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• W2021821392 abstract "Aim. Aquaporins are channel-forming proteins highly permeable to water and some small molecular solutes. We have previously shown that aquaporin-4 knockout mice have increased tolerance to ischemia. However, the mechanism of cardioprotection was unclear. The aim of the current study was to investigate the effects of aquaporin-4 deletion on baseline expression and phosphorylation of some cardioprotective protein kinases. Methods. Proteins were extracted from hearts of aquaporin-4 knockout mice and littermate wild-type controls and analyzed with Western blot. Samples were taken from young (≤ 6 months of age), and old (≥ 1 year) mice. Results. Western blots showed three different isoforms of aquaporin-4 in wild types, likely representing M1, M23, and Mz. Total AMP-dependent kinase expression was decreased in aquaporin-4 knockout hearts by 18 ± 13% (p = 0.02), while the expression of Akt kinase, extracellular signal regulated kinase 1/2, protein kinase C-epsilon, mitogen-associated kinase P38 and C-Jun N-terminal kinase was unchanged. The phosphorylation of Akt kinase was reduced in hearts from knockout mice by 41 ± 16% (p = 0.01). No other alterations in phosphorylation were found. These effects were only detected in young mice. Conclusion. Deletion of the aquaporin-4 gene decreased AMP-dependent kinase expression and Akt kinase phosphorylation in the heart. These changes may influence energy metabolism and endogenous cardioprotection." @default.
• W2021821392 created "2016-06-24" @default.
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• W2021821392 date "2014-05-05" @default.
• W2021821392 modified "2023-09-24" @default.
• W2021821392 title "Deletion of the aquaporin-4 gene alters expression and phosphorylation of protective kinases in the mouse heart" @default.
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• W2021821392 doi "https://doi.org/10.3109/00365513.2014.905698" @default.
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