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Antagonism of 2–5 A‐mediated inhibition of protein synthesis in intact cells by 2',5'‐(pA) 3
Author(s) -
Black Roberta J.,
Friedman R.M.,
Imai Jiro,
Torrence Paul F.
Publication year - 1985
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(85)81013-9
Subject(s) - antagonism , antagonist , chemistry , in vivo , in vitro , coprecipitation , calcium , phosphate , nucleotide , inhibitory postsynaptic potential , biochemistry , pharmacology , receptor , biology , endocrinology , inorganic chemistry , microbiology and biotechnology , organic chemistry , gene
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.