Zinc ionophores isolated from Terminalia bellirica fruit rind extract protect against cardiomyocyte hypoxia/reoxygenation injury

2021 ◽  
pp. 116394
Author(s):  
Vijaya Lakshmi Bodiga ◽  
Praveen Kumar Vemuri ◽  
Madhukar Rao Kudle ◽  
Sreedhar Bodiga
Keyword(s):  
Reoxygenation Injury ◽  
Terminalia Bellirica ◽  
Fruit Rind ◽  
Hypoxia Reoxygenation

scholarly journals H2S protects hippocampal neurons against hypoxia-reoxygenation injury by promoting RhoA phosphorylation at Ser188

2021 ◽  
Vol 7 (1) ◽  
Author(s):  
Ye Chen ◽  
Jiyue Wen ◽  
Zhiwu Chen
Keyword(s):  
Endothelial Cells ◽  
Hippocampal Neurons ◽  
Glucose Deprivation ◽  
Rhoa Activity ◽  
Mercaptopyruvate Sulfurtransferase ◽  
Dependent Protein ◽  
Cerebral Vasodilatation ◽  
Reoxygenation Injury ◽  
Hypoxia Reoxygenation

AbstractInhibition of RhoA-ROCK pathway is involved in the H2S-induced cerebral vasodilatation and H2S-mediated protection on endothelial cells against oxygen-glucose deprivation/reoxygenation injury. However, the inhibitory mechanism of H2S on RhoA-ROCK pathway is still unclear. The aim of this study was to investigate the target and mechanism of H2S in inhibition of RhoA/ROCK. GST-RhoAwild and GST-RhoAS188A proteins were constructed and expressed, and were used for phosphorylation assay in vitro. Recombinant RhoAwild-pEGFP-N1 and RhoAS188A-pEGFP-N1 plasmids were constructed and transfected into primary hippocampal nerve cells (HNCs) to evaluate the neuroprotective mechanism of endothelial H2S by using transwell co-culture system with endothelial cells from cystathionine-γ-lyase knockout (CSE−/−) mice and 3-mercaptopyruvate sulfurtransferase knockout (3-MST−/−) rats, respectively. We found that NaHS, exogenous H2S donor, promoted RhoA phosphorylation at Ser188 in the presence of cGMP-dependent protein kinase 1 (PKG1) in vitro. Besides, both exogenous and endothelial H2S facilitated the RhoA phosphorylation at Ser188 in HNCs, which induced the reduction of RhoA activity and membrane transposition, as well as ROCK2 activity and expression. To further investigate the role of endothelial H2S on RhoA phosphorylation, we detected H2S release from ECs of CSE+/+ and CSE−/− mice, and 3-MST+/+ and 3-MST−/− rats, respectively, and found that H2S produced by ECs in the culture medium is mainly catalyzed by CSE synthase. Moreover, we revealed that both endothelial H2S, mainly catalyzed by CSE, and exogenous H2S protected the HNCs against hypoxia-reoxygenation injury via phosphorylating RhoA at Ser188.

ELABELA alleviates syncytiotrophoblast hypoxia/reoxygenation injury and preeclampsia-like symptoms in mice by reducing apoptosis

Placenta ◽  
2021 ◽  
Vol 106 ◽  
pp. 30-39
Author(s):  
Jing Ma ◽  
Haoyue Hu ◽  
Miaoling Lin ◽  
Lu Chen ◽  
Mian Liu ◽  
...  
Keyword(s):  
Reoxygenation Injury ◽  
Hypoxia Reoxygenation

scholarly journals Two New Compounds From the Heartwood of Dalbergia melanoxylon and Their Protective Effect on Hypoxia/Reoxygenation Injury in H9c2

2021 ◽  
Vol 16 (1) ◽  
pp. 1934578X2098777
Author(s):  
Yang Liu ◽  
Ni Zhang ◽  
Jun-wei He ◽  
Lan-ying Chen ◽  
Li Yang ◽  
...  
Keyword(s):  
Superoxide Dismutase ◽  
Lactate Dehydrogenase ◽  
Protective Effect ◽  
Superoxide Dismutase Activity ◽  
Spectral Evidence ◽  
Reoxygenation Injury ◽  
Dalbergia Melanoxylon ◽  
New Compounds ◽  
Hypoxia Reoxygenation

A new neoflavonoid, named as (7 R)-(-)-3′,5-dihydroxy-4′,2,4-trimethoxy-dalbergiquinol (1) and a new phenanthrenedione, named as 3′,7-dihydroxy-3,6- dimethoxy-9-phenyl-1,4-phenanthrenedione (2), together with 4 known compounds, 5- O-methyldalbergiphenol (3), 3′,7-dihydroxy-4′,3,6-trimethoxy-9-phenyl-1,4-phenanthrenedione (4), (+)-obtusafuran (5), and melanoxin (6) were isolated from the heartwood of Dalbergia melanoxylon. Their structures were elucidated on the basis of chemical and spectral evidence, as well as by comparison with literature data. Moreover, compound 1 showed a protective effect on hypoxia/reoxygenation injury in H9c2 at 10.0 μM by decreasing lactate dehydrogenase and malondialdehyde activity and enhancing superoxide dismutase activity.

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