GAPDH-silence preserves H9C2 cells from acute hypoxia and reoxygenation injury

Shao, Liang; Ma, Aiqun; Figtree, Gemma A.; Zhang, Ping

doi:10.1016/j.ijbiomac.2015.08.028

Cited by 11 publications

(4 citation statements)

References 31 publications

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“…Cardiomyocyte apoptosis in vitro was estimated by flow cytometry after staining with Annexin V and propidium iodide (PI) (21). Briefly, cells were harvested and stained with an Annexin V-FITC/PI Kit (cat.…”

Section: Methodsmentioning

confidence: 99%

Proteinase‑activated receptor�2 deficiency is a protective factor against cardiomyocyte apoptosis during myocardial ischemia/reperfusion injury

Wang

Zhang

et al. 2019

Mol Med Report

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Previous studies have established that proteinase- activated receptor 2 (PAR2) activation protects against myocardial ischemia/reperfusion injury (MI/RI). However, the role of PAR2 deficiency in MI/RI remains unclear. The aim of the present study was to examine the effect of PAR2 deficiency on cardiomyocyte apoptosis and to clarify the potential molecular mechanisms for its protective effect against MI/RI. Using a mouse model of MI/RI, cardiac function was evaluated by echocardiography, infarct size was assessed by triphenyltetrazolium chloride staining, and myocardial cell apoptosis was measured by terminal deoxynucleotide transferase-mediated dUTP nick end-labeling staining. Annexin V/propidium iodide staining, and expression of Bcl-2 and cleaved PARP were determined to assess apoptosis in myocardial H9c2 cells exposed to hypoxia/reoxygenation (H/R) injury-simulating MI/RI. Phosphorylated ERK1/2, JNK, and p38 MAPK protein expression levels were analyzed by western blotting. The findings indicated that PAR2 deficiency markedly reduced cardiomyocyte apoptosis in the MI/RI mouse model, as well as in myocardial H9c2 cells exposed to H/R. Furthermore, PAR2 knockdown clearly prevented phosphorylation of ERK1/2 and JNK in myocardial H9c2 cells. The results revealed that PAR2 deficiency alleviated MI/RI-associated apoptosis by inhibiting phosphorylation of ERK1/2 and JNK. Therefore, targeted PAR2 silencing may be a potential therapeutic approach for alleviation of MI/RI.

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Section: Methodsmentioning

confidence: 99%

Proteinase‑activated receptor�2 deficiency is a protective factor against cardiomyocyte apoptosis during myocardial ischemia/reperfusion injury

Wang

Zhang

et al. 2019

Mol Med Report

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“…For osteosarcoma, research has contrastingly both observed that autophagy may either promote or inhibit proliferation under the context of different gene regulation (Kenific et al, 2010;Bao et al, 2018;Zhao et al, 2018). Literature has also indicated that autophagy could enhance cellular activity through anti-oxidative stress (Zhang et al, 2018) and that cells tend to increase oxidative stress under hypoxic conditions (Liang et al, 2015). Herein, we found that autophagy related proteins were overexpressed when 143b and U2OS cells were cultured in hypoxic environments.…”

Section: Discussionmentioning

confidence: 74%

NDUFA4L2 Regulated by HIF-1α Promotes Metastasis and Epithelial–Mesenchymal Transition of Osteosarcoma Cells Through Inhibiting ROS Production

Yang

Zheng

et al. 2020

Front. Cell Dev. Biol.

