| Autor: |
Yu K; Boehringer Ingelheim Pharmaceuticals, Inc., Ridgefield, CT 06877, USA., Kennedy CA, O'Neill MM, Barton RW, Tatake RJ |
| Jazyk: |
angličtina |
| Zdroj: |
Apoptosis : an international journal on programmed cell death [Apoptosis] 2001 Jun; Vol. 6 (3), pp. 151-60. |
| DOI: |
10.1023/a:1011375024832 |
| Abstrakt: |
In the present investigations, we have shown differential cleavage of cellular PARP and a caspase 3-selective synthetic tetrapeptide substrate, Z-DEVD-AFC or Ac-DEVD-AMC using a T lymphoblastoid cell line Jurkat, and its variant clone E6.1(J-E6). Anti-Fas antibody-mediated apoptosis resulted in DNA fragmentation and PARP cleavage in both Jurkat and J-E6 cells. However, unlike Jurkat, J-E6 cells did not cleave a synthetic tetrapeptide substrate efficiently. The failure to cleave the DEVD tetrapeptide by apoptotic J-E6 cells was not due to insufficient expression or processing of caspase 3 in J-E6 cells. Interestingly, when the J-E6 cells were transiently transfected with a cDNA encoding caspase 3, efficient cleavage of Z-DEVD-AFC was achieved. The observations that apoptotic J-E6 cells barely cleaved a synthetic DEVD tetrapeptide, but efficiently cleaved endogenous PARP, potentially at the most preferred DEVD site, suggest that active caspases may have disparate characteristics to recognize substrates presented in different context. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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