Imipramine administration induces changes in the phosphorylation of FAK and PYK2 and modulates signaling pathways related to their activity
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- 作者：Teresa Zalewskaa ; Adam Bielawskib ; Luiza Stanaszeka ; Krzysztof Wieczerzakb ; Małgorzata Ziemka-Nałęcza ; Irena Nalepab ; nfnalepa@cyf-kr.edu.pl" class="auth_mail" title="E-mail the corresponding author
- 关键词：α1-AR ; α1-adrenergic receptor ; CaMKII ; Ca2 ; +/calmodulin-dependent protein kinase II ; DAG ; diacylglycerol ; ECM ; extracellular matrix ; ERK1/2 ; extracellular signal-regulated kinases 1 and 2 ; FAK ; focal adhesion kinase ; GPCR ; G-protein coupled receptor ; LTP ; long-term potentiation ; MAPK ; mitogen-activated protein kinase ; pCREB ; phosphorylated cyclic-AMP response element-binding protein ; PKC ; protein kinase C ; PSA-NCAM ; polysialylated form of nerve cell adhesion molecule ; PYK2 ; proline-rich tyr
- 刊名：Biochimica et Biophysica Acta (BBA) - General Subjects
- 出版年：2016
- 出版时间：February 2016
- 年：2016
- 卷：1860
- 期：2
- 页码：424-433
- 全文大小：1252 K
文摘
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Different responses of FAK and PYK2 to imipramine confer their distinct functions.
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Imipramine-modulated FAK and PYK2 affect differently connected signaling pathways.
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The changes of FAK and PYK2 go with the Gq protein reduction and increased pERK.
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Imipramine-induced activation of PYK2 may compensate a simultaneous FAK inhibition.