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- W4246004805 startingPage "722" @default.
- W4246004805 abstract "P159 PYK2/CAKβis a Ca 2+ -dependent tyrosine kinase which has been shown to activate Src tyrosine kinase and downstream mitogen-activated protein kinases (MAPKs) such as extracellular signal-regulated kinase (ERK), c-Jun amino-terminal kinase (JNK), and p38 MAPK depending on a cell-type. Although angiotensin II (Ang II)-induced activation of PYK2 has been implicated in vascular remodeling, the precise role of PYK2/CAKβin Ang II-induced MAPK family activation and cell growth in vascular smooth muscle cells (VSMCs) remain largely unclear. To resolve this question, cultured rat aortic VSMCs were transfected with adenoviral vector expressing either wild type rat PYK2/CAKβ(PykWT) or its dominant-negative K457A mutant (PykDN), and MAPK family activation and protein synthesis were compared. The activation of MAPKs was measured by immunoblotting with the phospho-specific antibodies that selectively recognize the activated MAPKs. Protein synthesis was determined by 3 H-leucine incorporation. Both PykWT and PykDN transfection had no effect on Ang II-induced ERK activation. By contrast, PykWT transfection inhibited Ang II-induced JNK and p38 MAPK activation, whereas PykDN transfection markedly enhanced their activation. Interestingly, Ang II-induced 3 H-leucine uptake was totally blocked by PykWT transfection. However, PykDN transfection had no effect on Ang II-induced 3 H-Leucine uptake. From these data, we conclude that PYK2/CAKβnegatively regulates Ang II-induced vascular hypertrophy possibly through its inhibitory effect on JNK and p38 MAPK, providing new insight into the signal transduction mechanism of vascular remodeling." @default.
- W4246004805 created "2022-05-12" @default.
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- W4246004805 date "2000-10-01" @default.
- W4246004805 modified "2023-10-14" @default.
- W4246004805 title "Pyk2/Cakβ Negatively Regulates Angiotensin Ii-Induced Vascular Hypertrophy" @default.
- W4246004805 doi "https://doi.org/10.1161/hyp.36.suppl_1.722-a" @default.
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