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
. 2016 Aug 5;17(8):1278.
doi: 10.3390/ijms17081278.

The Ribonuclease A Superfamily in Humans: Canonical RNases as the Buttress of Innate Immunity

Affiliations
Review

The Ribonuclease A Superfamily in Humans: Canonical RNases as the Buttress of Innate Immunity

Patrick Koczera et al. Int J Mol Sci. .

Abstract

In humans, the ribonuclease A (RNase A) superfamily contains eight different members that have RNase activities, and all of these members are encoded on chromosome 14. The proteins are secreted by a large variety of different tissues and cells; however, a comprehensive understanding of these proteins' physiological roles is lacking. Different biological effects can be attributed to each protein, including antiviral, antibacterial and antifungal activities as well as cytotoxic effects against host cells and parasites. Different immunomodulatory effects have also been demonstrated. This review summarizes the available data on the human RNase A superfamily and illustrates the significant role of the eight canonical RNases in inflammation and the host defence system against infections.

Keywords: antimicrobial activity; canonical RNases; host defence protein; human RNases; secreted RNases.

PubMed Disclaimer

Figures

Figure 1
Figure 1
Ribonuclease (RNase) 1 is required for vascular homeostasis. (A) Endothelial cells (ECs) are the main source of large amounts of RNase 1; (B) Due to the ribonuclease activity of single- and double-stranded RNA as well as DNA-RNA hybrids, RNase 1 serves as a potent RNA scavenger for the normalization of serum viscosity and the clearance of perivascular polynucleotides; RNase 1 (C) shows antiviral activity against HIV and (D) is able to stimulate and induce maturation of dendritic cells (DCs). TNFα: Tumour necrosis factor alpha; IL: Interleukin; HIV: Human immunodeficiency virus; RNA: Ribonucleic acid.
Figure 2
Figure 2
Effects of the eosinophil cationic protein (ECP). (A) ECP is stored in the secondary granules of eosinophils and can be released upon eosinophil simulation; (B) ECP can induce degranulation of mast cells; (C) ECP has broad antimicrobial activity, including inhibition of viruses, Gram-positive and Gram-negative bacteria and fungal and helminthic pathogens; (D) dose-dependent cytotoxic effects have been described for ECP, including necrosis and apoptosis.
Figure 3
Figure 3
A schematic overview of the human canonical ribonucleases (RNases) in the host defence system. (A,B) RNases show antiviral activity and cytotoxic properties in mammalian cells and degrade RNA; (C) Cells of the immune system (immune cells, or ICs) secrete and are modulated by RNases; (D,F) Different mature cells secrete RNases, including endothelial (EnC) and epithelial (EpC) cells, for pericellular homeostasis; (E) Antimicrobial activity against bacteria, fungi and parasites has been demonstrated for RNases. RNA: Ribonucleic acid; HIV: Human immunodeficiency virus.

References

    1. Beintema J.J., Kleinedam R.G. The ribonuclease A superfamily: General discussion. Cell. Mol. Life Sci. 1998;54:825–832. doi: 10.1007/s000180050211. - DOI - PMC - PubMed
    1. Sorrentino S. The eight human “canonical” ribonucleases: Molecular diversity, catalytic properties, and special biological actions of the enzyme proteins. FEBS Lett. 2010;584:2194–2200. doi: 10.1016/j.febslet.2010.04.018. - DOI - PubMed
    1. Luhtala N., Parker R. T2 Family ribonucleases: Ancient enzymes with diverse roles. Trends Biochem. Sci. 2010;35:253–259. doi: 10.1016/j.tibs.2010.02.002. - DOI - PMC - PubMed
    1. Lander E.S., Linton L.M., Birren B., Nusbaum C., Zody M.C., Baldwin J., Devon K., Dewar K., Doyle M., FitzHugh W., et al. Initial sequencing and analysis of the human genome. Nature. 2001;409:860–921. doi: 10.1038/35057062. - DOI - PubMed
    1. Torrent M., Pulido D., Valle J., Nogués M.V., Andreu D., Boix E. Ribonucleases as a host-defence family: Evidence of evolutionarily conserved antimicrobial activity at the N-terminus. Biochem. J. 2013;456:99–108. doi: 10.1042/BJ20130123. - DOI - PubMed

Substances