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Caspase-7 Gene Disruption Reveals an Involvement of the Enzyme during the Early Stages of Apoptosis

Lookup NU author(s): Professor Colin Dingwall

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Abstract

Caspases play a key role during apoptotic execution. In an attempt to elucidate the specific role of caspase-7 we generated a chicken DT40 cell line in which both alleles of the gene were disrupted. Viability assays showed that caspase-7(-/-) clones are more resistant to the common apoptosis-inducing drugs etoposide and staurosporine. Caspase-7(-/-) cells show a delay in phosphatidylserine externalization and DNA fragmentation as well as cleavage of the caspase substrates poly(ADP-ribose) polymerase 1 and lamins B1 and B2. Caspase affinity labeling and activity assays indicated that deficient cells exhibit a delay in caspase activation compared with wild type DT40 cells, providing an explanation for the differences in apoptotic execution between caspase-7 null and wild type DT40 cells. These results strongly suggest that caspase-7 is involved earlier than other effector caspases in the apoptotic execution process in DT40 B lymphocytes.

Publication metadata

Author(s): Korfali N, Ruchaud S, Loegering D, Bernard D, Dingwall C, Kaufmann SH, Earnshaw WC

Publication type: Article

Publication status: Published

Journal: Journal of Biological Chemistry

Year: 2004

Volume: 279

Issue: 2

Pages: 1030-1039

ISSN (print): 0021-9258

ISSN (electronic): 1083-351X

Publisher: The American Society for Biochemistry and Molecular Biology, Inc.

URL: http://dx.doi.org/10.1074/jbc.M306277200

DOI: 10.1074/jbc.M306277200

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