Tat-NOL3 protects against hippocampal neuronal cell death induced by oxidative stress through the regulation of apoptotic pathways

Sohn, Eun Jeong; Shin, Min Jea; Eum, Won Sik; Kim, Dae Won; Yong, Ji; Ryu, Eun Ji; Park, Jung Hwan; Cho, Su Bin; Ju, Hyun; Kim, Sang Jin; Yeo, Hyeon Ji; Yeo, Eun Ji; Choi, Yeon Joo; Im, Seung Kwon; Kweon, Hae Young; Kim, Duk‐Soo; Yu, Yeon Hee; Cho, Sung‐Woo; Park, Meeyoung; Park, Jinseu; Cho, Yong‐Jun; Choi, Soo Young

doi:10.3892/ijmm.2016.2596

Cited by 16 publications

(8 citation statements)

References 54 publications

(64 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…These proteins target substrates for proteasome degradation and might contribute to autophagy [34]. Furthermore, the expression of apoptosis repressor nucleolar protein 3 (NOL3) was increased under hypoxia [35]. The hypoxia inducible factor-1 (HIF-1) signalling pathway was also activated, which is considered a protective pathway against apoptosis in mesenchymal stem cells [36, 37].…”

Section: Discussionmentioning

confidence: 99%

Proteomic analysis of human periodontal ligament cells under hypoxia

Luo

et al. 2019

Proteome Sci

View full text Add to dashboard Cite

Background The periodontal ligament is essential for homeostasis of periodontal tissue. A hypoxic milieu of the periodontal tissue is generated under periodontitis or during orthodontic treatment, which affects the periodontal and bone remodelling process. Here, we provide a comprehensive proteomic characterization of periodontal ligament cells under hypoxic conditions, aiming to reveal previously unappreciated biological changes and to help advance hypoxia-based therapeutic strategies for periodontal diseases. Methods Human periodontal ligament cells (hPDLCs) were characterized using immunohistochemistry (IHC) and flow cytometry (FACS). Successful hypoxia treatment of hPDLCs with 1% O 2 was confirmed by qRT-PCR. Proliferation was evaluated using an MTT assay. The proteomic expression profile under hypoxia was studied with the isobaric tags for relative and absolute quantification (iTRAQ) approach followed by protein identification and bioinformatic analysis, and western blot verification was performed. Results The hPDLCs were positive for vimentin, CD73 and CD105 and negative for keratin, CD34 and CD45. After hypoxia treatment, the mRNA expression of hypoxia-inducible factor 1a ( HIF1a) was upregulated. The proliferation rate was elevated during the first 6 h but decreased from 6 h to 72 h. A total of 220 differentially expressed proteins were quantified in hPDLCs under hypoxia (1% O 2 , 24 h), including 153 upregulated and 67 downregulated proteins, five of which were verified by western blot analysis. The Gene Ontology enriched terms included the energy metabolic process, membrane-bound organelle and vesicle, and protein binding terms. Kyoto Encyclopedia of Genes and Genomes (KEGG) analysis indicated several involved pathways, including glycolysis/gluconeogenesis, biosynthesis of amino acids, the HIF-1 signalling pathway, and focal adhesion. A protein–protein interaction (PPI) network demonstrated the dominant role of autophagy over apoptosis under hypoxia. Conclusion The proteomic profile of hPDLCs under hypoxia was mainly related to energy metabolism, autophagy, and responses to stimuli such as adhesion and inflammation. Previously unrecognized proteins including solute carrier family proteins, heat shock proteins, ubiquitination-related enzymes, collagen and S100 family proteins are involved in adaptive response to hypoxia in hPDLCs and are thus of great research interest in future work. Electronic supplementary material The online version of this article (10.1186/s12953-019-0151-2) contains supplementary material, which is available to authorized users.

show abstract

Section: Discussionmentioning

confidence: 99%

Proteomic analysis of human periodontal ligament cells under hypoxia

Luo

et al. 2019

Proteome Sci

View full text Add to dashboard Cite

show abstract

“…It has been reported that H 2 O 2 induces neuronal apoptosis through various signaling pathway, such as nuclear factor-κB, JNK/ERK (Liu et al, 2017), Cdc42/MLK3/MKK7/JNK3 pathway (Wang et al, 2017), P53, mitochondria-related Bax and Bcl-2 (Sohn et al, 2016), Akt/H2A phosphorylation (Park et al, 2016), et al In out research, time-course study revealed that H 2 O 2 activated caspase-3, ROCK1 and MLC in chronological sequence. Thus, H 2 O 2 activated caspase-3 through upstream pathways and then activated caspase-3 mediated ROCK1 and MLC activation.…”

Section: Discussionmentioning

confidence: 99%

Myosin IIA-related Actomyosin Contractility Mediates Oxidative Stress-induced Neuronal Apoptosis

Wang

Liu

et al. 2017

Front. Mol. Neurosci.

