DOI: 10.1073/pnas.93.5.2234. Cleavage of actin by interleukin 1 beta-converting enzyme to reverse DNase I inhibition.

Cleavage of actin by interleukin 1 beta-converting enzyme to reverse DNase I inhibition.

10.1073/pnas.93.5.2234

Crossref journal-article

Proceedings of the National Academy of Sciences

Proceedings of the National Academy of Sciences (341)

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 5

C Kayalar (first)
T Ord (additional)
M P Testa (additional)
L T Zhong (additional)
D E Bredesen (additional)

References 0 Referenced 225

None

Dates

Type	When
Created	23 years, 1 month ago (July 26, 2002, 10:35 a.m.)
Deposited	3 years, 4 months ago (April 13, 2022, 3:03 p.m.)
Indexed	1 month, 2 weeks ago (July 6, 2025, 1:43 p.m.)
Issued	29 years, 5 months ago (March 5, 1996)
Published	29 years, 5 months ago (March 5, 1996)
Published Online	29 years, 5 months ago (March 5, 1996)
Published Print	29 years, 5 months ago (March 5, 1996)

Funders 0

None

BibTeX

@article{Kayalar_1996, title={Cleavage of actin by interleukin 1 beta-converting enzyme to reverse DNase I inhibition.}, volume={93}, ISSN={1091-6490}, url={http://dx.doi.org/10.1073/pnas.93.5.2234}, DOI={10.1073/pnas.93.5.2234}, number={5}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={Kayalar, C and Ord, T and Testa, M P and Zhong, L T and Bredesen, D E}, year={1996}, month=mar, pages={2234–2238} }

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