Bradykinin in the Newborn Kidney

Tóth-Heyn, Péter; Guignard, Jean‐Pierre

doi:10.1159/000065014

Cited by 10 publications

(2 citation statements)

References 28 publications

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“…focal adhesions; renal papillae; recycling compartment BRADYKININ (BK) is an endogenous intrarenal hormone that plays an important role as a vasoactive modulator of renal function (43). In addition to its vasoactive actions, BK exerts significant effects on cellular growth and proliferation of cultured rat mesangial cells (2,10).…”

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confidence: 99%

Bradykinin induces formation of vesicle-like structures containing vinculin and PtdIns(4,5)P₂in renal papillary collecting duct cells

Márquez

Fernández-Tomé

Favale

et al. 2009

American Journal of Physiology-Renal Physiology

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Focal adhesions (FAs) are structures of cell attachment to the extracellular matrix. We previously demonstrated that the intrarenal hormone bradykinin (BK) induces the restructuring of FAs in papillary collecting duct cells by dissipation of vinculin, but not talin, from FAs through a mechanism that involves PLCbeta activation, and that it also induces actin cytoskeleton reorganization. In the present study we investigated the mechanism by which BK induces the dissipation of vinculin-stained FAs in collecting duct cells. We found that BK induces the internalization of vinculin by a noncaveolar and independent pinocytic pathway and that at least a fraction of this protein is delivered to the recycling endosomal compartment, where it colocalizes with the transferrin receptor. Regarding the reassembly of vinculin-stained FAs, we found that BK induces the formation of phosphatidylinositol 4,5-bisphosphate [PtdIns(4,5)P2]-enriched vinculin-containing vesicles, which, by following a polarized exocytic route, transport vinculin to the site of FA assembly, an action that depends on actin filaments. The present study, which was carried out with cells that were not genetically manipulated, shows for the first time that BK induces the formation of vesicle-like structures containing vinculin and PtdIns(4,5)P2, which transport vinculin to the site of FA assembly. Therefore, the modulation of the formation of these vesicle-like structures could be a physiological mechanism through which the cell can reuse the BK-induced internalized vinculin to be delivered for newly forming FAs in renal papillary collecting duct cells.

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confidence: 99%

Bradykinin induces formation of vesicle-like structures containing vinculin and PtdIns(4,5)P₂in renal papillary collecting duct cells

Márquez

Fernández-Tomé

Favale

et al. 2009

American Journal of Physiology-Renal Physiology

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“…Bradykinin (BK) is an endogenous intrarenal hormone that plays an important role as a modulator of the renal function, acting as a vasodilator and diuretic agent (29). In addition to its vasoactive actions, BK exerts significant effects on cellular growth and proliferation of cultured rat mesangial cells (1,7).…”

mentioning

confidence: 99%

Bradykinin modulates focal adhesions and induces stress fiber remodeling in renal papillary collecting duct cells

Márquez

Fernández-Tomé²,

Favale³

et al. 2008

American Journal of Physiology-Renal Physiology

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Márquez MG, del Carmen Fernández-Tome M, Favale NO, Pescio LG, Sterin-Speziale NB. Bradykinin modulates focal adhesions and induces stress fiber remodeling in renal papillary collecting duct cells. Am J Physiol Renal Physiol 294: F603-F613, 2008. First published December 26, 2007 doi:10.1152/ajprenal.00234.2007 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 function. stress fibers; cell-matrix adhesion; vinculin; talin; actin filaments FOCAL ADHESIONS (FAs) are specialized regions of the cell involved in the attachment to the extracellular matrix, where actin stress fibers and the extracellular matrix are connected (4, 35). FA assembly occurs through the binding of the integrinextracellular domain to extracellular matrix proteins, followed by the interaction of the ␤-integrin cytoplasmic domain with talin. Talin can then recruit vinculin, which, in turn, binds other FA proteins (15,21,33). In typical adherent cultured cells, a large number of distinct FAs, ranging in size from less than a square micrometer to several square micrometers, can be detected. The number of FAs, their size, and distribution can vary from one cell to another or even within a single cell, and their morphological diversity may be affected by multiple factors (36). In migrating cells, integrin-mediated adhesions are molecularly heterogeneous and appear in different forms such as "classic" FAs, fibrillar adhesions, and focal complexes. Each of these has a typical morphology and molecular composition (34). Besides h...

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Postnatal Renal Maturation

Baum

Anslow

2022

Pediatric Nephrology

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Bradykinin in the Newborn Kidney

Cited by 10 publications

References 28 publications

Bradykinin induces formation of vesicle-like structures containing vinculin and PtdIns(4,5)P₂in renal papillary collecting duct cells

Bradykinin induces formation of vesicle-like structures containing vinculin and PtdIns(4,5)P₂in renal papillary collecting duct cells

Bradykinin modulates focal adhesions and induces stress fiber remodeling in renal papillary collecting duct cells

Postnatal Renal Maturation

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Bradykinin in the Newborn Kidney

Cited by 10 publications

References 28 publications

Bradykinin induces formation of vesicle-like structures containing vinculin and PtdIns(4,5)P2in renal papillary collecting duct cells

Bradykinin induces formation of vesicle-like structures containing vinculin and PtdIns(4,5)P2in renal papillary collecting duct cells

Bradykinin modulates focal adhesions and induces stress fiber remodeling in renal papillary collecting duct cells

Postnatal Renal Maturation

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Bradykinin induces formation of vesicle-like structures containing vinculin and PtdIns(4,5)P₂in renal papillary collecting duct cells

Bradykinin induces formation of vesicle-like structures containing vinculin and PtdIns(4,5)P₂in renal papillary collecting duct cells