期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1981
卷号：78
期号：6
页码：3343-3347
DOI：10.1073/pnas.78.6.3343
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：Superoxide dismutase (SOD; superoxide: superoxide oxidoreductase, EC 1.15.1.1 ) catalyzes the dismutation of O2- free radicals formed during various enzymatic reactions or by ionizing radiation. Genes coding for SOD and sensitivity to exogenous interferon (IF) are syntenic in both mouse and man. Diethyldithiocarbamate (DDC) has been shown to inhibit SOD activity by chelating Cu2+, the metal ion essential for the catalytic activity of the enzyme. Mouse cell lines L, L929, L1210 S6, and L1210 R3 and a human cell line (WISH) pretreated with homologous IF and different concentrations of DDC for various periods of time were tested for their ability to support virus multiplication. Treatment of cells with DDC resulted in dose- and time-dependent inhibition of SOD activity and, simultaneously, in the reduction of antiviral protection by exogenous IF. Cells pretreated for 4 hr with DDC and then washed thoroughly were also resistant to IF, but DDC was without effect if the IF effect was first "established" by a 4-hr exposure to IF before addition of DDC. Under the conditions employed, DDC treatment did not result in any detectable inhibition of DNA, RNA, or protein synthesis in these cells. The data suggest that SOD or a related Cu2+-requiring enzyme may be necessary for the establishment of the IF-induced antiviral state in both human and murine cells.
