AMP-Activated Protein Kinase is Highly Expressed in Neurons in the Developing Rat Brain and Promotes Neuronal Survival Following Glucose Deprivation

2001 ◽  
Vol 17 (1) ◽  
pp. 45-58 ◽  
Author(s):  
Carsten Culmsee ◽  
Jennifer monnig ◽  
Bruce E. Kemp ◽  
Mark P. Mattson
Keyword(s):  
Protein Kinase ◽  
Rat Brain ◽  
Neuronal Survival ◽  
Glucose Deprivation ◽  
Amp Activated Protein Kinase ◽  
Developing Rat

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.

Expanding roles for AMP-activated protein kinase in neuronal survival and autophagy

BioEssays ◽  
2009 ◽  
Vol 31 (9) ◽  
pp. 944-952 ◽  
Author(s):  
Jeroen Poels ◽  
Miloš R. Spasić ◽  
Patrick Callaerts ◽  
Koenraad K. Norga
Keyword(s):  
Protein Kinase ◽  
Neuronal Survival ◽  
Amp Activated Protein Kinase

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
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