Isolation and partial characterization of a protease involved in Fas-induced apoptosis.
Protease involvement has been implicated in the signalling process of activation-induced apoptosis. Here we report the isolation of a protease from Jurkat T cells undergoing Fas-induced apoptosis. Although the protease probably is a serine protease, it seems to be distantly related to members of the ICE/ced-3/Ich-1(nedd-2) family. In a cell-free system using isolated thymocyte nuclei, the protease rapidly induces DNA fragmentation and morphological changes typically seen in apoptosis. Our results clearly show protease activation downstream to Fas-ligation and implicate an important role for the isolated protease in signalling of Fas-induced apoptosis.
Schlegel
J
J
Institute of Environmental Medicine, Karolinska Institutet, Stockholm, Sweden.
Peters
I
I
Orrenius
S
S
D000818:Animals; D000954:Antigens, Surface / Q000378:metabolism*; D017209:Apoptosis / Q000187:drug effects / Q000276:immunology* / Q000502:physiology*; D020170:Caspase 1; D002460:Cell Line; D002467:Cell Nucleus / Q000201:enzymology; D003546:Cysteine Endopeptidases / Q000378:metabolism; D010450:Endopeptidases / Q000302:isolation & purification* / Q000378:metabolism; D006801:Humans; D066298:In Vitro Techniques; D011480:Protease Inhibitors / Q000494:pharmacology; D051381:Rats; D015398:Signal Transduction; D013601:T-Lymphocytes / Q000166:cytology / Q000201:enzymology / Q000276:immunology; D019014:fas Receptor
D000954:Antigens, Surface; D011480:Protease Inhibitors; D019014:fas Receptor; D010450:Endopeptidases; D003546:Cysteine Endopeptidases; D020170:Caspase 1