7 results on '"Guangdong Yang"'
Search Results
2. Hydrogen sulfide and metal interaction: the pathophysiological implications
- Author
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Devin Mantle and Guangdong Yang
- Subjects
Mammals ,Carbon Monoxide ,Gasotransmitters ,Clinical Biochemistry ,Animals ,Cell Biology ,General Medicine ,Hydrogen Sulfide ,Nitric Oxide ,Molecular Biology ,Signal Transduction - Abstract
Hydrogen sulfide (H
- Published
- 2022
3. H
- Author
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Kalem, Barrow, Yuehong, Wang, Ruihuan, Yu, Jiechun, Zhu, and Guangdong, Yang
- Subjects
Aging ,Mice ,Oxidative Stress ,Heart Diseases ,Cystathionine gamma-Lyase ,Animals ,Angiotensin-Converting Enzyme 2 ,Hydrogen Peroxide ,Hydrogen Sulfide ,Rats - Abstract
Cystathionine gamma-lyase (CSE)-derived hydrogen sulfide (H
- Published
- 2021
4. Involvement of calcium-sensing receptors in hypoxia-induced vascular remodeling and pulmonary hypertension by promoting phenotypic modulation of small pulmonary arteries
- Author
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Guangdong Yang, Hong-Xia Li, Li Zhang, Rui Wang, Hongjiang Shao, Shuzhi Bai, Weihua Zhang, Jian Sun, Xue Peng, Xin-Yan Wang, Lina Wang, Lingyun Wu, Guang-Wei Li, Hongzhu Li, Yu-Hui Xi, and Changqing Xu
- Subjects
Male ,medicine.medical_specialty ,Pathology ,Hypertension, Pulmonary ,Clinical Biochemistry ,Calponin ,Pulmonary Artery ,Vascular Remodeling ,Muscle hypertrophy ,Right ventricular hypertrophy ,Reference Values ,Internal medicine ,medicine.artery ,Proliferating Cell Nuclear Antigen ,medicine ,Animals ,Humans ,Osteopontin ,Rats, Wistar ,Hypoxia ,Molecular Biology ,Heart Failure ,Tissue Inhibitor of Metalloproteinase-3 ,Lung ,biology ,Hypertrophy, Right Ventricular ,Cell Biology ,General Medicine ,Hypoxia (medical) ,medicine.disease ,Pulmonary hypertension ,Disease Models, Animal ,Endocrinology ,medicine.anatomical_structure ,Matrix Metalloproteinase 9 ,Pulmonary artery ,biology.protein ,Matrix Metalloproteinase 2 ,medicine.symptom ,Receptors, Calcium-Sensing - Abstract
Phenotype modulation of pulmonary artery smooth muscle cells (PASMCs) plays an important role during hypoxia-induced vascular remodeling and pulmonary hypertension (PAH). We had previously shown that calcium-sensing receptor (CaSR) is expressed in rat PASMCs. However, little is known about the role of CaSR in phenotypic modulation of PASMCs in hypoxia-induced PAH as well as the underlying mechanisms. In this study, we investigated whether CaSR induces the proliferation of PASMCs in small pulmonary arteries from both rats and human with PAH. PAH was induced by exposing rats to hypoxia for 7–21 days. The mean pulmonary arterial pressure (mPAP), right ventricular hypertrophy index (RVI), the percentage of medial wall thickness to the external diameter (WT %), and cross-sectional total vessel wall area to the total area (WA %) of small pulmonary arteries were determined by hematoxylin and eosin (HE), masson trichrome and Weigert’s staining. The protein expressions of matrix metalloproteinase (MMP)-2 and MMP-9, the tissue inhibitors of metalloproteinase (TIMP)-3, CaSR, proliferating cell nuclear antigen (PCNA), phosphorylated extracellular signal-regulated kinase (p-ERK), and smooth muscle cell (SMC) phenotype marker proteins in rat small pulmonary arteries, including calponin, SMα-actin (SMAα), and osteopontin (OPN), were analyzed by immunohistochemistry and Western blotting, respectively. In addition, immunohistochemistry was applied to paraffin-embedded human tissues from lungs of normal human and PAH patients with chronic heart failure (PAH/CHF). Compared with the control group, mPAP, RVI, WT % and WA % in PAH rats were gradually increased with the prolonged hypoxia. At the same time, the expressions of CaSR, MMP-2, MMP-9, TIMP-3, PCNA, OPN, and p-ERK were markedly increased, while the expressions of SMAα and calponin were significantly reduced in lung tissues or small pulmonary arteries of PAH rats. Neomycin (an agonist of CaSR) enhanced but NPS2390 (an antagonist of CaSR) weakened these hypoxic effects. We further found that the expression change of CaSR, PCNA, and SMC phenotypic marker proteins in PAH/CHF lungs was similar to those in PAH rats. Our data suggest that CaSR is involved in the pulmonary vascular remodeling and PAH by promoting phenotypic modulation of small pulmonary arteries.
