|  Help  |  About  |  Contact Us

Publication : Developmental defects and rescue from glucose intolerance of a catalytically-inactive novel Ship2 mutant mouse.

First Author  Dubois E Year  2012
Journal  Cell Signal Volume  24
Issue  11 Pages  1971-80
PubMed ID  22750293 Mgi Jnum  J:256569
Mgi Id  MGI:6115955 Doi  10.1016/j.cellsig.2012.06.012
Citation  Dubois E, et al. (2012) Developmental defects and rescue from glucose intolerance of a catalytically-inactive novel Ship2 mutant mouse. Cell Signal 24(11):1971-80
abstractText  The function of the phosphoinositide 5-phosphatase Ship2 was investigated in a new mouse model expressing a germline catalytically-inactive Ship2(/) mutant protein. Ship2(/) mice were viable with defects in somatic growth and in development of muscle, adipose tissue and female genital tract. Lipid metabolism and insulin secretion were also affected in these mice, but glucose tolerance, insulin sensitivity and insulin-induced PKB phosphorylation were not. We expected that the expression of the catalytically inactive Ship2 protein in PI 3''-kinase-defective p110alpha(D933A/+) mice would counterbalance the phenotypes of parental mice by restoring normal PKB signaling but, for most of the parameters tested, this was not the case. Indeed, often, the Ship2(/) phenotype had a dominant effect over the p110alpha(D933A/+) phenotype and, sometimes, there was a surprising additive effect of both mutations. p110alpha(D933A/+)Ship2(/) mice still displayed a reduced PKB phosphorylation in response to insulin, compared to wild type mice yet had a normal glucose tolerance and insulin sensitivity, like the Ship2(/) mice. Together, our results suggest that the Ship2(/) phenotype is not dependent on an overstimulated class I PI 3-kinase-PKB signaling pathway and thus, indirectly, that it may be more dependent on the lack of Ship2-produced phosphatidylinositol 3,4-bisphosphate and derived phosphoinositides.
Quick Links:
 
Quick Links:
 

Expression

Publication --> Expression annotations

 

Other

7 Bio Entities

Trail: Publication

0 Expression