Mass Spectrometry Reviews,
Journal Year:
2021,
Volume and Issue:
42(2), P. 577 - 616
Published: June 22, 2021
Abstract
Glycosylation
is
one
of
the
most
significant
and
abundant
posttranslational
modifications
in
mammalian
cells.
It
mediates
a
wide
range
biofunctions,
including
cell
adhesion,
communication,
immune
trafficking,
protein
stability.
Also,
aberrant
glycosylation
has
been
associated
with
various
diseases
such
as
diabetes,
Alzheimer's
disease,
inflammation,
deficiencies,
congenital
disorders,
cancers.
The
alterations
distributions
glycan
glycopeptide
isomers
are
involved
development
progression
several
human
diseases.
However,
microheterogeneity
brings
great
challenge
to
glycomic
glycoproteomic
analysis,
characterization
isomers.
Over
decades,
different
methods
approaches
have
developed
facilitate
Mass
spectrometry
(MS)
powerful
tool
utilized
for
isomeric
analysis
due
its
high
sensitivity
rich
structural
information
using
fragmentation
techniques.
comprehensive
remains
when
utilizing
MS
alone.
Therefore,
separation
methods,
liquid
chromatography,
capillary
electrophoresis,
ion
mobility,
were
resolve
before
MS.
These
techniques
coupled
better
identification
quantitation
Additionally,
bioinformatic
tools
essential
automated
processing
data
studies
biological
cohorts.
Here
this
review,
we
discuss
commonly
employed
MS‐based
techniques,
hyphenated
software,
facilitating
separation,
identification,
Glycobiology,
Journal Year:
2016,
Volume and Issue:
27(1), P. 3 - 49
Published: Aug. 24, 2016
Simple
and
complex
carbohydrates
(glycans)
have
long
been
known
to
play
major
metabolic,
structural
physical
roles
in
biological
systems.
Targeted
microbial
binding
host
glycans
has
also
studied
for
decades.
But
such
can
only
explain
some
of
the
remarkable
complexity
organismal
diversity
nature.
Reviewing
subject
about
two
decades
ago,
one
could
find
very
few
clear-cut
instances
glycan-recognition-specific
that
were
intrinsic
value
organism
expressing
them.
In
striking
contrast
there
is
now
a
profusion
examples,
this
updated
review
cannot
be
comprehensive.
Instead,
historical
overview
presented,
broad
principles
outlined
examples
cited,
representing
diverse
types
roles,
mediated
by
various
glycan
classes,
different
evolutionary
lineages.
What
remains
unchanged
fact
while
all
theories
regarding
are
supported
compelling
evidence,
exceptions
each
found.
retrospect,
not
surprising.
Complex
appear
ubiquitous
cells
nature,
essential
life
forms.
Thus,
>3
billion
years
evolution
consistently
generated
organisms
use
these
molecules
many
key
even
sometimes
coopting
them
minor
functions.
respect,
no
from
other
macromolecular
building
blocks
(nucleic
acids,
proteins
lipids),
simply
more
rapidly
evolving
complex.
It
time
functional
fully
incorporated
into
mainstream
sciences.
Physiological Reviews,
Journal Year:
2020,
Volume and Issue:
101(2), P. 427 - 493
Published: July 30, 2020
In
the
mid-1980s,
identification
of
serine
and
threonine
residues
on
nuclear
cytoplasmic
proteins
modified
by
a
N-acetylglucosamine
moiety
(O-GlcNAc)
via
an
O-linkage
overturned
widely
held
assumption
that
glycosylation
only
occurred
in
endoplasmic
reticulum,
Golgi
apparatus,
secretory
pathways.
contrast
to
traditional
glycosylation,
O-GlcNAc
modification
does
not
lead
complex,
branched
glycan
structures
is
rapidly
cycled
off
transferase
(OGT)
O-GlcNAcase
(OGA),
respectively.
Since
its
discovery,
O-GlcNAcylation
has
been
shown
contribute
numerous
cellular
functions,
including
signaling,
protein
localization
stability,
transcription,
chromatin
remodeling,
mitochondrial
function,
cell
survival.
Dysregulation
cycling
implicated
progression
wide
range
diseases,
such
as
diabetes,
diabetic
complications,
cancer,
cardiovascular,
neurodegenerative
diseases.
This
review
will
outline
our
current
understanding
processes
involved
regulating
turnover,
role
physiology,
how
dysregulation
contributes
pathophysiological
processes.
Annual Review of Neuroscience,
Journal Year:
2015,
Volume and Issue:
38(1), P. 105 - 125
Published: April 4, 2015
This
review
presents
principles
of
glycosylation,
describes
the
relevant
glycosylation
pathways
and
their
related
disorders,
highlights
some
neurological
aspects
issues
that
continue
to
challenge
researchers.
More
than
100
rare
human
genetic
disorders
result
from
deficiencies
in
different
are
known
today.
Most
these
impact
central
and/or
peripheral
nervous
systems.
Patients
typically
have
developmental
delays/intellectual
disabilities,
hypotonia,
seizures,
neuropathy,
metabolic
abnormalities
multiple
organ
Among
there
is
great
clinical
diversity
because
all
cell
types
differentially
glycosylate
proteins
lipids.
The
patients
hundreds
misglycosylated
products,
which
afflict
a
myriad
processes,
including
signaling,
cell-cell
interaction,
migration.
vast
complexity
glycan
composition
function,
along
with
limited
availability
analytic
tools,
has
impeded
identification
key
glycosylated
molecules
cause
pathologies.
To
date,
few
critical
target
been
pinpointed.
Annals of Translational Medicine,
Journal Year:
2018,
Volume and Issue:
6(24), P. 477 - 477
Published: Dec. 1, 2018
Abstract:
Congenital
disorders
of
glycosylation
are
a
genetically
and
clinically
heterogeneous
group
>130
diseases
caused
by
defects
in
various
steps
along
glycan
modification
pathways.
The
vast
majority
these
monogenic
autosomal
recessive
have
multi-systemic
manifestations,
mainly
growth
failure,
developmental
delay,
facial
dysmorphisms,
variable
coagulation
endocrine
abnormalities.
Carbohydrate
deficient
transferrin
(CDT)
protein-linked
analysis
with
mass
spectrometry
can
diagnose
some
subtypes
congenital
(CDG),
while
many
currently
rely
on
massively
parallel
genomic
sequencing
for
diagnosis.
Early
detection
is
important,
as
few
treatable.
Molecular
biochemical
techniques
continue
to
further
our
understanding
this
rapidly
expanding
diverse
disorders.
