Antioxidants and Redox Signaling,
Journal Year:
2014,
Volume and Issue:
22(5), P. 347 - 349
Published: Sept. 2, 2014
It
has
been
almost
two
decades
since
the
first
demonstration
of
hydrogen
sulfide
(H2S)
as
a
physiological
mediator
cognitive
function
and
vascular
tone.
H2S
is
physiologically
important
because
it
protects
various
organs
from
ischemia–reperfusion
injury
besides
regulating
inflammation,
oxygen
sensing,
cell
growth,
senescence.
The
production,
metabolism,
regulation
have
studied
extensively.
modulates
target
proteins
through
sulfhydration
(or
sulfuration)
or
by
reduction
cysteine
disulfide
bonds.
A
large
number
novel
H2S-donating
compounds
are
being
developed
owing
to
therapeutic
potential
H2S.
Recently,
polysulfides,
rather
than
H2S,
identified
molecules
that
sulfhydrate
sulfurate)
their
proteins.
Antioxid.
Redox
Signal.
22,
347–349.
Molecules,
Journal Year:
2014,
Volume and Issue:
19(12), P. 21183 - 21199
Published: Dec. 16, 2014
In
addition
to
nitric
oxide
and
carbon
monoxide,
hydrogen
sulfide
(H2S),
synthesized
enzymatically
from
l-cysteine
or
l-homocysteine,
is
the
third
gasotransmitter
in
mammals.
Endogenous
H2S
involved
regulation
of
many
physiological
processes,
including
vascular
tone.
Although
initially
it
was
suggested
that
wall
only
by
smooth
muscle
cells
relaxes
them
activating
ATP-sensitive
potassium
channels,
more
recent
studies
indicate
endothelial
as
well.
Endothelial
production
stimulated
factors,
acetylcholine,
shear
stress,
adipose
tissue
hormone
leptin,
estrogens
plant
flavonoids.
some
preparations
plays
a
role
endothelium-derived
hyperpolarizing
factor
small
intermediate-conductance
calcium-activated
channels.
signaling
up-regulated
pathologies,
such
obesity
cerebral
ischemia-reperfusion.
addition,
activates
NO
synthase
inhibits
cGMP
degradation
phosphodiesterase
5
thus
potentiating
effect
NO-cGMP
pathway.
Moreover,
H2S-derived
polysulfides
directly
activate
protein
kinase
G.
Finally,
interacts
with
form
nitroxyl
(HNO)—a
potent
vasorelaxant.
appears
play
an
important
multidimensional
endothelium-dependent
vasorelaxation.
Frontiers in Physiology,
Journal Year:
2016,
Volume and Issue:
7
Published: Aug. 2, 2016
Control
over
the
Na,K-ATPase
function
plays
a
central
role
in
adaptation
of
organisms
to
hypoxic
and
anoxic
conditions.
As
enzyme
itself
does
not
possess
O2
binding
sites
its
"oxygen-sensitivity"
is
mediated
by
variety
redox-sensitive
modifications
including
S-glutathionylation,
S-nitrosylation
phosphorylation.
This
an
overview
current
knowledge
on
plethora
molecular
mechanisms
tuning
activity
ATP-consuming
cellular
metabolic
activity.
Recent
findings
suggest
that
oxygen-derived
free
radicals
H2O2,
NO,
oxidised
glutathione
are
signalling
messengers
make
"oxygen-sensitive".
very
ancient
pathway
targeting
thiols
all
three
subunits
as
well
kinases
sustains
at
"optimal"
level
avoiding
terminal
ATP
depletion
maintaining
transmembrane
ion
gradients
cells
anoxia-tolerant
species.
We
acknowledge
complexity
underlying
processes
we
characterise
sources
reactive
oxygen
nitrogen
species
production
cells,
identify
their
targets,
thiol
groups
which,
upon
modification,
impact
Structured
accordingly,
this
review
presents
summery
(i)
radical
(ii)
localisation
regulatory
within
reversible
play
responses
enzymes
stimuli
(hypoxia,
receptors'
activation)
control
(iii)
phosphorylation,
(iv)
fine
modulation
survival
success
under
The
co-authors
attempted
cover
contradictions
standing
hypotheses
field
propose
possible
future
developments
dynamic
area
research,
importance
which
hard
overestimate.
Better
understanding
successful
strategies
will
it
harness
them
use
for
treatment
patients
with
stroke
myocardial
infarction,
sleep
apnoea
high
altitude
pulmonary
oedema,
those
undergoing
surgical
interventions
associated
interruption
blood
perfusion.
Antioxidants and Redox Signaling,
Journal Year:
2014,
Volume and Issue:
22(5), P. 347 - 349
Published: Sept. 2, 2014
It
has
been
almost
two
decades
since
the
first
demonstration
of
hydrogen
sulfide
(H2S)
as
a
physiological
mediator
cognitive
function
and
vascular
tone.
H2S
is
physiologically
important
because
it
protects
various
organs
from
ischemia–reperfusion
injury
besides
regulating
inflammation,
oxygen
sensing,
cell
growth,
senescence.
The
production,
metabolism,
regulation
have
studied
extensively.
modulates
target
proteins
through
sulfhydration
(or
sulfuration)
or
by
reduction
cysteine
disulfide
bonds.
A
large
number
novel
H2S-donating
compounds
are
being
developed
owing
to
therapeutic
potential
H2S.
Recently,
polysulfides,
rather
than
H2S,
identified
molecules
that
sulfhydrate
sulfurate)
their
proteins.
Antioxid.
Redox
Signal.
22,
347–349.
