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      Extracellular Signal-Regulated Kinase and the Small GTP-Binding Protein p21Rac1 Are Involved in the Regulation of Gene Transcription by Angiotensin II

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          To study the role of extracellular-signal-regulated kinase (ERK) cascade and the small GTP-ase proteins in the activation of the c-fos promoter by angiotensin II (AII), transient transfection experiments were performed in CHO cells stably expressing the rat AT<sub>1A</sub> receptor. In this system AII activated ERK in 1 min and also increased the transcriptional activity of the c-fos promoter-luciferase reporter gene construct. The activation of the promoter proved to be dependent on the Ras-Raf-ERK cascade as cotransfection of expression vectors known to specifically inhibit this cascade blocked the effect of AII. Dominant-negative p21Rac1 mutant partially blocked the activation of the c-fos promoter by AII. However, activation of the c-fos promoter was independent of protein kinase C (PKC) as bisindolylmaleimide I, a specific PKC inhibitor did not block the effect of AII. These results suggest that AII activates the transcription of the c-fos through the Ras-Raf-ERK cascade. Furthermore, p21Rac1 is involved in the modulation of the c-fos promoter by AII.

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          Most cited references 21

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          Protein kinases and phosphatases: the yin and yang of protein phosphorylation and signaling.

           Tony Hunter (1995)
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            A role for Pyk2 and Src in linking G-protein-coupled receptors with MAP kinase activation.

            The mechanisms by which mitogenic G-protein-coupled receptors activate the MAP kinase signalling pathway are poorly understood. Candidate protein tyrosine kinases that link G-protein-coupled receptors with MAP kinase include Src family kinases, the epidermal growth factor receptor, Lyn and Syk. Here we show that lysophosphatidic acid (LPA) and bradykinin induce tyrosine phosphorylation of Pyk2 and complex formation between Pyk2 and activated Src. Moreover, tyrosine phosphorylation of Pyk2 leads to binding of the SH2 domain of Src to tyrosine 402 of Pyk2 and activation of Src. Transient overexpression of a dominant interfering mutant of Pyk2 or the protein tyrosine kinase Csk reduces LPA- or bradykinin-induced activation of MAP kinase. LPA- or bradykinin-induced MAP kinase activation was also inhibited by overexpression of dominant interfering mutants of Grb2 and Sos. We propose that Pyk2 acts with Src to link Gi- and Gq-coupled receptors with Grb2 and Sos to activate the MAP kinase signalling pathway in PC12 cells.
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              PD 098059 Is a Specific Inhibitor of the Activation of Mitogen-activated Protein Kinase Kinasein Vitroandin Vivo


                Author and article information

                Nephron Exp Nephrol
                Cardiorenal Medicine
                S. Karger AG
                April 2001
                11 January 2001
                : 9
                : 2
                : 142-149
                aDepartment of Pathophysiology, Faculty of Medicine, International Nephrology Training and Research Center, Semmelweis University; Departments of bMicrobiology, and cPhysiology, and d1st Department of Medicine, Faculty of Medicine, Semmelweis University, Budapest, Hungary; eHospital for Sick Children, University of Toronto, Toronto, Canada, and fDepartment of Medicine, University of Colorado Health Sciences Center, Denver, Colo., USA
                52605 Exp Nephrol 2001;9:142–149
                © 2001 S. Karger AG, Basel

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                Page count
                Figures: 4, References: 53, Pages: 8
                Self URI (application/pdf): https://www.karger.com/Article/Pdf/52605
                Original Paper


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