關于商城

商城指南

支付方式

配送方式

售后服務

雅吉生物助力科研文獻參考

發(fā)布時間：2024/9/24 9:44:39 閱讀次數：114

【引用產品】：小鼠心肌細胞HL-1

【產品貨號】：YS341C

【論文標題】：AKT1 ａnd AKT2 Induce Distinct Phosphorylation Patterns in HL-1 Cardiac Myocytes

【論文網址】：https://pubs.acs.org/doi/10.1021/pr500131g

【影響因子】：5.279

【反應物種】：Mouse

【發(fā)表時間】：2014-11-29

【單位】：蘇州大學

【實驗】： 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.