Sigma-1 receptor stimulation by dehydroepiandrosterone ameliorates cognitive impairment through activation of CaM kinase II, protein kinase C and extracellular signal-regulated kinase in olfactory bulbectomized mice

2011 ◽  
Vol 117 (5) ◽  
pp. 879-891 ◽  
Author(s):  
Shigeki Moriguchi ◽  
Yui Yamamoto ◽  
Tatsuya Ikuno ◽  
Kohji Fukunaga
Keyword(s):  
Protein Kinase C ◽  
Cognitive Impairment ◽  
Cam Kinase Ii ◽  
Cam Kinase ◽  
Receptor Stimulation ◽  
Sigma 1 Receptor ◽  
Extracellular Signal Regulated Kinase ◽  
Kinase C ◽  
Extracellular Signal ◽  
Sigma 1

scholarly journals Differential targeting of protein kinase C and CaM kinase II signalings to vimentin.

1995 ◽  
Vol 131 (4) ◽  
pp. 1055-1066 ◽  
Author(s):  
M Ogawara ◽  
N Inagaki ◽  
K Tsujimura ◽  
Y Takai ◽  
M Sekimata ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Signaling Pathways ◽  
Phosphorylation Site ◽  
Ectopic Expression ◽  
Expression Vectors ◽  
Cam Kinase Ii ◽  
Cam Kinase ◽  
Receptor Stimulation ◽  
Kinase C

Hydrolysis of inositol phospholipids by receptor stimulation activates two separate signaling pathways, one leading to the activation of protein kinase C (C kinase) via formation of diacylglycerol. The other is the inositol trisphosphate (IP3)/Ca2+ pathway and a major downstream kinase which is activated is Ca2+/calmodulin-dependent protein kinase II (CaM kinase II). To examine signaling pathways of C kinase and CaM kinase II to the cytoskeletal protein vimentin, we prepared monoclonal antibodies YT33 and MO82 which recognize the phosphorylation state of vimentin by C kinase and by CaM kinase II, respectively. Ectopic expression of constitutively active C kinase or CaM kinase II in primary cultured astrocytes by microinjection of the corresponding expression vectors induced phosphorylation of vimentin at each specific phosphorylation site, followed by reorganization of vimentin filament networks. In contrast, simultaneous activation of C kinase and CaM kinase II by inositol phospholipid hydrolysis with receptor stimulation led to an exclusive phosphorylation of vimentin at the CaM kinase II site, not at the site of C kinase. These results indicate that the intracellular targeting of C kinase and CaM kinase II signalings to vimentin is regulated separately, under physiological conditions.

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