The dual role of ribonucleases in tumor-host relationship
DOI:
https://doi.org/10.32471/exp-oncology.2312-8852.vol-41-no-3.13456Keywords:
ribonuclease, RNA, RNase inhibitors, tumor growth, tumor treatmentAbstract
Summary. Ribonucleases are enzymes that destroy RNA, play an important role in protein synthesis, epigenetic regulation of genetic activity, cell proliferation and apoptosis. Ribonucleases are important antimicrobial, antiviral and immune defense factors. Despite the same biochemical properties, they exhibit unequal, sometimes opposite biological effects. While mostly ribonucleases inhibit cell proliferation, induce apoptosis and inhibit the growth of tumors, some ribonucleases stimulate vascular growth, proliferation and tumor development. RNase inhibitors have an opposite effect. The correct use of these features of RNases can provide additional opportunities for the development of a strategy of targeted influence on tumor growth.
References
Sorrentino S. The eight human “canonical” ribonucleases: molecular diversity, catalytic properties, and special biological actions of the enzyme proteins. FEBS Lett 2010; 584: 2194–200.
Koczera P, Martin L, Marx G, et al. The ribonuclease a superfamily in humans: canonical RNases as the buttress of innate immunity. Int J Mol Sci 2016; 17: 1278.
Jain C. Novel role for RNase PH in the degradation of structured RNA. J Bacteriol 2012; 194: 3883–90.
Marcaida MJ, DePristo MA, Chandran V, et al. The RNA degradosome: life in the fast lane of adaptive molecular evolution. Trends Biochem Sci 2006; 31: 359–65.
Halicka HD, Ardelt B, Shogen K, et al. Mild hyperthermia predisposes tumor cells to undergo apoptosis upon treatment with onconase. Int J Oncol 2007; 30: 841–7.
Matoušek J, Matoušek J. Plant ribonucleases and nucleases as antiproliferative agens targeting human tumors growing in mice. Recent Pat DNA Gene Seq 2010; 4: 29–39.
Huang W, Zhao M, Wei N, et al. Site-specific RNase A activity was dramatically reduced in serum from multiple types of cancer patients. PLoS One 2014; 9: e96490.
Spalletti-Cernia D, Sorrentino R, Di Gaetano S, et al. Antineoplastic ribonucleases selectively kill thyroid carcinoma cells via caspase-mediated induction of apoptosis. J Clin Endocrinol Metab 2003; 88: 2900–907.
Ardelt W, Ardelt B, Darzynkiewicz Z. Ribonucleases as potential modalities in anticancer therapy. Eur J Pharmacol 2009; 625: 181–9.
Fang EF, Ng TB. Ribonucleases of different origins with a wide spectrum of medicinal applications. Biochim Biophys Acta 2011; 1815: 65–74.
Lee JE, Raines RT. Ribonucleases as novel chemotherapeutics: The ranpirnase example. BioDrugs 2008; 22: 53–8.
Mitkevich VA, Ilinskaya ON, Makarov AA. Antitumor RNases: killer’s secrets. Cell Cycle 2015; 14: 931–2.
Grossman D, Van Hoof A. RNase II structure completes group portrait of 3′ exoribonucleases. Nat Struct Mol Biol 2006; 13: 760–1.
Paushkin SV, Patel M, Furia BS, et al. Identification of a human endonuclease complex reveals a link between tRNA splicing and pre-mRNA 3′ end formation. Cell 2004; 117: 311–21.
Shruti G, Sukhdev S, Singh KS. An Overview on ribonucleases and their therapeutic effects. Insight 2016; 1: 1–11.
Erbe W, Preiss J, Seifert R, et al. Increase in RNase and DPNase activities in ascites tumor cells induced by various cytostatic agents. Biochem Biophys Res Commun 1966; 23: 392–7.
Gotte G, Helmy AM, Ercole C et al. Double domain swapping in bovine seminal RNase: formation of distinct N-and C-swapped tetramers and multimers with increasing biological activities. PLoS One 2012; 7: e46804.
Giancola C, Ercole C, Fotticchia I et al. Structure-cytotoxicity relationships in bovine seminal ribonuclease: New insights from heat and chemical denaturation studies on variants. FEBS J 2011; 278: 111–22.
Kotchetkov R, Cinatl J, Krivtchik AA, et al. Selective activity of BS-RNase against anaplastic thyroid cancer. Anticancer Res 2001; 21: 1035–42.
