Silibinin activates AMP-activated protein kinase to protect neuronal cells from oxygen and glucose deprivation-re-oxygenation

2014 ◽  
Vol 454 (2) ◽  
pp. 313-319 ◽  
Author(s):  
Zhi Xie ◽  
Sheng-quan Ding ◽  
Ya-fang Shen
Keyword(s):  
Protein Kinase ◽  
Neuronal Cells ◽  
Glucose Deprivation ◽  
Oxygen And Glucose Deprivation ◽  
Amp Activated Protein Kinase

Protective effect of nicotinamide on neuronal cells under oxygen and glucose deprivation and hypoxia/reoxygenation

2004 ◽  
Vol 11 (4) ◽  
pp. 472-481 ◽  
Author(s):  
Chiung-Chyi Shen ◽  
Hsueh-Meei Huang ◽  
Hsiu-Chung Ou ◽  
Huan-Lian Chen ◽  
Wen-Chi Chen ◽  
...  
Keyword(s):  
Protective Effect ◽  
Neuronal Cells ◽  
Glucose Deprivation ◽  
Oxygen And Glucose Deprivation ◽  
Hypoxia Reoxygenation

Identification and characterization of a novel sucrose-non-fermenting protein kinase/AMP-activated protein kinase-related protein kinase, SNARK

2001 ◽  
Vol 355 (2) ◽  
pp. 297-305 ◽  
Author(s):  
Diana L. LEFEBVRE ◽  
Yahong BAI ◽  
Nazanin SHAHMOLKY ◽  
Monika SHARMA ◽  
Raymond POON ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Cellular Response ◽  
Catalytic Domain ◽  
Metabolic Stress ◽  
Glucose Deprivation ◽  
Protein Band ◽  
Northern Blotting ◽  
Significant Similarity ◽  
Amp Activated Protein Kinase

Subtraction hybridization after the exposure of keratinocytes to ultraviolet radiation identified a differentially expressed cDNA that encodes a protein of 630 amino acid residues possessing significant similarity to the catalytic domain of the sucrose-non-fermenting protein kinase (SNF1)/AMP-activated protein kinase (AMPK) family of serine/threonine protein kinases. Northern blotting and reverse-transcriptase-mediated PCR demonstrated that mRNA transcripts for the SNF1/AMPK-related kinase (SNARK) were widely expressed in rodent tissues. The SNARK gene was localized to human chromosome 1q32 by fluorescent in situ hybridization. SNARK was translated in vitro to yield a single protein band of approx. 76kDa; Western analysis of transfected baby hamster kidney (BHK) cells detected two SNARK-immunoreactive bands of approx. 76-80kDa. SNARK was capable of autophosphorylation in vitro; immunoprecipitated SNARK exhibited phosphotransferase activity with the synthetic peptide substrate HMRSAMSGLHLVKRR (SAMS) as a kinase substrate. SNARK activity was significantly increased by AMP and 5-amino-4-imidazolecarboxamide riboside (AICAriboside) in rat keratinocyte cells, implying that SNARK might be activated by an AMPK kinase-dependent pathway. Furthermore, glucose deprivation increased SNARK activity 3-fold in BHK fibroblasts. These findings identify SNARK as a glucose- and AICAriboside-regulated member of the AMPK-related gene family that represents a new candidate mediator of the cellular response to metabolic stress.

scholarly journals A role of DNA-dependent protein kinase for the activation of AMP-activated protein kinase in response to glucose deprivation

2012 ◽  
Vol 1823 (12) ◽  
pp. 2099-2108 ◽  
Author(s):  
Parmeshwar Narayan Amatya ◽  
Hong-Beum Kim ◽  
Seon-Joo Park ◽  
Cha-Kyung Youn ◽  
Jin-Won Hyun ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Glucose Deprivation ◽  
Dependent Protein Kinase ◽  
Dependent Protein ◽  
Amp Activated Protein Kinase

scholarly journals Ghrelin Inhibits Apoptosis in Hypothalamic Neuronal Cells during Oxygen-Glucose Deprivation

Endocrinology ◽  
2007 ◽  
Vol 148 (1) ◽  
pp. 148-159 ◽  
Author(s):  
Hyunju Chung ◽  
Eunhee Kim ◽  
Dae Hee Lee ◽  
Sanghee Seo ◽  
Sunghee Ju ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Infarct Volume ◽  
Neuronal Cells ◽  
Reactive Oxygen Species Generation ◽  
Glucose Deprivation ◽  
Positive Energy ◽  
Oxygen Glucose Deprivation ◽  
Cytochrome C Release ◽  
Hypothalamic Neurons ◽  
Antiapoptotic Effect

Ghrelin is an endogenous ligand for the GH secretagogue receptor, produced and secreted mainly from the stomach. Ghrelin stimulates GH release and induces positive energy balances. Previous studies have reported that ghrelin inhibits apoptosis in several cell types, but its antiapoptotic effect in neuronal cells is unknown. Therefore, we investigated the role of ghrelin in ischemic neuronal injury using primary hypothalamic neurons exposed to oxygen-glucose deprivation (OGD). Here we report that treatment of hypothalamic neurons with ghrelin inhibited OGD-induced cell death and apoptosis. Exposure of neurons to ghrelin caused rapid activation of ERK1/2. Ghrelin-induced activation of ERK1/2 and the antiapoptotic effect of ghrelin were blocked by chemical inhibition of MAPK, phosphatidylinositol 3 kinase, protein kinase C, and protein kinase A. Ghrelin attenuated OGD-induced activation of c-Jun NH2-terminal kinase and p-38 but not ERK1/2. We also investigated ghrelin regulation of apoptosis at the mitochondrial level. Ghrelin protected cells from OGD insult by inhibiting reactive oxygen species generation and stabilizing mitochondrial transmembrane potential. In addition, ghrelin-treated cells showed an increased Bcl-2/Bax ratio, prevention of cytochrome c release, and inhibition of caspase-3 activation. Finally, in vivo administration of ghrelin significantly reduced infarct volume in an animal model of ischemia. Our data indicate that ghrelin may act as a survival factor that preserves mitochondrial integrity and inhibits apoptotic pathways.

scholarly journals Glucose Deprivation Regulates KATPChannel Trafficking via AMP-Activated Protein Kinase in Pancreatic β-Cells

Diabetes ◽  
2009 ◽  
Vol 58 (12) ◽  
pp. 2813-2819 ◽  
Author(s):  
Ajin Lim ◽  
Sun-Hyun Park ◽  
Jong-Woo Sohn ◽  
Ju-Hong Jeon ◽  
Jae-Hyung Park ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Glucose Deprivation ◽  
Β Cells ◽  
Pancreatic Β Cells ◽  
Amp Activated Protein Kinase
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