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This Article Full Text Full Text (PDF) All Versions of this Article: 294/3/F603    most recent 00234.2007v1 Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in ISI Web of Science Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Articles by Márquez, M. G. Articles by Sterin-Speziale, N. B. Search for Related Content PubMed PubMed Citation Articles by Márquez, M. G. Articles by Sterin-Speziale, N. B.

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

¹Instituto de Investigaciones en Ciencias de la Salud Humana, Universidad Nacional de La Rioja, La Rioja; and ²Cátedra de Biología Celular, Departamento de Ciencias Biológicas, Facultad de Farmacia y Bioquímica, Universidad de Buenos Aires, and ³Instituto de Química y Fisico-Química Biológicas-Consejo Nacional de Investigaciones Cientificas y Tecnicas, Buenos Aires, Argentina

Submitted 18 May 2007 ; accepted in final form 20 December 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 PLCβ in rat renal papillae, we attempted to determine whether BK can modulate FA restructuring by this mechanism, by pretreating cultured cells with the PLCβ inhibitor U73122. [GenBank] 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 PLCβ. 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