View full text Add to dashboard Cite

Oxidative stress-induced neuronal apoptosis plays an important role in the progression of central nervous system (CNS) diseases. In our study, when neuronal cells were exposed to hydrogen peroxide (H2O2), an exogenous oxidant, cell apoptosis was observed with typical morphological changes including membrane blebbing, neurite retraction and cell contraction. The actomyosin system is considered to be responsible for the morphological changes, but how exactly it regulates oxidative stress-induced neuronal apoptosis and the distinctive functions of different myosin II isoforms remain unclear. We demonstrate that myosin IIA was required for neuronal contraction, while myosin IIB was required for neuronal outgrowth in normal conditions. During H2O2-induced neuronal apoptosis, myosin IIA, rather than IIB, interacted with actin filaments to generate contractile forces that lead to morphological changes. Moreover, myosin IIA knockout using clustered regularly interspaced short palindromic repeats/CRISPR-associated protein-9 nuclease (CRISPR/Cas9) reduced H2O2-induced neuronal apoptosis and the associated morphological changes. We further demonstrate that caspase-3/Rho-associated kinase 1 (ROCK1) dependent phosphorylation of myosin light chain (MLC) was required for the formation of the myosin IIA-actin complex. Meanwhile, either inhibition of myosin II ATPase with blebbistatin or knockdown of myosin IIA with siRNA reversely attenuated caspase-3 activation, suggesting a positive feedback loop during oxidative stress-induced apoptosis. Based on our observation, myosin IIA-actin complex contributes to actomyosin contractility and is associated with the positive feedback loop of caspase-3/ROCK1/MLC pathway. This study unravels the biochemical and mechanistic mechanisms during oxidative stress-induced neuronal apoptosis and may be applicable for the development of therapies for CNS diseases.

show abstract

“…Although the pathological cause of AD is still mostly unknown, past findings have proven that patients with AD show an accumulation of abnormally folded beta-amyloid (Aβ) in senile plaques and neuronal apoptosis [ 2 ]. Oxidative stress has been reported as one of the key causes of neuronal apoptosis during the development of AD, which is associated with the remarkable accumulation of reactive oxygen species (ROS), mitochondrial dysfunction, and calcium accumulation [ 3 ]. ROS are catalyzed by a combination of redox active metal ions and Aβ in AD [ 4 ].…”

Section: Introductionmentioning

confidence: 99%

Pharmacological Basis for the Use of Evodiamine in Alzheimer’s Disease: Antioxidation and Antiapoptosis

Zhang

Wang

et al. 2018

IJMS

View full text Add to dashboard Cite

Evodiamine (Evo), a major alkaloid compound isolated from the dry unripened fruit of Evodia fructus, has a wide range of pharmacological activities. The present study sought to explore the neuroprotective effects of Evo in l-glutamate (l-Glu)-induced apoptosis of HT22 cells, and in a d-galactose and aluminum trichloride-developed Alzheimer’s disease (AD) mouse model. Evo significantly enhanced cell viability, inhibited the accumulation of reactive oxygen species, ameliorated mitochondrial function, increased the B-cell lymphoma-2 protein content, and inhibited the high expression levels of Bax, Bad, and cleaved-caspase-3 and -8 in l-Glu-induced HT22 cells. Evo also enhanced the phosphorylation activities of protein kinase B and the mammalian target of rapamycin in the l-Glu-induced HT22 cells. In the AD mouse model, Evo reduced the aimless and chaotic movements, reduced the time spent in the central area in the open field test, and decreased the escape latency time in the Morris water maze test. Evo reduced the deposition of amyloid beta 42 (Aβ42) in the brain, and increased the serum level of Aβ42, but showed no significant effects on Aβ40. In addition, six weeks of Evo administration significantly suppressed oxidative stress by modulating the related enzyme levels. In the central cholinergic system of AD mice, Evo significantly increased the serum levels of acetylcholine and choline acetyltransferase and decreased the level of acetylcholinesterase in the serum, hypothalamus, and brain. Our results provide experimental evidence that Evo can serve as a neuroprotective candidate for the prevention and/or treatment of neurodegenerative diseases.

show abstract

Tat-NOL3 protects against hippocampal neuronal cell death induced by oxidative stress through the regulation of apoptotic pathways

Cited by 16 publications

References 54 publications

Proteomic analysis of human periodontal ligament cells under hypoxia

Proteomic analysis of human periodontal ligament cells under hypoxia

Myosin IIA-related Actomyosin Contractility Mediates Oxidative Stress-induced Neuronal Apoptosis

Pharmacological Basis for the Use of Evodiamine in Alzheimer’s Disease: Antioxidation and Antiapoptosis

Contact Info

Product

Resources

About