- Published
- 2014
5. Involvement of dopamine D2 receptors activation in ischemic post-conditioning-induced cardioprotection through promoting PKC-ε particulate translocation in isolated rat hearts
- Author
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Bo Wu, Jun Gao, Hong-Xia Li, Guangdong Yang, Lingyun Wu, Ye Tian, Changqing Xu, Hongzhu Li, Rui Wang, Shuzhi Bai, Lina Wang, Jin Guo, Yu-Hui Xi, and Hong Li
- Subjects
Agonist ,Male ,medicine.medical_specialty ,medicine.drug_class ,Clinical Biochemistry ,Gene Expression ,chemical and pharmacologic phenomena ,Chromosomal translocation ,Apoptosis ,Myocardial Reperfusion Injury ,Protein Kinase C-epsilon ,In Vitro Techniques ,Ventricular Function, Left ,Dopamine receptor D2 ,Internal medicine ,Malondialdehyde ,medicine ,Haloperidol ,Ventricular Pressure ,Animals ,Myocytes, Cardiac ,Rats, Wistar ,Receptor ,Ischemic Postconditioning ,Molecular Biology ,Creatine Kinase ,Protein kinase C ,Cardioprotection ,business.industry ,Receptors, Dopamine D2 ,Superoxide Dismutase ,Myocardium ,Cell Biology ,General Medicine ,Catalase ,Coronary Vessels ,Bromocriptine ,Rats ,Protein Transport ,Endocrinology ,business ,medicine.drug - Abstract
Dopamine D2 receptors (DR2) are important regulators in many organs, including cardiac system. Protein kinase C (PKC) activation and translocation is associated with cardioprotection against ischemic post-conditioning (PC); however, the regulatory role of DR2 during this process has been unknown. This study hypothesized that the prevention of cardiomyocyte damage by DR2 activation is associated with PKC translocation to the cell membrane. In the present study, we found that the ischemia/reperfusion (I/R) increased the expressions of DR2 mRNA and protein, which were further enhanced by PC. Bromocriptine (DR2 agonist) up-regulated the PC-induced DR2 expressions, and Haloperidol (DR2 antagonist) reversed the increase of DR2 expressions by Bromocriptine. PC reduced I/R-induced cardiomyocytes damage, apoptosis and myocardial infarct size, and improved cardiac function. Compared with PC, Bromocriptine further enhanced the cardioprotective roles of PC, but Haloperidol canceled the protection effect of Bromocriptine. PC up-regulated PKC-e translocation in the particulate fraction, which was further strengthened by Bromocriptine but canceled by Haloperidol. In the cytosolic fraction, the changes of the PKC-e translocation were opposite to the particulate fraction. These findings suggest that DR2 activation provides cardioprotection via promoting PC-induced translocation of PKC-e.
- Published
- 2013
6. Exogenous hydrogen sulfide attenuates diabetic myocardial injury through cardiac mitochondrial protection
- Author
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Shiyun Dong, Xiaoning Leng, Yajun Zhao, Hulun Li, Rui Wang, Weihua Zhang, Changqing Xu, Yuwen Wang, Xin Zhong, Leihong Wang, Lingyun Wu, Xinying Zhang, Fanghao Lu, Guangdong Yang, and Jing Jia
- Subjects
Male ,medicine.medical_specialty ,Clinical Biochemistry ,Sodium hydrosulfide ,Mitochondrion ,Nitric oxide ,Diabetes Mellitus, Experimental ,chemistry.chemical_compound ,Internal medicine ,medicine ,Myocyte ,Animals ,Myocytes, Cardiac ,Hydrogen Sulfide ,Rats, Wistar ,Molecular Biology ,chemistry.chemical_classification ,Reactive oxygen species ,biology ,business.industry ,Caspase 3 ,Cytochrome c ,Myocardium ,Cystathionine gamma-Lyase ,Cytochromes c ,NADPH Oxidases ,Cell Biology ,General Medicine ,Streptozotocin ,Mitochondria ,Rats ,Endocrinology ,chemistry ,Biochemistry ,Apoptosis ,NADPH Oxidase 4 ,biology.protein ,business ,Reactive Oxygen Species ,medicine.drug - Abstract
In the study, we investigated how exogenous H(2)S (hydrogen sulfide) influenced streptozotocin (STZ)-induced diabetic myocardial injury through cardiac mitochondrial protection and nitric oxide (NO) synthesis in intact rat hearts and primary neonatal rat cardiomyocytes. Diabetes was induced by STZ (50 mg/kg) and the daily administration of 100 μM NaHS (sodium hydrosulfide, an H(2)S donor) in the diabetes + NaHS treatment group. At the end of 4, 8, and 12 weeks, the morphological alterations and functions of the hearts were observed using transmission electron microscopy and echocardiography system. The percentage of apoptotic cardiomyocytes, the mitochondrial membrane potential, the production of reactive oxygen species (ROS) and the level of NO were measured. The expressions of cystathionine-γ-lyase (CSE), caspase-3 and -9, the mitochondrial NOX4 and cytochrome c were analyzed by western blotting. The results showed the cardiac function injured, morphological changes and the apoptotic rate increased in the diabetic rat hearts. In the primary neonatal rat cardiomyocytes of high glucose group, ROS production was increased markedly, whereas the expression of CSE and the level of NO was decreased. However, treatment with NaHS significantly reversed the diabetic rat hearts function, the morphological changes and decreased the levels of ROS and NO in the primary neonatal rat cardiomyocytes administrated with high glucose group. Furthermore, NaHS down-regulated the expression of mitochondrial NOX4 and caspase-3 and -9 and inhibited the release of cytochrome c from mitochondria in the primary neonatal rat cardiomyocytes. In conclusion, H(2)S is involved in the attenuation of diabetic myocardial injury through the protection of cardiac mitochondria.
