Antagonism of 2–5 A‐mediated inhibition of protein synthesis in intact cells by 2',5'‐(pA)3

FEBS Letters

Friedman, R.M.²  Black, Roberta J.¹  Imai, Jiro³  Torrence, Paul F.³ 

[1] Laboratory of Molecular Oncology, National Cancer Institute-Frederick Cancer Research Facility, National Institutes of Health, Frederick, MD 21701 USA;Department of Pathology, Uniformed Services University of the Health Sciences, 4301 Jones Bridge Road, Bethesda, MD 20814 USA;Laboratory of Chemistry, National Institute of Arthritis, Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA

关键词: Interferon;    2–5 A;    Protein synthesis;    2';    5'-(pA)3;    p5'A2'p5'A2'p5'A;    3';    5 '-(p2' dA)3;    p5' (2' dA)3;    p5' (2' dA)3' p5 ' (2' dA);   

DOI  :  10.1016/0014-5793(85)81013-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

In vitro studies have shown that the translational inhibitory activity of 2–5 A can be blocked by the oligoribonucleotide 2',5'-(pA)₃. We have examined the effect of simultaneous introduction of inhibitor and antagonist into intact mouse cells using calcium phosphate coprecipitation. Upon introduction of 10⁻⁴ M 2',5'-(pA)₃ and 10⁻⁶ M 2–5 A, inhibition of protein synthesis was prevented. Efficiency of calcium phosphate precipitation of 2–5 A in the presence or absence of 2',5'-(pA)₃ was comparable. Introduction of 2',5'-(pA)₃ analogs showed that nucleotides which do not bind well to the 2–5 A dependent endonuclease do not prevent 2–5 A inhibitory activity. Thus, 2',5'-(pA)₃ functions as an antagonist of 2–5 A in vivo.

【 授权许可】

Unknown