
cited.
bioRxiv (Cold Spring Harbor Laboratory),
Год журнала:
2023,
Номер
unknown
Опубликована: Янв. 11, 2023
Comparative
"omics"
studies
have
revealed
unique
aspects
of
human
neurobiology,
yet
an
evolutionary
perspective
the
brain
N-glycome
is
lacking.
Here,
we
performed
multi-regional
characterization
rat,
macaque,
chimpanzee,
and
N-glycomes
using
chromatography
mass
spectrometry,
then
integrated
these
data
with
complementary
glycotranscriptomic
data.
We
found
that
in
primates
has
evolved
more
rapidly
than
underlying
transcriptomic
framework,
providing
a
mechanism
for
generating
additional
diversity.
show
evolution
hominids
been
characterized
by
increase
complexity
α(2-6)-linked
N-acetylneuraminic
acid
along
human-specific
cell-type
expression
key
glycogenes.
Finally,
comparing
prenatal
adult
N-glycome,
identify
region-specific
neurodevelopmental
pathways
lead
to
distinct
spatial
N-glycosylation
profiles
mature
brain.Evolution
marked
shift
sialic
linkage.
bioRxiv (Cold Spring Harbor Laboratory),
Год журнала:
2023,
Номер
unknown
Опубликована: Май 31, 2023
ABSTRACT
Protein
N-linked
glycosylation
is
a
ubiquitous
modification
in
the
secretory
pathway
that
plays
critical
role
development
and
function
of
brain.
N-glycans
have
distinct
composition
undergo
tight
regulation
brain,
but
spatial
distribution
these
structures
remains
relatively
unexplored.
Here,
we
systematically
employed
carbohydrate
binding
lectins
with
differing
specificities
to
various
classes
appropriate
controls
identify
multiple
regions
mouse
Lectins
high-mannose-type
N-glycans,
most
abundant
class
brain
showed
diffuse
staining
some
punctate
observed
on
high
magnification.
specific
motifs
complex
including
fucose
bisecting
GlcNAc,
more
partitioned
labeling,
synapse-rich
molecular
layer
cerebellum.
Understanding
across
will
aid
future
studies
protein
modifications
disease
bioRxiv (Cold Spring Harbor Laboratory),
Год журнала:
2023,
Номер
unknown
Опубликована: Окт. 22, 2023
Abstract
To
understand
implications
of
protein
glycosylation
for
clinical
diagnostic
and
biopharmaceuticals,
innovative
glycoproteomic
technologies
are
required.
Recently,
significant
advances
were
made,
particularly
toward
structure-focused
N-
glyco-proteomic
analyses.
The
mass
spectrometric
analysis
intact
glycopeptides
using
stepped
collision
fragmentation
along
with
glycan
oxonium
ion
profiling
now
enables
to
reliably
discriminate
between
different
structures.
Still,
there
weaknesses
that
current
approaches
must
overcome:
1)
handling
incorrect
identifications,
2)
identification
rare
modified
glycans,
3)
insufficient
coverage,
especially
in
complex
samples.
address
these
shortcomings,
we
have
developed
an
workflow
aims
at
providing
comprehensive
site-specific
structural
data
on
human
blood
plasma
glycoproteins.
features
depletion
plus
various
fractionation
strategies
the
use
high-resolution
spectrometry
fragmentation.
Furthermore,
by
including
a
decision
tree
procedure
established
validation,
could
significantly
improve
description
micro-heterogeneity.
Our
allows
reliable
differentiation
ambiguous
structures
like
antenna-versus
core-fucosylation
glycans
such
as
sulfated
glucuronidated
ones.
With
this
workflow,
able
advance
glycoproteins
concentrations
low
10
pg/mL.
A
total
1,929
942
glycosites
derived
from
805
middle-to
low-abundant
identified.
Overall,
presented
holds
great
potential
our
understanding
foster
discovery
biomarkers.
Figure
