Inositol phospholipid turnover and protein kinase C translocation are stimulated by poly(I).poly(C) in human amnion cells (UAC).
Polyinosinic-polycytidylic acid, a potent inducer of inducer of interferon (IFN) production and activator of some IFN-induced enzymes, inhibits [3H]uridine incorporation into the RNA of vesicular stomatitis virus even in the absence of IFN synthesis, transiently triggers the breakdown of inositol phospholipids and activates the translocation of protein kinase C. Since IFNs also have similar activities these results suggest that IFN induction and IFN function are realised through common biochemical pathways.
Premecz
G
G
Microbiological Research Group, National Institute of Hygiene, Budapest, Hungary.
Markovits
A
A
Bagi
G
G
Farkas
T
T
Földes
I
I
D000650:Amnion / Q000187:drug effects / Q000378:metabolism*; D002472:Cell Transformation, Viral / Q000187:drug effects; D002478:Cells, Cultured; D006801:Humans; D007294:Inositol / Q000378:metabolism; D007700:Kinetics; D010716:Phosphatidylinositols / Q000378:metabolism*; D011070:Poly I-C / Q000494:pharmacology*; D011493:Protein Kinase C / Q000378:metabolism*; D014721:Vesicular stomatitis Indiana virus / Q000187:drug effects / Q000235:genetics
D010716:Phosphatidylinositols; D007294:Inositol; D011493:Protein Kinase C; D011070:Poly I-C