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PMID: 8700913 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

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

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 93 ·No. 5 ·1996-03-05 ·Pages 2234-8

Kayalar C, Ord T, Testa MP, Zhong LT, Bredesen DE

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.

MeSH Terms
Actin Cytoskeleton/metabolism Actins/antagonists & inhibitors,metabolism Animals Apoptosis Caspase 1 Cysteine Endopeptidases/metabolism Humans Interleukin-1/metabolism PC12 Cells Peptide Mapping Protein Binding Rats Substrate Specificity
Chemicals
Actins Interleukin-1 Cysteine Endopeptidases Caspase 1
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Kayalar C
La Jolla Cancer Research Foundation, CA 92037, USA.
Ord T
Testa M P
Zhong L T
Bredesen D E
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.93.5.2234
Published
1996-03-05
Pages
2234-8
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC39941
Subset
IM
Grants
PHS HHS · 12282 · United States
External Links
PubMed source DOI: 10.1073/pnas.93.5.2234 PMC Full Text View journal details
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