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Internucleosomal DNA fragmentation following the activation of endonucleases is the common end point of apoptosis. DNase I, a Ca2+/Mg2+-dependent endonuclease ubiquitously expressed in mammalian tissues, has been implicated to mediate internucleosomal DNA degradation in human cells undergoing apoptosis. DNase I is highly polymorphic, and at least six alleles of DNase I are known. DNase II, the ubiquitously expressed acidic deoxyribonuclease, acts downstream of caspase activation and may also induce DNA digestion during apoptosis. DNase I cleaves DNA to 5'-phosphodinucleotide and 5'-phospho- oligonucleotide end-products, whereas DNase II cleaves DNA to 3'-phosphomononucleotide and 3'-phosphooligonucleotide end-products. The mechanism by which DNase II cuts DNA is similar to DNase I, which produces nicks rather than double-strand cuts. DNase II is usually present in cytoplasm of epithelial cells, but it appears concentrated in the nuclei of lens fibers. In contrast, DNase I is always concentrated in nuclei of epithelial and fiber cells.
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Protein Aliases: deoxyribonuclease; Deoxyribonuclease 1; Deoxyribonuclease I; Deoxyribonuclease-1; Deoxyribonuclease1; DeoxyribonucleaseI; DNASE 1; DNase I; DNase I lysosomal; DNase I, lysosomal; DNL 1; Dornase alfa; FLJ38093; human urine deoxyribonuclease I
Gene Aliases: DNASE1; DNL1; DRNI
UniProt ID: (Human) P24855
Entrez Gene ID: (Human) 1773
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