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Phospholipase C and phospholipase A 2 are involved in the antiviral activity of human interferon‐α
Author(s) -
Premecz György,
Markovits Andrea,
Bagi György,
Farkas Tibor,
Földes István
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)80635-0
Subject(s) - vesicular stomatitis virus , phospholipase c , phospholipase a2 , biochemistry , arachidonic acid , phospholipase , diacylglycerol kinase , phospholipid , phospholipase a , biology , cytosol , phosphoinositide phospholipase c , protein kinase c , interferon , phorbol , mechanism of action , chemistry , microbiology and biotechnology , enzyme , in vitro , membrane , virus , virology
Treatment of human amniotic cells (UAC) with human interferon‐α (Hu‐IFNα) or phorbol myristate acetate (PMA) resulted in translocation of protein kinase C (PK‐C) activity from the cytosol fraction to that of the membranes. Analysis of 32 P incorporation into phospholipid fractions and studies of alterations in fatty acid content for the major phospholipids of IFN‐treated cells suggest that phospholipases C and A 2 are activated by Hu‐IFNα . Addition of neomycin (an inhibitor of phospholipase C), as well as mepacrine (an inhibitor of phospholipase A 2 ) to IFN‐treated cells inhibited the antiviral activity of Hu‐IFNα in the vesicular stomatitis virus (VSV)‐UAC system used. These observations indicate that (i) activation of PK‐C and (ii) diacylglycerol formation, arachidonic acid and/or lysophosphatidylcholine release are important steps in the mechanism of action of IFN.