IQUIFIB   02644
INSTITUTO DE QUIMICA Y FISICOQUIMICA BIOLOGICAS "PROF. ALEJANDRO C. PALADINI"
Unidad Ejecutora - UE
artículos
Título:
Bradykinin modulates focal nadhesion and inuces stress fiber remodeling in renal papillary collecting duct cells
Autor/es:
MARÍA GABRIELA MARQUEZ; MARÍA DEL C FERNANDEZ-TOME; NICOLÁS O FAVALE; LUCILA GISELE PESCIO; NORMA BEATRIZ STERIN-SPEZIALE
Revista:
America Journal Physiology Renal Physiology
Editorial:
American Physiological Society
Referencias:
Año: 2007 vol. 294 p. 603 - 613
Resumen:
Bradykinin modulates focal adhesions
and induces stress fiber remodeling in renal papillary collecting
duct cells. Am J Physiol Renal Physiol 294: F000F000, 2008. First
published December 26, 2007; doi:10.1152/ajprenal.00234.2007.
Focal adhesions (FAs) are specialized regions of cell attachment to the
extracellular matrix. Previous works have suggested that bradykinin
(BK) can modulate cell-matrix interaction. In the present study, we
used a physiological cellular model to evaluate the potential role of
BK in modulating FAs and stress fibers. We performed a quantitative
morphometric analysis of FAs in primary cultured rat renal papillary
collecting duct cells, which included size, axial ratio (shape), and
average length. After 1, 5, or 10 min of incubation with BK, cultured
cells were immunostained and analyzed by confocal microscopy.
Although the shape of FAs was not altered, BK induced a decrease in
the number of vinculin-stained FAs per cell, and a decrease in both
their size and their average length, but not in talin-containing FAs,
thus suggesting that BK could be inducing a restructuring of FAs. BK
also induced a remodeling of the actin filament assemblies rather than
their dissipation. Since we have previously demonstrated that BK
stimulates activation of PLC in rat renal papillae, we attempted to
determine whether BK can modulate FA restructuring by this mechanism,
by pretreating cultured cells with the PLC inhibitor U73122.
The present study, performed under physiological conditions with
cells that were not genetically manipulated, provides new experimental
evidence supporting the notion that the intrarenal hormone BK
modulates FAs and actin cytoskeleton organization through a mechanism
that involves the activation of PLC. We propose this finding
as a novel mechanism for BK modulation of tubular collecting duct
functiAm J Physiol Renal Physiol 294: F000F000, 2008. First
published December 26, 2007; doi:10.1152/ajprenal.00234.2007.
Focal adhesions (FAs) are specialized regions of cell attachment to the
extracellular matrix. Previous works have suggested that bradykinin
(BK) can modulate cell-matrix interaction. In the present study, we
used a physiological cellular model to evaluate the potential role of
BK in modulating FAs and stress fibers. We performed a quantitative
morphometric analysis of FAs in primary cultured rat renal papillary
collecting duct cells, which included size, axial ratio (shape), and
average length. After 1, 5, or 10 min of incubation with BK, cultured
cells were immunostained and analyzed by confocal microscopy.
Although the shape of FAs was not altered, BK induced a decrease in
the number of vinculin-stained FAs per cell, and a decrease in both
their size and their average length, but not in talin-containing FAs,
thus suggesting that BK could be inducing a restructuring of FAs. BK
also induced a remodeling of the actin filament assemblies rather than
their dissipation. Since we have previously demonstrated that BK
stimulates activation of PLC in rat renal papillae, we attempted to
determine whether BK can modulate FA restructuring by this mechanism,
by pretreating cultured cells with the PLC inhibitor U73122.
The present study, performed under physiological conditions with
cells that were not genetically manipulated, provides new experimental
evidence supporting the notion that the intrarenal hormone BK
modulates FAs and actin cytoskeleton organization through a mechanism
that involves the activation of PLC. We propose this finding
as a novel mechanism for BK modulation of tubular collecting duct
functi in rat renal papillae, we attempted to
determine whether BK can modulate FA restructuring by this mechanism,
by pretreating cultured cells with the PLC inhibitor U73122.
The present study, performed under physiological conditions with
cells that were not genetically manipulated, provides new experimental
evidence supporting the notion that the intrarenal hormone BK
modulates FAs and actin cytoskeleton organization through a mechanism
that involves the activation of PLC. We propose this finding
as a novel mechanism for BK modulation of tubular collecting duct
functi inhibitor U73122.
The present study, performed under physiological conditions with
cells that were not genetically manipulated, provides new experimental
evidence supporting the notion that the intrarenal hormone BK
modulates FAs and actin cytoskeleton organization through a mechanism
that involves the activation of PLC. We propose this finding
as a novel mechanism for BK modulation of tubular collecting duct
functi. We propose this finding
as a novel mechanism for BK modulation of tubular collecting duct
functi