Premium
(2′‐5′)A n ‐dependent endoribonuclease: Enzyme levels are regulated by IFNβ, IFNγ, and cell culture conditions
Author(s) -
FloydSmith Georgia
Publication year - 1988
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.240380103
Subject(s) - rnase p , endoribonuclease , interferon , microbiology and biotechnology , biology , cell culture , cell , cell growth , enzyme , ribonuclease , rna , rnase mrp , biochemistry , virology , gene , genetics
The levels of a (2′‐5′) A n ‐dependent endonuclease (RNase L) were determined in extracts prepared from murine L cells and Ehrlich ascites tumor (EAT) cells by measuring specific binding of protein to a labeled derivative of (2′‐5′)A n , (2′‐5′)A 3 [ 32 P]pCp. RNase L levels were found to depend both on interferon (IFN) treatment and on cell growth conditions. Treatment of murine L cells and EAT cells with 100–2,000 IRU IFNβ or IFNγ resulted in a similar 2–4‐fold increase in the levels of RNase L when cells were present at low density. The levels of RNase L were also shown to increase 2–3‐fold as cells approached saturation density. Serum‐starved cells also displayed relatively high levels of RNase L. RNase L levels in cells maintained at high cell density did not change appreciably following treatment with IFNβ or IFNγ. Regulation of RNase L levels by cell growth conditions as well as by IFNβ or IFNγ treatment suggests that RNase L may play an important role in regulating the levels of cellular mRNAs as well as acting to degrade viral RNAs.
Accelerating Research
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom
Address
John Eccles HouseRobert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom