Formation of 50 kbp chromatin fragments in isolated liver nuclei is mediated by protease and endonuclease activation
| Autor: | Pierluigi Nicotera, Sten Orrenius, David Wade, Annie Gahm, Boris Zhivotovsky |
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| Rok vydání: | 1994 |
| Předmět: |
Male
Proteases medicine.medical_treatment Biophysics Apoptosis Cell Fractionation Cleavage (embryo) Biochemistry Liver nuclei Divalent Serine Endonuclease Structural Biology Endopeptidases Genetics medicine Animals Rats Wistar Molecular Biology Cell Nucleus chemistry.chemical_classification Protease biology Chemistry Cell Biology Endonucleases Molecular biology Chromatin Rats Enzyme Activation Liver biology.protein Calcium DNA Damage |
| Zdroj: | FEBS Letters. 351:150-154 |
| ISSN: | 0014-5793 |
| DOI: | 10.1016/0014-5793(94)00827-2 |
| Popis: | 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, Ca2+ or Mg2+ 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 Ca2+. 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. |
| Databáze: | OpenAIRE |
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