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. 2015 Aug 25;290(40):24237–24254. doi: 10.1074/jbc.M115.666883

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© 2015 by The American Society for Biochemistry and Molecular Biology, Inc.

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FIGURE 6. — TUDC triggers integrin- and PKA-dependent inhibition of hyperosmolarity-induced Fyn and Yes activation. A, rat livers were perfused as mentioned in the perfusion plans. B, liver samples were analyzed for activating phosphorylation of Src kinase family members Fyn, Yes, and c-Src. C, blots were analyzed densitometrically. t = 60 min was compared with the respective control (t = 0 min, set as 1), i.e. sample without institution of either hyperosmolarity (385 mosmol/liter) or TUDC (20 μmol/liter), or with the respective inhibitor (i.e. H89 (2 μmol/liter), GRADSP and GRGDSP (each 10 μmol/liter). Densitometric analysis (means ± S.E.) of at least three independent perfusion experiments is shown. In line with a previous study (1), hyperosmolarity induced within 30 min a significant phosphorylation of Fyn and Yes (*, p < 0.05), however no c-Src activation was observed. Phosphorylation of Fyn and Yes was inhibited by TUDC (#, p < 0.05). Inhibition of Fyn and Yes phosphorylation by TUDC was sensitive to H89 and GRGDSP ($, p < 0.05), however GRADSP had no effect.