Abstract:
:To investigate the involvement of proteases in apoptosis, rat thymocytes were treated with the glucocorticoid hormone methylprednisolone or the topoisomerase II inhibitor etoposide in the presence of selective substrate inhibitors of either interleukin-1 beta-converting enzyme (ICE), (Z-Val-Ala-Asp-chloromethylketone, VADcmk) or Ca(2+)-regulated serine protease (Suc-Ala-Ala-Pro-Phe-chloromethylketone, AAPFcmk). VADcmk protected from lamin proteolysis, chromatin fragmentation, cell shrinkage, and formation of apoptotic nuclei in both methylprednisolone- and etoposide-treated thymocytes when present during the initiation of the apoptotic process. AAPFcmk prevented lamin breakdown, chromatin fragmentation, and apoptotic morphological changes in thymocytes treated with methylprednisolone, but not with etoposide. Both MPS- and etoposide-treated thymocytes exhibited enhanced ICE-like protease activity which was maximal 1 h after treatment. This increase in proteolytic activity was blocked by VADcmk, but not AAPFcmk. Our findings suggest that ICE-like protease activity is critically involved in the early phase of both methylprednisolone- and etoposide-induced apoptosis in thymocytes, whereas the Ca(2+)-regulated serine protease is an obligatory component of the proteolytic cascade in methylprednisolone-induced apoptosis.
journal_name
Exp Cell Resjournal_title
Experimental cell researchauthors
Zhivotovsky B,Gahm A,Ankarcrona M,Nicotera P,Orrenius Sdoi
10.1006/excr.1995.1391subject
Has Abstractpub_date
1995-12-01 00:00:00pages
404-12issue
2eissn
0014-4827issn
1090-2422pii
S0014-4827(85)71391-2journal_volume
221pub_type
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