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 ◽  
...  
2017 ◽  
Vol 292 (21) ◽  
pp. 8716-8728 ◽  
Author(s):  
Yoshifumi Sato ◽  
Tomonori Tsuyama ◽  
Chinami Sato ◽  
Md. Fazlul Karim ◽  
Tatsuya Yoshizawa ◽  
...  

2013 ◽  
Vol 85 (7) ◽  
pp. 991-998 ◽  
Author(s):  
Ramachandran Balasubramanian ◽  
Hiroshi Maruoka ◽  
P. Suresh Jayasekara ◽  
Zhan-Guo Gao ◽  
Kenneth A. Jacobson

2017 ◽  
Vol 41 (5) ◽  
pp. 544-554 ◽  
Author(s):  
Chunyan Liu ◽  
Yanan Hao ◽  
Fei Yin ◽  
Yonglan Zhang ◽  
Jianhui Liu

2019 ◽  
Vol 75 (4) ◽  
pp. 423-432 ◽  
Author(s):  
Tomasz Szkudelski ◽  
Katarzyna Szkudelska

Abstract AMP-activated protein kinase (AMPK) is present in different kinds of metabolically active cells. AMPK is an important intracellular energy sensor and plays a relevant role in whole-body energy homeostasis. AMPK is activated, among others, in response to glucose deprivation, caloric restriction and increased physical activity. Upon activation, AMPK affects metabolic pathways leading to increased formation of ATP and simultaneously reducing ATP-consuming processes. AMPK is also expressed in pancreatic β cells and is largely regulated by glucose, which is the main physiological stimulator of insulin secretion. Results of in vitro studies clearly show that glucose-induced insulin release is associated with a concomitant inhibition of AMPK in β cells. However, pharmacological activation of AMPK significantly potentiates the insulin-secretory response of β cells to glucose and to some other stimuli. This effect is primarily due to increased intracellular calcium concentrations. AMPK is also involved in the regulation of gene expression and may protect β cells against glucolipotoxic conditions. It was shown that in pancreatic islets of humans with type 2 diabetes, AMPK is downregulated. Moreover, studies with animal models demonstrated impaired link between glucose and AMPK activity in pancreatic islet cells. These data suggest that AMPK may be a target for compounds improving the functionality of β cells. However, more studies are required to better elucidate the relevance of AMPK in the (patho)physiology of the insulin-secreting cells.


2010 ◽  
Vol 425 (3) ◽  
pp. 541-551 ◽  
Author(s):  
Diana Han ◽  
Byungho Yang ◽  
L. Karl Olson ◽  
Alexander Greenstein ◽  
Seung-Hoon Baek ◽  
...  

Chronic hyperglycaemia is detrimental to pancreatic β-cells by causing impaired insulin secretion and diminished β-cell function through glucotoxicity. Understanding the mechanisms underlying β-cell survival is crucial for the prevention of β-cell failure associated with glucotoxicity. Autophagy is a dynamic lysosomal degradation process that protects organisms against metabolic stress. To date, little is known about the physiological function of autophagy in the pathogenesis of diabetes. In the present study, we explored the roles of autophagy in the survival of pancreatic β-cells exposed to high glucose using pharmacological and genetic manipulation of autophagy. We demonstrated that chronic high glucose increases autophagy in rat INS-1 (832/13) cells and pancreatic islets, and that this increase is enhanced by inhibition of 5′-AMP-activated protein kinase. Our results also indicate that stimulation of autophagy rescues pancreatic β-cells from high-glucose-induced cell death and inhibition of autophagy augments caspase-3 activation, suggesting that autophagy plays a protective role in the survival of pancreatic β-cells. Greater knowledge of the molecular mechanisms linking autophagy and β-cell survival may unveil novel therapeutic targets needed to preserve β-cell function.


2002 ◽  
Vol 30 (2) ◽  
pp. 307-311 ◽  
Author(s):  
I. Leclerc ◽  
B. Viollet ◽  
G. da Silva Xavier ◽  
A. Kahn ◽  
G. A. Rutter

AMP-activated protein kinase (AMPK) is a regulator of cellular metabolism in response to changes in the energy status of the cells. AMPK was known to shut down energy-consuming pathways in response to a fall in the ATP/AMP ratio by phosphorylating key enzymes of intermediate metabolism. Here we will discuss the recent evidence implicating AMPK in the regulation of gene expression in mammals, mainly in the liver and in the pancreatic β-cells.


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