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雅吉生物助力科研文獻(xiàn)參考

發(fā)布時(shí)間：2024/9/24 9:44:39      閱讀次數(shù)：231

【引用產(chǎn)品】：小鼠心肌細(xì)胞HL-1
 
【產(chǎn)品貨號(hào)】：YS341C
 
【論文標(biāo)題】：AKT1 ａnd AKT2 Induce Distinct Phosphorylation Patterns in HL-1 Cardiac Myocytes
 
【論文網(wǎng)址】：https://pubs.acs.org/doi/10.1021/pr500131g
 
【影響因子】：5.279
 
【反應(yīng)物種】：Mouse
 
【發(fā)表時(shí)間】：2014-11-29
 
【單 位】：蘇州大學(xué)
 
【實(shí) 驗(yàn)】： HL-1 Cardiac Myocytes
The protein kinase AKT is a central kinase in the heart ａnd has a major impactongrowth/hypertrophy, survival/apoptosis, ａnd metabolism. To gain more insight into AKT isoform-specific signaling at the molecular level, we investigated the phosphoproteome of HL-1 cardiomyocytes carrying AKT1 or AKT2 isoform-specific knock down, respectively. We combined stable isotope labeling with high resolution mass spectrometry ａnd identified 377 regulated phosphopeptides. Although AKT1 is expressed at 4-fold higher levels, insulin stimulation mainly activated AKT2, which might in part rely on a preferred interaction of AKT2 with the mammalian target of rapamycin complex 2. In line with this result, the highest number of regulated phosphopeptides was identified in the AKT2 knock down cells. Isoform-specific regulation of AKT targets not previously described could be observed, ａnd specific regulation of indirect target sites allows a deeper insight into affected biological processes. In the myocardial context, we identified many phosphosites supporting a connection of AKT to excitation–contraction coupling. Phosphoproteins identified included L-type calcium channel, ryanodine receptor, junctophilin, histidine-rich calcium binding protein, phospholamban, heat shock protein beta-6, ａnd Ca2+/calmodulin-dependent kinase II. In conclusion, AKT isoform-specific knock down combined with quantitative phosphoproteomics provided a powerful strategy to unravel AKT isoform-specific signaling.


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