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Original Research

Differential expression of Gs in a murine model of homocysteinemic heart failure

, , , , , , & show all
Pages 79-84 | Published online: 28 Dec 2022

Figures & data

Figure 1 In vivo G protein content of Gs and Gi in wild type and CBS KO mice. β-actin was used as a standard for both protein samples. Gs content in CBS KO mice was reduced to 46% (P < 0.01, n = 4) that of control values based on 3 different tissue homogenates. Pixel intensity was digitized using UnScanIt Software.

Figure 1 In vivo G protein content of Gs and Gi in wild type and CBS KO mice. β-actin was used as a standard for both protein samples. Gs content in CBS KO mice was reduced to 46% (P < 0.01, n = 4) that of control values based on 3 different tissue homogenates. Pixel intensity was digitized using UnScanIt Software.

Figure 2 In vitro G protein content of Gs and Gi in serum-starved HL-1 cells using the following concentrations for 24 hours: 0 μM, 25 μM, 50 μM, 100 μM, 500 μM. No differential expression was detected (P < 0.05, n = 3). Pixel intensity was digitized using UnScanIt Software.

Figure 2 In vitro G protein content of Gs and Gi in serum-starved HL-1 cells using the following concentrations for 24 hours: 0 μM, 25 μM, 50 μM, 100 μM, 500 μM. No differential expression was detected (P < 0.05, n = 3). Pixel intensity was digitized using UnScanIt Software.

Figure 3 Proposed in vivo model G protein content based on decrease in Gs content. High homocysteine levels created by CBS KO model decreased Gs content available for calcium signaling. A decrease in Gs content decreased chronotropic and ionotropic response to circulating GPCR agonists that utilize this G protein.

Figure 3 Proposed in vivo model G protein content based on decrease in Gs content. High homocysteine levels created by CBS KO model decreased Gs content available for calcium signaling. A decrease in Gs content decreased chronotropic and ionotropic response to circulating GPCR agonists that utilize this G protein.