Phospholipase C and phospholipase A2 are involved in the antiviral activity of human interferon-alpha.

Abstract:

:Treatment of human amniotic cells (UAC) with human interferon-alpha (Hu-IFN alpha) 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 32P 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 A2 are activated by Hu-IFN alpha. Addition of neomycin (an inhibitor of phospholipase C), as well as mepacrine (an inhibitor of phospholipase A2) to IFN-treated cells inhibited the antiviral activity of Hu-IFN alpha 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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Premecz G,Markovits A,Bagi G,Farkas T,Földes I

doi

10.1016/0014-5793(89)80635-0

subject

Has Abstract

pub_date

1989-06-05 00:00:00

pages

257-60

issue

2

eissn

0014-5793

issn

1873-3468

pii

0014-5793(89)80635-0

journal_volume

249

pub_type

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