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Formation of 50 kbp chromatin fragments in isolated liver nuclei is mediated by protease and endonuclease activation
Author(s) -
Zhivotovsky Boris,
Wade David,
Gahm Annie,
Orrenius Sten,
Nicotera Pierluigi
Publication year - 1994
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 - 10.1016/0014-5793(94)00827-2
Subject(s) - chromatin , proteases , cleavage (geology) , dna fragmentation , microbiology and biotechnology , dna , endonuclease , fragmentation (computing) , biology , divalent , chemistry , apoptosis , biochemistry , enzyme , programmed cell death , paleontology , ecology , organic chemistry , fracture (geology)
Isolated rat liver nuclei were incubated in the presence of divalent cations, and the mechanisms underlying the subsequent chromatin fragmentation were investigated. Either of the two cations, Ca 2+ or Mg 2+ was sufficient to produce chromatin fragments with sizes between 700 and 300 kbp. The formation of chromatin fragments of 50 kbp as well as the following internucleosomal DNA cleavage ‐ which are characteristic of apoptosis ‐ were markedly stimulated in the presence of Ca 2+ . Chromatin degradation to 50 kbp and smaller (oligonucleosome‐size) fragments was prevented by inhibitors of endonucleases and serine proteases. We suggest a mechanism whereby the concerted activity of both proteases and endonucleases results in the widespread chromatin cleavage observed in cellls undergoing apoptosis.