Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
Review
. 2020 Jul 11;10(7):1036.
doi: 10.3390/biom10071036.

Deoxyribonucleases and Their Applications in Biomedicine

Lucia Lauková  1 , Barbora Konečná  2 , Ľubica Janovičová  2 , Barbora Vlková  2 , Peter Celec  2   3   4
Affiliations
Review

Deoxyribonucleases and Their Applications in Biomedicine

Lucia Lauková et al. Biomolecules. .

Abstract

Extracellular DNA, also called cell-free DNA, released from dying cells or activated immune cells can be recognized by the immune system as a danger signal causing or enhancing inflammation. The cleavage of extracellular DNA is crucial for limiting the inflammatory response and maintaining homeostasis. Deoxyribonucleases (DNases) as enzymes that degrade DNA are hypothesized to play a key role in this process as a determinant of the variable concentration of extracellular DNA. DNases are divided into two families-DNase I and DNase II, according to their biochemical and biological properties as well as the tissue-specific production. Studies have shown that low DNase activity is both, a biomarker and a pathogenic factor in systemic lupus erythematosus. Interventional experiments proved that administration of exogenous DNase has beneficial effects in inflammatory diseases. Recombinant human DNase reduces mucus viscosity in lungs and is used for the treatment of patients with cystic fibrosis. This review summarizes the currently available published data about DNases, their activity as a potential biomarker and methods used for their assessment. An overview of the experiments with systemic administration of DNase is also included. Whether low-plasma DNase activity is involved in the etiopathogenesis of diseases remains unknown and needs to be elucidated.

Keywords: DAMPs; DNA fragmentation; inflammation; nuclease activity; toll-like receptor.

PubMed Disclaimer

Conflict of interest statement

The authors confirm that there are no conflicts of interest.

Figures

Figure 1
Figure 1
Classification of deoxyribonucleases (DNases) to two families. DNase I family includes four types of DNases: DNase I, DNase1L1, DNase1L2 and DNase1L3. DNase II family includes three types of DNases: DNase II (α), DNase II β and L-DNase II.
Figure 2
Figure 2
Cleavage of DNA by deoxyribonuclease I (DNase I) and deoxyribonuclease II (DNase II). DNase I cleaves DNA to form two oligonucleotide-end products with 5′-phospho and 3′-hydroxy ends, while DNase II cleaves DNA to form two oligonucleotide-end products with 5′-hydroxy and 3′-phospho ends.
Figure 3
Figure 3
Deoxyribonuclease (DNase) activity measured using the single radial enzyme diffusion (SRED) method in Kunitz units (K.u.). Plasma samples were analyzed using a gel containing DNA after overnight incubation at 37 °C in the dark. The area of the circles represents DNA in the gel cleaved by DNase in the plasma samples. Dilutions of DNase were used as a calibrator.
See this image and copyright information in PMC

Similar articles

See all similar articles

Cited by

See all "Cited by" articles

References

    1. Mandel P., Metais P. Les acides nucléiques du plasma sanguin chez l’homme. C. R. Seances Soc. Biol. Fil. 1948;142:241–243. - PubMed
    1. Magna M., Pisetsky D.S. The Alarmin Properties of DNA and DNA-associated Nuclear Proteins. Clin. Ther. 2016;38:1029–1041. doi: 10.1016/j.clinthera.2016.02.029. - DOI - PubMed
    1. Han D.S.C., Ni M., Chan R.W.Y., Chan V.W.H., Lui K.O., Chiu R.W.K., Lo Y.M.D. The Biology of Cell-free DNA Fragmentation and the Roles of DNASE1, DNASE1L3, and DFFB. Am. J. Hum. Genet. 2020;106:202–214. doi: 10.1016/j.ajhg.2020.01.008. - DOI - PMC - PubMed
    1. Shpak M., Kugelman J.R., Varela-Ramirez A., Aguilera R.J. The phylogeny and evolution of deoxyribonuclease II: An enzyme essential for lysosomal DNA degradation. Mol. Phylogenet. Evol. 2008;47:841–854. doi: 10.1016/j.ympev.2007.11.033. - DOI - PMC - PubMed
    1. Junowicz E., Spencer J.H. Studies on bovine pancreatic deoxyribonuclease A. II. The effect of different bivalent metals on the specificity of degradation of DNA. Biochim. Biophys. Acta. 1973;312:85–102. doi: 10.1016/0005-2787(73)90054-3. - DOI - PubMed

Publication types

MeSH terms

LinkOut - more resources