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Involvement of poly(ADP‐ribose) polymerase and activation of caspase‐3‐like protease in heat shock‐induced apoptosis in tobacco suspension cells
Author(s) -
Tian Rui-Hua,
Zhang Gui-You,
Yan Chang-Hui,
Dai Yao-Ren
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)01561-1
Subject(s) - poly adp ribose polymerase , dna laddering , apoptosis , polymerase , protease , microbiology and biotechnology , caspase , biology , hsp70 , dna fragmentation , programmed cell death , chemistry , heat shock protein , biochemistry , dna , enzyme , gene
The cleavage of poly(ADP‐ribose) polymerase (PARP) by caspase (casp)‐3 is an essential link in the apoptotic pathway in animal cells. In plant cells, however, there is no authentic evidence for the similar role that PARP may play during apoptosis. Using a heat shock (HS)‐induced apoptosis system of tobacco cells, we found that immediately after a 4 h heat treatment, PARP was cleaved to form an 89 kDa signature fragment, while DNA laddering appeared only after a 20 h recovery following the HS. An activation of casp‐3‐like protease was also observed. The results suggest that apoptosis in plants and animals may share common mechanisms. On the other hand, when cells were preincubated with 4 mM 3‐aminobenzamide or 2–8 mM nicotinamide, the specific inhibitors of PARP, before HS treatment, apoptotic cell death was reduced significantly. Our results thus imply that PARP may also be involved in apoptosis in a different way from the casp‐related events.