Hypothermia-dependent and -independent effects of forced swim on the phosphorylation states of signaling molecules in mouse hippocampus.
2012
Abstract Forced swim (FS) stress induces diverse biochemical responses in the brain of rodents. Here, we examined the effect of hypothermia induced by FS in cold water on the
phosphorylationof FS-sensitive signaling molecules in the mouse brain. As we have shown previously, FS in cold water induced a significant increase in the level of tyrosine
phosphorylationof SIRPα, a neuronal membrane protein, in mouse hippocampus, while such effect of FS was markedly reduced in mice subjected to FS in warm water. FS in cold water also induced
phosphorylationof
mitogen-activated protein kinase kinase(MEK) as well as of cAMP response element-binding protein (
CREB), or
dephosphorylationof α isoform of Ca 2+ /calmodulin-dependent protein kinase II (αCaMKII) in the hippocampus. These effects of FS on the
phosphorylationof these molecules were also lost in mice subjected to FS in warm water. Genetic ablation of SIRPα did not change the
phosphorylationstates of these molecules in the brain. Forced cooling of anesthetized mice, which induced a marked increase in the
phosphorylationof SIRPα, induced
dephosphorylationof αCaMKII in the brain, while the same treatment did not affect the
phosphorylationlevel of MEK and
CREB.
Hibernationalso induced an increase and a decrease of the
phosphorylationof SIRPα and αCaMKII, respectively, in the brain of
chipmunk. These results suggest that hypothermia is a major element that determines the levels of
phosphorylationof αCaMKII and SIRPα during the FS in cold water, while it is not for the
phosphorylationlevels of MEK and
CREB.
Keywords:
-
Correction
-
Source
-
Cite
-
Save
27
References
1
Citations
NaN
KQI