- Published
- 2012
7. Involvement of calcium-sensing receptor in oxLDL-induced MMP-2 production in vascular smooth muscle cells via PI3K/Akt pathway
- Author
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Jin Guo, Changqing Xu, Lingyun Wu, Guangdong Yang, Rui Wang, Shuzhi Bai, Wen He, Hong-Xia Li, Hongzhu Li, Wenjing Xing, Ye Tian, Guang-Wei Li, Yu-Hui Xi, and Fan-Juan Kong
- Subjects
Male ,medicine.medical_specialty ,Vascular smooth muscle ,MAP Kinase Signaling System ,Morpholines ,Clinical Biochemistry ,Adamantane ,Gadolinium ,Muscle, Smooth, Vascular ,Rats, Sprague-Dawley ,chemistry.chemical_compound ,Phosphatidylinositol 3-Kinases ,Western blot ,Internal medicine ,Quinoxalines ,medicine ,Animals ,LY294002 ,Receptor ,Molecular Biology ,Protein kinase B ,PI3K/AKT/mTOR pathway ,Aorta ,Cells, Cultured ,Phosphoinositide-3 Kinase Inhibitors ,Anthracenes ,medicine.diagnostic_test ,Chemistry ,JNK Mitogen-Activated Protein Kinases ,Cell Biology ,General Medicine ,Atherosclerosis ,Cell biology ,Rats ,Lipoproteins, LDL ,Endocrinology ,Chromones ,Phosphorylation ,Matrix Metalloproteinase 2 ,lipids (amino acids, peptides, and proteins) ,Calcium-sensing receptor ,Proto-Oncogene Proteins c-akt ,Receptors, Calcium-Sensing - Abstract
Matrix metalloproteinase-2 (MMP-2) is constitutively expressed in vascular smooth muscle cells (VSMCs) and up-regulated in atherosclerotic lesion by various stimuli, such as oxidized low-density lipoprotein (oxLDL). Calcium-sensing receptor (CaSR) is also expressed in VSMCs, but it remains unclear whether CaSR is associated with overproduction of MMP-2 in VSMCs. In this study, the expression of MMP-2 was detected by real-time PCR and Western blot analysis, and the gelatinolytic activity of MMP-2 was measured using gelatin zymography. Our results showed that oxLDL enhanced MMP-2 expression and activity in rat aortic VSMCs in a time- and dose-dependent manner. In addition, CaSR expression was up-regulated by oxLDL. Manipulating CaSR function in these cells by NPS2390 (an antagonist of CaSR) or GdCl(3) (an agonist of CaSR) affected the oxLDL-induced MMP-2 production. In VSMCs, oxLDL stimulated the rapid activation of phosphatidylinositol 3-kinase (PI3K)/Akt signal pathway, as determined by Western blot analysis. Phosphorylation of Akt and MMP-2 production stimulated by oxLDL were attenuated by LY294002 (a specific inhibitor of PI3K). Activation of Akt was suppressed by NPS2390 but enhanced by GdCl(3). In contrast, oxLDL had no stimulatory effect on the phosphorylation of JNK, and pretreatment with SP600125 (an inhibitor of JNK) produced no significant effect on oxLDL-induced MMP-2 production. These results suggest that CaSR mediates oxLDL-induced MMP-2 production in VSMCs via PI3K/Akt signal pathway.
- Published
- 2011
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