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Functional characte...
Functional characterization of DNase X, a novel endonuclease expressed in muscle cells
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- Los, Marek Jan (författare)
- Department of Immunology and Cell Biology, University of Münster, Münster, and German Cancer Research Center, Division of Molecular Genome Analysis, Heidelberg, Germany
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- Neubuser, D. (författare)
- Department of Immunology and Cell Biology, University of Münster, Münster, and German Cancer Research Center, Division of Molecular Genome Analysis, Heidelberg, Germany
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- Coy, J. F. (författare)
- German Cancer Research Center, Division of Molecular Genome Analysis, Heidelberg, Germany
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- Mozoluk, M. (författare)
- Department of Immunology and Cell Biology, University of Münster, Münster
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- Poustka, A. (författare)
- German Cancer Research Center, Division of Molecular Genome Analysis, Heidelberg, Germany
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- Schulze-Osthoff, Klaus (författare)
- Department of Immunology and Cell Biology, University of Münster, Münster, Germany
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(creator_code:org_t)
- 2000-05-31
- 2000
- Engelska.
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Ingår i: Biochemistry. - : American Chemical Society (ACS). - 0006-2960 .- 1520-4995. ; 39:25, s. 7365-7373
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https://liu.diva-por... (primary) (Raw object)
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http://liu.diva-port...
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https://urn.kb.se/re...
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https://doi.org/10.1...
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Abstract
Ämnesord
Stäng
- The activation of endonucleases resulting in the degradation of genomic DNA is one of the most characteristic changes in apoptosis. Here, we report the characterization of a novel endonuclease, termed DNase X due to its X-chromosomal localization. The active nuclease is a 35 kDa protein with 39% identity to DNase I. When incubated with isolated nuclei, recombinant DNase X was capable of triggering DNA degradation at internucleosomal sites. Similarly to DNase I, the nuclease activity of DNase X was dependent on Ca2+ and Mg2+ and inhibited by Zn2+ ions or chelators of bivalent cations. Overexpression of DNase X caused internucleosomal DNA degradation and induction of cell death associated with increased caspase activation. Despite the presence of two potential caspase cleavage sites, DNase X was processed neither in vitro nor in vivo by different caspases. Interestingly, after initiation of apoptosis DNase X was translocated from the cytoplasm to the nuclear compartment and aggregated as a detergent-insoluble complex. Abundant expression of DNase X mRNA was detected in heart and skeletal muscle cells, suggesting that DNase X may be involved in apoptotic or other biological events in muscle tissues.
Ämnesord
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
Nyckelord
- apoptotic endonuclease
- caspase-activated dnase
- death
- epithelial-cells
- fragmentation
- human deoxyribonuclease-ii
- human xq28
- molecular-cloning
- protein
- rat parotid-gland
Publikations- och innehållstyp
- ref (ämneskategori)
- art (ämneskategori)
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