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Osteosarcoma (OS) accounts for a large proportion of the types of bone tumors that are newly diagnosed, and is a relatively common bone tumor. However, there are still no effective treatments for this affliction. One interesting avenue is related to the mitochondrial NDUFA4L2 protein, which is encoded by the nuclear gene and is known to be a critical mediator in the regulation of cell survival. Thus, in this study, we aimed to investigate the effect of NDUFA4L2 upon the metastasis and epithelial–mesenchymal transition of OS. We found that NDUFA4L2 protein expression was upregulated in hypoxic conditions. We also used 2-ME and DMOG, which are HIF-1α inhibitors and agonists, respectively, to assess the effects related to decreasing or increasing HIF-1α expression. 2-ME caused a significant decrease of NDUFA4L2 expression and DMOG had the opposite effect. It was obvious that down-regulation of NDUFA4L2 had a direct interaction with the apoptosis of OS cells. Western blotting, wound healing analyses, Transwell invasion assays, and colony formation assays all indicated and supported the conclusion that NDUFA4L2 promoted OS cell migration, invasion, proliferation, and the epithelial–mesenchymal transition. During experiments, we incidentally discovered that autophagy and the ROS inhibitor could be used to facilitate the rescuing of tumor cells whose NDUFA4L2 was knocked down. Our findings will help to further elucidate the dynamics underlying the mechanism of OS cells and have provided a novel therapeutic target for the treatment of OS.

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“…Nonetheless, up-regulation of GAPDH mRNA may reflect a higher protein need for other cellular functions. For example, in mammalian cells during ischemia-reperfusion (which causes cell damage by hypoxia-reoxygenation) GAPDH participates in apoptosis (Li et al, 2012), autophagy and antioxidant response (Liang et al, 2015). Potential roles of GAPDH outside energy metabolism will be examined in future studies in shrimp.…”

Section: Discussionmentioning

confidence: 99%

Regulation of glyceraldehyde-3-phosphate dehydrogenase by hypoxia inducible factor 1 in the white shrimp Litopenaeus vannamei during hypoxia and reoxygenation

Camacho‐Jiménez

Leyva‐Carrillo

Peregrino‐Uriarte

et al. 2019

Comparative Biochemistry and Physiology Part A: Molecular &

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Hypoxia is a frequent source of stress in the estuarine habitat of the white shrimp Litopenaeus vannamei. During hypoxia, L. vannamei gill cells rely more heavily on anaerobic glycolysis to obtain ATP. This is mediated by transcriptional up-regulation of glycolytic enzymes including glyceraldehyde-3-phosphate dehydrogenase (GAPDH). The hypoxia inducible factor 1 (HIF-1) is an important transcriptional activator of several glycolytic enzymes during hypoxia in diverse animals, including crustaceans. In this work, we cloned and sequenced a fragment corresponding to the 5′ flank of the GAPDH gene and identified a putative HIF-1 binding site, as well as sites for other transcription factors involved in the hypoxia signaling pathway. To investigate the role of HIF-1 in GAPDH regulation, we simultaneously injected double-stranded RNA (dsRNA) into shrimp to silence HIF-1α and HIF-1β under normoxia, hypoxia, and hypoxia followed by reoxygenation, and then measured gill HIF-1α, HIF-1β expression, GAPDH expression and activity, and glucose and lactate concentrations at 0, 3, 24 and 48 h. During normoxia, HIF-1 silencing induced up-regulation of GAPDH transcripts and activity, suggesting that expression is down-regulated via HIF-1 under these conditions. In contrast, HIF-1 silencing during hypoxia abolished the increases in GAPDH expression and activity, glucose and lactate concentrations. Finally, HIF-1 silencing during hypoxia-reoxygenation prevented the increase in GAPDH expression, however, those changes were not reflected in GAPDH activity and lactate accumulation. Altogether, these results indicate that GAPDH and glycolysis are transcriptionally regulated by HIF-1 in gills of white shrimp.

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GAPDH-silence preserves H9C2 cells from acute hypoxia and reoxygenation injury

Cited by 11 publications

References 31 publications

Proteinase‑activated receptor�2 deficiency is a protective factor against cardiomyocyte apoptosis during myocardial ischemia/reperfusion injury

Proteinase‑activated receptor�2 deficiency is a protective factor against cardiomyocyte apoptosis during myocardial ischemia/reperfusion injury

NDUFA4L2 Regulated by HIF-1α Promotes Metastasis and Epithelial–Mesenchymal Transition of Osteosarcoma Cells Through Inhibiting ROS Production

Regulation of glyceraldehyde-3-phosphate dehydrogenase by hypoxia inducible factor 1 in the white shrimp Litopenaeus vannamei during hypoxia and reoxygenation

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