title: Cleavage of actin by interleukin 1 beta-converting enzyme to reverse DNase I inhibition.
abstract: Three of the predominant features of apoptosis are internucleosomal DNA fragmentation, plasma membrane bleb formation, and retraction of cell processes. We demonstrate that actin is a substrate for the proapoptotic cysteine protease interleukin 1beta-converting enzyme. Actin cleaved by interleukin 1beta-converting enzyme can neither inhibit DNase I nor polymerize to its filamentous form as effectively as intact actin. These findings suggest a mechanism for the coordination of the proteolytic, endonucleolytic, and morphogenetic aspects of apoptosis.
authors.affiliation: La Jolla Cancer Research Foundation, CA 92037, USA.
authors.forename: C
authors.initials: C
authors.lastname: Kayalar
authors.forename: T
authors.initials: T
authors.lastname: Ord
authors.forename: M P
authors.initials: MP
authors.lastname: Testa
authors.forename: L T
authors.initials: LT
authors.lastname: Zhong
authors.forename: D E
authors.initials: DE
authors.lastname: Bredesen
mesh_terms: D008841:Actin Cytoskeleton / Q000378:metabolism; D000199:Actins / Q000037:antagonists & inhibitors / Q000378:metabolism*; D000818:Animals; D017209:Apoptosis; D020170:Caspase 1; D003546:Cysteine Endopeptidases / Q000378:metabolism*; D006801:Humans; D007375:Interleukin-1 / Q000378:metabolism; D016716:PC12 Cells; D010449:Peptide Mapping; D011485:Protein Binding; D051381:Rats; D013379:Substrate Specificity
chemical_list: D000199:Actins; D007375:Interleukin-1; D003546:Cysteine Endopeptidases; D020170:Caspase 1