Ghrelin suppresses tunicamycin- or thapsigargin-triggered endoplasmic reticulum stress-mediated apoptosis in primary cultured rat cortical neuronal cells

Chung, Hyun Ju; Chung, Habong; Bae, Chong Woo; Kim, Chong‐Jin; Park, Seungjoon

doi:10.1507/endocrj.k10e-396

Cited by 37 publications

(20 citation statements)

References 57 publications

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“…In previous papers, we reported the protective effect of ghrelin on oxygen-glucose deprivation induced apoptosis [5] and tunicamycin-induced endoplasmic reticulum (ER) stress in neuronal cells [20]. In this study we investigated the effect of ghrelin on hypoxia induced autophagic cell death.…”

Section: Ghrelin Protects Adult Rat Hippocampal Nscs Against Ogd Insultmentioning

confidence: 95%

Ghrelin protects adult rat hippocampal neural stem cells from excessive autophagy during oxygen-glucose deprivation

2018

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Abstract. Ghrelin functions as a neuroprotective agent and saves neurons from various insults include ischemic injury. However, it remains to be elucidated whether ghrelin protects neuronal cells against ischemic injury-induced excessive autophagy. Autophagy is required for the maintenance of neural stem cell homeostasis. However, regarding autophagic cell death, it is commonly assumed that excessive autophagy leads to self-elimination of mammalian cells. The purpose of this study was to investigate the potential neuroprotection effects of ghrelin from excessive autophagy in adult rat hippocampal neural stem cells (NSCs). Oxygen-Glucose Deprivation (OGD) strongly induces autophagy in adult rat hippocampal NSCs. Ghrelin treatment inhibited OGD-induced cell death of adult rat hippocampal NSCs assessed by cell-counting-kit-8 assay. Ghrelin also suppressed OGD-induced excessive autophagy activity. The protective effect of ghrelin was accompanied by an increased expression levels of Bcl-2, p-62 and decreased expression level of LC3-II, Beclin-1 by Western blot. Furthermore, ghrelin reduced autophagosome formation and number of GFP-LC3 transfected puncta. In conclusion, our data suggest that ghrelin protects adult rat hippocampal NSCs from excessive autophagy in experimental stroke (oxygen-glucose deprivation) model. Regulating autophagic activity may be a potential optimizing target for promoting adult rat hippocampal NSCs based therapy for stroke.

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Section: Ghrelin Protects Adult Rat Hippocampal Nscs Against Ogd Insultmentioning

confidence: 95%

Ghrelin protects adult rat hippocampal neural stem cells from excessive autophagy during oxygen-glucose deprivation

2018

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“…During ER stress, multiple signaling pathways are activated, including double-stranded RNA-activated protein kinase (PKR), the PKR-like ER kinase (PERK) and eukaryotic translation initiation factor 2 alpha (eIF2α), which suppress protein synthesis (Prostko et al, 1993;Teske et al, 2011). The UPR also activates synthesis of glucose-regulated protein 78 (GRP78), one of the endoplasmic reticulum chaperone molecules that can bind unfolded proteins and degrade misfolded proteins (Laitusis et al, 1999), and activation of transcription factors such as activating transcription factor (ATF6), inositol-requiring enzyme 1α (IRE1α), C/EBP homologous protein (CHOP), and caspase-12 (Urano et al, 2000;Yoshida et al, 2001;Lee et al, 2002;Back et al, 2006;Chung et al, 2011;. Excessive and prolonged stresses ultimately lead to inflammation and apoptosis (Fribley et al, 2009;Jäger et al, 2012;Sovolyova et al, 2014).…”

Section: Introductionmentioning

confidence: 99%

Melatonin suppresses methamphetamine-triggered endoplasmic reticulum stress in C6 cells glioma cell lines

et al. 2017

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-Methamphetamine (METH) is a neurotoxic drug that causes brain damage by inducing neuronal and glial cell death together with glial cell hyperactivity-mediated progressive neurodegeneration. Previous studies have shown that METH induced glial cell hyperactivity and death via oxidative stress, the inflammatory response, and endoplasmic reticulum stress (ER stress) mechanisms, and melatonin could reverse these effects. However, the exact mechanism of the protective role of melatonin in METH-mediated ER stress has not been understood. This study investigated the protective effect of melatonin against METH toxicity-mediated ER stress in glial cells. Our study demonstrated that METH increased glial cell toxicity related to METH-induced ER stress by stimulating the unfolded protein response (UPR) to activate the expression of ER stress transducers, including phosphorylated doublestranded RNA-activated protein kinase (PKR)-like ER kinase (p-PERK), activating transcription factor (ATF6), and phosphorylated inositol-requiring enzyme 1 (p-IRE1). Moreover, the expression of binding immunoglobulin protein (Bip), CCAAT/enhancer-binding protein homologous protein (CHOP), caspase-12, phosphorylated eukaryotic translation initiation factor 2 alpha (p-eIF2α) and spliced X-box-binding protein-1 (XBP-1) mRNA were also increased. Melatonin reduced ER stress induced by METH toxicity by reducing the expression of ER stress response genes and proteins in a concentration-dependent manner. In addition, melatonin promoted the expression of Bip chaperone in a concentration-dependent manner. Taken together, our findings suggest that melatonin can protect against ER stress-induced glial cell death induced by METH.

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“…In this study, ghrelin was not able to protect against 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine insults in ucp2-/-mice, but was effective in their wild-type equivalents [3]. More recently, ghrelin was shown to protect primary neurons from ER stress [49]. Thus, GHS-R1a agonists could potentially be used to prevent aging-related and/or environmental-induced ROS production and accumulation.…”

Section: Ghs-r1a and Neuroprotectionmentioning

confidence: 64%

The Ghrelin Receptors (GHS-R1a and GHS-R1b)

Albarran-Zeckler¹,

Smith²

2013

Endocrine Development

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The growth hormone (GH) secretagogue receptor (GHS-R1a) is a G protein-coupled receptor (GPCR) expressed in the brain as well as other areas of the body. In the early 1990s, this receptor was expression cloned in MERCK laboratories by using a group of synthesized small molecules known to increase GH release in humans and other animals. Since its discovery, hundreds of studies have shown the importance of this receptor and its endogenous ligand, ghrelin, in metabolism, neurotransmission, and behavior. Even more relevant are the prospective benefits that will result from pharmacologic manipulation of GHS-R1a. Multiple GHS-R1a agonists and antagonists are available for experimentation, and some have been used in patients with promising results. Studies in rodents have revealed intriguing potential roles for GHS-R1a modulation. Our goal in this chapter is to connect these studies with the inherent advantages of targeting this receptor pharmacologically.

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Ghrelin suppresses tunicamycin- or thapsigargin-triggered endoplasmic reticulum stress-mediated apoptosis in primary cultured rat cortical neuronal cells

Cited by 37 publications

References 57 publications

Ghrelin protects adult rat hippocampal neural stem cells from excessive autophagy during oxygen-glucose deprivation

Ghrelin protects adult rat hippocampal neural stem cells from excessive autophagy during oxygen-glucose deprivation

Melatonin suppresses methamphetamine-triggered endoplasmic reticulum stress in C6 cells glioma cell lines

The Ghrelin Receptors (GHS-R1a and GHS-R1b)

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