scholarly journals Stimulation of human and mouse erythrocyte Na+-K+-2Cl−cotransport by osmotic shrinkage does not involve AMP-activated protein kinase, but is associated with STE20/SPS1-related proline/alanine-rich kinase activation

2010 ◽  
Vol 588 (13) ◽  
pp. 2315-2328 ◽  
Author(s):  
Brice Sid ◽  
Lisa Miranda ◽  
Didier Vertommen ◽  
Benoît Viollet ◽  
Mark H. Rider
2006 ◽  
Vol 70 (6) ◽  
pp. 1925-1934 ◽  
Author(s):  
Franck Rencurel ◽  
Marc Foretz ◽  
Michel R. Kaufmann ◽  
Deborah Stroka ◽  
Renate Looser ◽  
...  

FEBS Letters ◽  
2001 ◽  
Vol 505 (3) ◽  
pp. 348-352 ◽  
Author(s):  
Christophe Beauloye ◽  
Anne-Sophie Marsin ◽  
Luc Bertrand ◽  
Ulrike Krause ◽  
D.Grahame Hardie ◽  
...  

1995 ◽  
Vol 9 (7) ◽  
pp. 541-546 ◽  
Author(s):  
Nathalie Henin ◽  
M.‐Françoise Vincent ◽  
Harry E. Gruber ◽  
Georges Van Den Berghe

2003 ◽  
Vol 30 (2) ◽  
pp. 151-161 ◽  
Author(s):  
BA Kefas ◽  
Y Cai ◽  
Z Ling ◽  
H Heimberg ◽  
L Hue ◽  
...  

We have recently shown that conditions known to activate AMP-activated protein kinase (AMPK) in primary beta-cells can trigger their apoptosis. The present study demonstrates that this is also the case in the MIN6 beta-cell line, which was used to investigate the underlying mechanism. Sustained activation of AMPK was induced by culture with the adenosine analogue AICA-riboside or at low glucose concentrations. Both conditions induced a sequential activation of AMPK, c-Jun-N-terminal kinase (JNK) and caspase-3. The effects of AMPK on JNK activation and apoptosis were demonstrated by adenoviral expression of constitutively active AMPK, a condition which reproduced the earlier-described AMPK-dependent effects on pyruvate kinase and acetyl-coA-carboxylase. The effects of JNK activation on apoptosis were demonstrated by the observations that (i). its inhibition by dicumarol prevented caspase-3 activation and apoptosis, (ii). adenoviral expression of the JNK-interacting scaffold protein JIP-1/IB-1 increased AICA-riboside-induced JNK activation and apoptosis. In primary beta-cells, AMPK activation was also found to activate JNK, involving primarily the JNK 2 (p54) isoform. It is concluded that prolonged stimulation of AMPK can induce apoptosis of insulin-producing cells through an activation pathway that involves JNK, and subsequently, caspase-3.


Circulation ◽  
2016 ◽  
Vol 134 (5) ◽  
pp. 405-421 ◽  
Author(s):  
Hong Liu ◽  
Yujin Zhang ◽  
Hongyu Wu ◽  
Angelo D’Alessandro ◽  
Gennady G. Yegutkin ◽  
...  

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