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Effect of interferon on phospholipid methylation by peripheral blood mononuclear cells
Author(s) -
Bougnoux P.,
Bonvini E.,
Chang Z.L.,
Hoffman T.
Publication year - 1982
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/jcb.240200302
Subject(s) - phosphatidylethanolamine , phospholipid , peripheral blood mononuclear cell , phosphatidylcholine , methylation , methyltransferase , biochemistry , chemistry , methionine , enzyme , intracellular , interferon , microbiology and biotechnology , biology , membrane , in vitro , immunology , dna , amino acid
The effect of human interferon (IFN) preparations on the metabolic pathway leading to the synthesis of phosphatidylcholine (PC) by a stepwise addition of methyl groups to phosphatidylethanolamine (PE) was investigated in human peripheral blood mononuclear (PBMN) cells. An inhibition of the synthesis of PC via this pathway was regularly observed with both α‐ (recombinant or natural) and β‐IFN. This inhibition was apparent within the first 5 min of treatment, reached its maximum between 15 min and 1 hr, and persisted at the same level until 6 hr, the last time point examined. Each of the transmethylated products of PF underwent a similar inhibition, as measured by the turnover rate of individual products. The intracellular pool of the methyl donors, methionine and S ‐adenosyl‐methionine (SAM), was shown to be unaffected. The methyltransferase activity of IFN‐pretreated cell extracts was unchanged. These findings support the hypothesis that IFN induces a functional change in phospholipid methylation at the level of organized membrane‐bound phospholipid methyltransferase enzymes in intact cells.