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|
Identifier |
000372850 |
Title |
Θετική και αρνητική ρύθμιση των μικρών GTRασων RHO και του κυτταροσκελετού ακτίνης από BMP και TGF-B |
Alternative Title |
Positive and negative regulation of small Gtpases Rho and actin cytoskeleton by BMP and TGF-B |
Author
|
Κωνσταντινίδης, Γεώργιος
|
Thesis advisor
|
Στουρνάρας, Χρήστος
|
Reviewer
|
Καρδάσης, Δημήτρης
Τσατσάνης, Χρήστος
Μουστάκας, Αριστείδης
Γραβάνης, Αχιλλέας
Σουρβίνος, Γιώργος
Παπακωνσταντή, Ευαγγελία
|
Abstract |
Actin
cytoskeleton
dynamics
support
and
coordinate
a
large
number
of
signaling
events
that
control
cell
proliferation,
differentiation
and
migration.
Cytoskeletal
plasticity
is
based
on
multi-‐protein
complexes
that
regulate
actin
polymerization,
stability
and
assembly
with
myosin.
Growth
factors
provide
essential
signals
that
govern
cytoskeletal
dynamics.
One
such
growth
factor
network
is
the
transforming
growth
factor
β
(TGF-‐β)
that
includes
secreted
polypeptides
such
as
bone
morphogenetic
proteins
(BMP)
and
activins.
Here,
it
is
demonstrated
that
BMP-‐7
signals
through
Smad1,
p38
and
p44/42
(Erk1/2)
MAPKs
and
induces
actin
polymerization
and
focal
adhesion
remodeling
in
starved
fibroblasts
and
various
other
cell
lines
as
potently
as
TGF-‐β.
Moreover,
BMP-‐7
induces
migration
of
Swiss3T3
fibroblasts
letting
at
the
same
time
proliferation
and
apoptosis
unaffected.
An
important
regulator
of
actin
remodeling,
the
kinase
ROCK1
mediates
changes
of
actin
dynamics
by
BMP-‐7,
while
this
growth
factor
induces
rapid
activation
of
RhoA
and
RhoB
GTPases
with
concomitant
inactivation
of
Cdc42.
In
parallel,
BMP-‐7
induces
RhoB
and
Smad6
expression
providing
with
a
positive
and
a
negative
signalling
feedback
simultaneously.
Activation
of
Rho
GTPases
and
the
downstream
ROCK1
kinase
by
BMP-‐7
correlate
well
with
induction
of
phosphorylation
on
Ser19
of
the
myosin
light
chain,
but
not
with
LIMK1
kinase
activation.
ROCK
inhibitor
Y-‐27632
blocks
actin
polymerization
and
reduces
migration
capacity
induced
by
BMP-‐7.
Furthermore,
the
same
ROCK
inhibitor
blocks
the
myosin
light
chain
phosphorylation
of
Ser19
during
BMP-‐7
signalling.
Depletion
of
endogenous
myosin
light
chain
also
inhibits
the
actin
remodeling
induced
by
BMP-‐7.
Thus,
in
a
next
step,
this
novel
pathway
regulates
fibroblast
migration
without
affecting
cell
proliferation.
Taking
everything
into
consideration,
here
it
is
established
not
only
that
BMP
signals
through
Smad
and,
the
so-‐called,
non-‐Smad
pathway
of
MAPKs,
but
also
through
Rho/ROCK
pathway
which
targets
myosin
light
chain
during
actin
remodeling
and
migration
of
Swiss3T3
fibroblasts.
|
Language |
Greek |
Subject |
Actin |
|
Biochemistry |
|
Bone morphogenetic protein |
|
Cytoskeleton |
|
Myosin light chain |
|
Myosin light chain kinase |
|
Rho coiled- coiledkinase 1 |
|
Transforming growth factor β |
|
Ακτίνη |
|
Ελαφριά αλυσίδα μυοσίνης |
|
Κινάση της ελαφριάς αλυσίδας μυοσίνης |
|
Κυτταροσκελετός |
|
Μετασχηματίζων αυξητικός παράγοντας β |
|
Πρωτεϊνη μορφογένεσης οστών |
Issue date |
2011-12-14 |
Collection
|
School/Department--School of Medicine--Department of Medicine--Doctoral theses
|
|
Type of Work--Doctoral theses
|
Permanent Link |
https://elocus.lib.uoc.gr//dlib/9/2/a/metadata-dlib-1331719544-168672-23176.tkl
|
Views |
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