@article{ref1,
title="DNA fragmentation during thymic apoptosis is catalyzed by DNase γ",
journal="Apoptosis",
year="1996",
author="Tanuma, S.",
volume="1",
number="2",
pages="147-152",
abstract="The physiological and pathological importance of cell death by apoptosis has recently been recognized. One of the hallmarks of apoptosis is the enzymatic cleavage of genomic DNA into nucleosomal oligomers. The identification of an endonuclease responsible for apoptosis might help to explain how this cell suicide is regulated and why DNA is cleaved. Here, we found that γ type of DNase was retained in apoptotic rat thymocyte nuclei. Homogeneously purified DNase γ (Mr = 33 kDa) from the apoptotic nuclei was revealed to be a Ca2+/Mg2+-dependent endonuclease and inhibited by Zn2+. This enzyme cleaved chromosomal DNA with 3'-hydroxyl (OH) and 5'-phosphoryl (P) ends. The cleavage ends and its divalent cation dependencies match those observed in apoptotic thymocytes induced by X-irradiation or glucocorticoid treatment, indicating that this endonuclease is a central component of the thymic apoptosis machinery. © 1990 Rapid Science Publishers.<p /><p>Language: en</p>",
language="en",
issn="1360-8185",
doi="10.1007/bf01321021",
url="http://dx.doi.org/10.1007/bf01321021"
}