Leonurine Ameliorates Oxidative Stress and Insufficient Angiogenesis by Regulating the PI3K/Akt-eNOS Signaling Pathway in H2O2-Induced HUVECs - PubMed (original) (raw)
Leonurine Ameliorates Oxidative Stress and Insufficient Angiogenesis by Regulating the PI3K/Akt-eNOS Signaling Pathway in H2O2-Induced HUVECs
Li Liao et al. Oxid Med Cell Longev. 2021.
Abstract
Thrombus is considered to be the pathological source of morbidity and mortality of cardiovascular disease and thrombotic complications, while oxidative stress is regarded as an important factor in vascular endothelial injury and thrombus formation. Therefore, antioxidative stress and maintaining the normal function of vascular endothelial cells are greatly significant in regulating vascular tension and maintaining a nonthrombotic environment. Leonurine (LEO) is a unique alkaloid isolated from Leonurus japonicus Houtt (a traditional Chinese medicine (TCM)), which has shown a good effect on promoting blood circulation and removing blood stasis. In this study, we explored the protective effect and action mechanism of LEO on human umbilical vein endothelial cells (HUVECs) after damage by hydrogen peroxide (H2O2). The protective effects of LEO on H2O2-induced HUVECs were determined by measuring the cell viability, cell migration, tube formation, and oxidative biomarkers. The underlying mechanism of antioxidation of LEO was investigated by RT-qPCR and western blotting. Our results showed that LEO treatment promoted cell viability; remarkably downregulated the intracellular generation of reactive oxygen species (ROS), malondialdehyde (MDA) production, and lactate dehydrogenase (LDH); and upregulated the nitric oxide (NO) and superoxide dismutase (SOD) activity in H2O2-induced HUVECs. At the same time, LEO treatment significantly promoted the phosphorylation level of angiogenic protein PI3K, Akt, and eNOS and the expression level of survival factor Bcl2 and decreased the expression level of death factor Bax and caspase3. In conclusion, our findings suggested that LEO can ameliorate the oxidative stress damage and insufficient angiogenesis of HUVECs induced by H2O2 through activating the PI3K/Akt-eNOS signaling pathway.
Copyright © 2021 Li Liao et al.
Conflict of interest statement
The authors have declared no other competing interests.
Figures
Figure 1
Chemical structure of LEO.
Figure 2
Detection of cell survival rate by MTT assay: (a) effect of LEO on the proliferation of HUVEC; (b) effect of H2O2 on the viability of HUVEC; (c) the survival rate of H2O2-induced injury following treatment with LEO at different concentrations; (d) effect of LEO on cell morphology after H2O2-induced injury in HUVECs. Values are presented as means ± S.D. (n = 6). #P < 0.05, ##P < 0.01, and ###P < 0.001 vs. control group; ∗P < 0.05, ∗∗P < 0.01, and ∗∗∗P < 0.001 vs. H2O2 group.
Figure 3
Detection of cell migration rate and wound closure. Values are presented as means ± S.D. (n = 3). #P < 0.05, ##P < 0.01, and ###P < 0.001 vs. control group; ∗P < 0.05, ∗∗P < 0.01, and ∗∗∗P < 0.001 vs. H2O2 group. The bar chart shows quantitative data for HUVEC migration with the treatment of different concentrations of LEO.
Figure 4
Evaluation for the tube formation in HUVECs. Images for the in vitro formed tubes in HUVECs. Values are presented as means ± S.D. (n = 3). #P < 0.05, ##P < 0.01, and ###P < 0.001 vs. control group; ∗P < 0.05, ∗∗P < 0.01, and ∗∗∗P < 0.001 vs. H2O2 group. The bar chart shows quantitative data for HUVEC tube formation with the treatment of different concentrations of LEO.
Figure 5
LEO inhibits oxidative damages in H2O2 stimulated in HUVECs. ROS generation in HUVECs was determined by measuring DCFH fluorescence. The ROS fluorescence intensity index was presented as the percentage of the control group. Data are represented as the mean ± S.D. of three separate experiments (n = 6). #P < 0.05, ##P < 0.01, and ###P < 0.001 vs. control group; ∗P < 0.05, ∗∗P < 0.01, and ∗∗∗P < 0.001 vs. H2O2 group.
Figure 6
Effect of LEO on NO, MDA, LDH, and SOD levels in HUVECs treated with H2O2. Values are presented as means ± S.D. (n = 3). #P < 0.05, ##P < 0.01, and ###P < 0.001 vs. control group; ∗P < 0.05, ∗∗P < 0.01, and ∗∗∗P < 0.001 vs. H2O2 group.
Figure 7
Effect of LEO on the mRNA expression and protein expression of Bax, Bcl2, and caspase3 in HUVECs: (a) effect of LEO on the mRNA expression of Bax, Bcl2, and caspase3 in HUVECs; (b) effect of LEO on the protein expression of Bax, Bcl2, and caspase3 in HUVECs. Values are presented as means ± S.D. (n = 3). #P < 0.05, ##P < 0.01, and ###P < 0.001 vs. control group; ∗P < 0.05, ∗∗P < 0.01, and ∗∗∗P < 0.001 vs. H2O2 group.
Figure 8
Effect of LEO on protein expression of PI3K, p-PI3K, Akt, p-Akt, eNOS, and p-eNOS in HUVEC. Values are presented as means ± S.D. (n = 3). #P < 0.05, ##P < 0.01, and ###P < 0.001 vs. control group; ∗P < 0.05, ∗∗P < 0.01, and ∗∗∗P < 0.001 vs. H2O2 group.
Figure 9
H2O2 can induce the expression of apoptotic protein Bax and inhibit the phosphorylation of PI3K/Akt by increasing the content of ROS, while LEO can promote the phosphorylation of PI3K/Akt and further promote the expression of eNOS, thus promoting the survival, proliferation, migration, and NO release of endothelial cells. At the same time, phosphorylated-Akt can also inhibit the expression of apoptotic proteins such as Bcl2 and Bax, thus inhibiting endothelial cell apoptosis induced by ROS. “←” indicates activation, and “⟝” indicates inhibition.
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