APK regulated IFN-c induced nucleotide Re translocation of PKC was, they had no significant effect on IFN-c stimulates PKC and STAT1 phosphorylation mediated IRF-1 expression. In light of these observations, Tipifarnib R115777 it was interesting, the contribution of these signaling pathways in the expression of type IV CIITA and MHC-II IFN-stimulated BMDM determine c. As shown recently had 19, the inhibition of p38 MAPK had no significant effect on gene expression either CIITA or MHC-II. In contrast, inhibition of PI3K strong expression of type IV CIITA and MHC-II genes adversely Chtigt what r one The important PI3K in the modulation of the IFN response in BMDM c induced. Taken together, these data suggest that although PKC activity t is important to its nuclear translocation is not necessary to IFN type IV C stimulates CIITA and MHC-II gene expression, and the point of the existence of regulatory mechanisms that are not identified PI3K.
Clearly, further study is needed to better understand BAY 73-4506 the regulation of expression of CIITA. In contrast to the expression of IRF 1, CIITA and MHC II on the JAK STAT h Depends, PKC activation, has occurred independently of p38 MAPK and PI3K Ngig of JAK2 in IFN-c stimulated BMDM. These results raise the question of how IFN signaling pathways activated C independent Ngig of JAK. A recent study shows that IFN c is a physical association between rapid IFN-c receptor 1 and the adapter MyD88 and the formation of a p38 MAPK signalosome contains lt Mixed line kinase and c-Jun N terminal kinase interacting protein 1 induces, 11 A hnlicher mechanism nnte k explained Ren, the activation of PI3K, which has proven to be stimulated with LPS in MyD88 associate macrophages.
40 Whether the case has for the activation of PKC by IFN c is not yet proven. It is clear that further investigation be necessary to examine the r Potential MyD88 in mediating the activation of PKC and PI3K has in macrophages stimulated with IFN c. The finding that IFN c stimulation of phosphorylation of serine 727 STAT1 of G 6976 inhibited ¨ suggesting that PKC acted as a kinase for this phosphorylation and is consistent with the observation that IFN induces the association of PKC has C STAT1. A r Similar to the PKC d in acute Promyelozytenleuk Mie cells was reported Been shown Where is to phosphorylate PKC for a connection and STAT1.
14 contrast to most nuclear proteins lacking PKC isozymes a signal canonical nuclear localization, 41 out suggesting that other mechanisms are involved in the transport process. When phosphorylated STAT1 dimers translocate to the nucleus, it is m Possible that PKC STAT1 used as a shuttle service to access the kernel. Acknowledgments We thank Marcel Desrosiers and Dr. Robert Lodge for their help in confocal microscopy and immunofluorescence. This work was supported by the Canadian Institutes of Health Research Grant MOP 12933rd Albert Descoteaux h Lt Canada Research Chair and was a Fellow Researcher of the FRSQ. Tamsir O. Diallo was supported in part by a postdoctoral fellowship from the Pasteur Foundation / Fondation Armand-Frappier. Christine mat was supported by grants from the Canadian Institutes of Health Research. Progression of the proteins