| In the present study , we searched a protein data base for potential death substrates possessing the CPP 32 cleavage site , DEVD , and identified several candidates including RFC 140 , the large subunit of replication factor C , which we subsequently demonstrated to be specifically cleaved in a variety of cell types undergoing apoptosis in response to different cytotoxic agents , whereas no degradation is observed in a cell line resistant to etoposide induced apoptosis . ^^^ The abrogation of RFC 140 cleavage in apoptotic extracts by Ac DEVD CHO , a potent inhibitor of CPP 32 , together with the finding that a CPP 32 consensus cleavage sequence , DEVD , exists in RFC 140 , suggests that CPP 32 or a close relative is responsible for RFC 140 degradation in apoptosis . . ^^^ |