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Am J Physiol Renal Physiol 284: F282-F292, 2003. First published October 1, 2002; doi:10.1152/ajprenal.00115.2002
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Vol. 284, Issue 2, F282-F292, February 2003

Bradykinin reduces growth factor-induced glomerular ERK1/2 phosphorylation

Eric Cellier1, Marilyne Mage1, Johan Duchêne1, Christiane Pécher1, Réjean Couture2, Jean-Loup Bascands1, and Jean-Pierre Girolami1

1 Institut National de la Santé et de la Recherche Médicale U388, IFR 31, Institut Louis Bugnard, 31403 Toulouse Cedex 4, France; and 2 Department of Physiology, Faculté de Médecine, Université de Montréal, Montreal, Quebec, Canada H3C 3J7

Several experimental data report both mitogenic and antimitogenic effects of bradykinin (BK). To conciliate these apparent opposite effects, we hypothesized that, depending on cell context activation, BK could reduce the mitogenic effect of growth factors. Therefore, in the present study we assessed the existence of possible negative cross talk between BK and potential pathogenic growth factors in freshly isolated rat glomeruli (IG). Next, we determined whether this cross talk could be pharmacologically recruited during angiotensin-converting enzyme (ACE) inhibition in the diabetic rat. In IG from normal rats, BK, via activation of the B2 kinin receptor (B2R), causes a transient stimulation of ERK1/2 phosphorylation, whereas it inhibits ERK1/2 phosphorylation induced by IGF-1, PDGF-BB, VEGF, or basic FGF. The reduction of growth factor-induced ERK1/2 phosphorylation is abolished by an inhibitor of tyrosine phosphatase. In glomeruli from diabetic rats, hyperglycemia increased the phosphorylation level of ERK-1/2 as well as oxidative stress. The reversal of these events by ACE inhibition is mediated via B2R activation. These observations are consistent with a potential therapeutic role of BK and B2R during glomerulosclerosis.

kinin B2 receptor; growth factors; mitogen-activated protein kinases; angiotensin-converting enzyme inhibition


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