Monitoring activation of ribonuclease L by 2',5'-oligoadenylates using purified recombinant enzyme and intact malignant glioma cells.
A wide range of methods have been developed to study RNase L activation in cell-free systems and in intact cells. Many of the original methods were developed in the laboratory of I. Kerr in the early 1980s (e.g., see Knight et al.). Additional methods described in this article were developed or adapted from research in other fields after the cloning of RNase L and the appreciation of its role in apoptosis. These methods provide the basic techniques needed to induce RNase L activation in vitro and to measure some of its biological effects in living mammalian cells.
Rusch
L
L
Department of Cancer Biology, Lerner Research Institute, Cleveland Clinic Foundation, Cleveland, Ohio 44195, USA.
Dong
B
B
Silverman
R H
RH
D000227:Adenine Nucleotides / Q000494:pharmacology*; D017304:Annexin A5 / Q000378:metabolism; D004722:Endoribonucleases / Q000378:metabolism*; D004789:Enzyme Activation; D005910:Glioma / Q000201:enzymology* / Q000473:pathology; D006801:Humans; D006868:Hydrolysis; D009843:Oligoribonucleotides / Q000494:pharmacology*; D012335:RNA, Ribosomal / Q000378:metabolism; D011994:Recombinant Proteins / Q000378:metabolism; D014407:Tumor Cells, Cultured
D000227:Adenine Nucleotides; D017304:Annexin A5; D009843:Oligoribonucleotides; D012335:RNA, Ribosomal; D011994:Recombinant Proteins; C023505:2',5'-oligoadenylate; D004722:Endoribonucleases; C031956:2-5A-dependent ribonuclease