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Image Search Results
Journal: American Journal of Physiology - Heart and Circulatory Physiology
Article Title: Human muscle-specific A-kinase anchoring protein polymorphisms modulate the susceptibility to cardiovascular diseases by altering cAMP/PKA signaling
doi: 10.1152/ajpheart.00034.2018
Figure Lengend Snippet: S1653R and E2124G human in muscle-specific A-kinase anchoring protein (mAKAP) single-nucleotide polymorphisms (SNPs) were successfully created by site-directed mutagenesis, and both mutants did not alter mAKAP expression along with β1- and β2-adrenergic receptors (β1- and β2-ARs). A: double digestion of mutated plasmids by the restriction enzymes ApaI and NotI with only two expected bands and no other contaminating bands on 1% Tris-acetate-EDTA gels, as provided by Biomatik. The DNA marker shows the corresponding molecular weight of DNA (in bp). B: representative Western blots showing mAKAP and GAPDH bands and quantification of the same using one-way ANOVA with Tukey’s multiple-comparison test. Three independent experiments (n = 3) of human embryonic kidney (HEK)-293T cell lysates were analyzed, and data are expressed as means ± SE. **P < 0.01 vs. control untransfected cells [control: 0.2409 ± 0.06368; wild type (WT): 1.417 ± 0.1330; S1653R: 1.261 ± 0.2145; E2124G: 1.375 ± 0.1905]. C: representative Western blots for β1- and β2-ARs along with GAPDH and quantification by one-way ANOVA with Tukey’s multiple-comparison test. Four independent experiments (n = 4) were performed, and data are expressed as means ± SE: β1-AR (control: 0.8779 ± 0.1198; WT: 1.005 ± 0.09496; S1653R: 1.015 ± 0.1226; E2124G: 0.9573 ± 0.05715) and β2-AR (control: 2.166 ± 0.08062; WT: 1.903 ± 0.1221; S1653R: 1.927 ± 0.2458; E2124G: 1.894 ± 0.1986).
Article Snippet: A : double digestion of mutated plasmids by the restriction enzymes ApaI and
Techniques: Mutagenesis, Expressing, Marker, Molecular Weight, Western Blot, Comparison, Control