Elevated PTEN activity was caused by cox 2 siRNA in hOBs. Furthermore, COX 2 silencing notably suppressed the PTEN phosphorylation at both Celecoxib Celebrex Ser380 and Ser380/Thr382/ 383. Results from densitometric quantification show that the decline in PTEN phosphorylation at Ser380 alone is not distinct from that at Ser380/ Thr382/383 in COX 2 silenced hOBs. In improvement, hOBs transfected with PTEN siRNA showed increased Akt phosphorylation and reduced p27Kip1 protein level but didn’t affect COX 2 levels, suggesting that COX 2 isn’t the target of PTEN in hOBs. We further examined whether COX 1 exhibits similar results as COX 2 on PTEN/Akt signaling in hOBs. COX 1 siRNA somewhat paid off mRNA levels but didn’t change of the levels of p Akt, p27Kip1 and p PTEN. Ramifications of COX 2 silencing on r Akt and p27Kip1 PGE2 may be the primary product of COX 2 enzymatic function. We examined Ribonucleic acid (RNA) the effects of PGE2 on p Akt and p27Kip1 levels in COX 2 silenced hOBs, to date=june 2011 that the COX 2 silencing induced loss of p Akt and raise in p27Kip1 were as a result of PGE2 deficiency. Our data show that PGE2 somewhat elevated cAMP levels in hOBs, showing that the PGE2 is bioactive. Moreover, both 100 and 10 nM of PGE2 significantly corrected COX 2 siRNA suppressed PGE2 production. These results suggested that 10 nM PGE2 is sufficient to replace the basal concentration of PGE2 in cultured hOBs. But, 10 nM PGE2 did not reverse the COX 2 siRNAmediated decrease of p Akt and upsurge in p27Kip1 levels in hOBs. The effective rhCOX 2 protein, however not inactivated rhCOX 2, significantly Besides COX Pemirolast 69372-19-6 2 enzymatic activity, leading to PGE2 generation, we examined whether the enzymatic activity of COX 2 also contributed to PTEN phosphorylation in hOBs by analyzing the result of rhCOX 2 protein transfection on PTEN phosphorylation. Our data show that rhCOX 2 protein transfection dramatically increased PGE2 production, and pre treatment of 10 uM NS398 on rhCOX 2 protein had no significant impact on PGE2 production. Most of all, rhCOX 2 protein transfection dramatically improved COX 2 and p PTEN levels, while inactivated rhCOX 2 could not raise p PTEN levels in hOBs. Since PGE2 replenishment failed to reverse the COX 2 siRNAinduced effects on Akt signaling, we examined whether COX 2 protein replenishment reversed COX 2 dependent effects in hOBs. Our data show that rhCOX 2 protein transfection somewhat changed COX 2 silencing dependent PGE2 decrease, while blocking the enzymatic action of rhCOX 2 by treatment with 10 uM NS398 suppressed rhCOX 2 dependent PGE2 production in hOBs. Above all, rhCOX 2 transfection significantly changed COX 2 siRNA suppressed COX 2 and p PTEN degrees in hOBs.