Spadaccini R, Ercole C, Gentile MA, et al. NMR studies on structure and dynamics of the monomeric derivative of BS-RNase: new insights for 3D domain swapping. PLoS One 2012; 7: e29076.
Futami J, Yamada H. Design of cytotoxic ribonucleases by cationization to enhance intracellular protein delivery. Current Pharm Biotechnol 2008; 9: 180–4.
Turcotte RF, Lavis LD, Raines RT. Onconase cytotoxicity relies on the distribution of its positive charge. FEBS J 2009; 276: 4270–81.
Ye XY, Ng TB. A novel and potent ribonuclease from fruiting bodies of the mushroom Pleurotus pulmonarius. Biochem Biophys Res Commun 2002; 293: 857–61.
Majchrzak A, Witkowska M, Medra A, et al. In vitro cytotoxicity of ranpirnase (onconase) in combination with components of R-CHOP regimen against diffuse large B cell lymphoma (DLBCL) cell line. Postepy Hig Med Dosw (Online) 2013; 67: 1166–72.
Wang X, Guo Z. Chlorotoxin-conjugated onconase as a potential anti-glioma drug. Oncol Lett 2015; 9: 1337–42.
Altomare DA, Rybak SM, Pei J, et al. Onconase responsive genes in human mesothelioma cells: implications for an RNA damaging therapeutic agent. BMC Cancer 2010; 10: 34.
Zwolinska M, Smolewski P. Onkonaza-rybonukleaza o aktywnosci przeciwnowotworowej. Onconase: a ribonuclease with antitumor activity. Postepy Hig Med Dosw (Online) 2010; 64: 58–66 (in Polish).
Qiao M, Zu L-D, He X-H, et al. Onconase downregulates microRNA expression through targeting microRNA precursors. Cell Res 2012; 22: 1199–202.
Squiquera L, Taxman DJ, Brendle SA, et al. Ranpirnase eradicates human papillomavirus in cultured cells and heals anogenital warts in a Phase I study. Antivir Ther 2017; 22: 247–55.
Garipov AR, Nesmelov AA, Cabrera-Fuentes HA, et al. Bacillus intermedius ribonuclease (BINASE) induces apoptosis in human ovarian cancer cells. Toxicon 2014; 92: 54–9.
Mahmud RS, Ilinskaya ON. Antiviral activity of binase against the pandemic influenza A (H1N1) virus. Acta Naturae 2013; 5: 44.
Luhtala N, Parker R. T2 Family ribonucleases: ancient enzymes with diverse roles. Trends Biochem Sci 2010; 35: 25359.
Zhang R, Zhao L, Wang H, Ng TB. A novel ribonuclease with antiproliferative activity toward leukemia and lymphoma cells and HIV-1 reverse transcriptase inhibitory activity from the mushroom, Hohenbuehelia serotina. Int J Mol Med 2014; 33: 209–14.
Sun M, Sun L, Sun D, Zhang C, Li M. Targeted delivery of immuno-RNase may improve cancer therapy. Cancer Cell Int 2018; 18: 58.
Vlassov V V, Zuber G, Felden B, Behr J-P, Giegè R. Cleavage of tRNA with imidazole and spermine imidazole constructs: a new approach for probing RNA structure. Nucleic Acids Res 1995; 23: 3161–7.
Haigis MC, Kurten EL, Raines RT. Ribonuclease inhibitor as an intracellular sentry. Nucleic Acids Res 2003; 31: 1024–32.
Libonati M, Gotte G. Oligomerization of bovine ribonuclease A: structural and functional features of its multimers. Biochem J 2004; 380: 311–27.
Sheng J, Xu Z. Three decades of research on angiogenin: a review and perspective. Acta Biochim Biophys Sin 2015; 48: 399–410.
Yamasaki S, Ivanov P, Hu G-F, et al. Angiogenin cleaves tRNA and promotes stress-induced translational repression. J Cell Biol 2009; 185: 35–42.
Fu H, Feng J, Liu Q, et al. Stress induces tRNA cleavage by angiogenin in mammalian cells. FEBS Lett 2009; 583: 437–42.
Pizzo E, Sarcinelli C, Sheng J, et al. Ribonuclease/angiogenin inhibitor 1 regulates stress-induced subcellular localization of angiogenin to control growth and survival. J Cell Sci 2013; 126: 4308–19.
Yoshioka N, Wang L, Kishimoto K, et al. A therapeutic target for prostate cancer based on angiogenin-stimulated angiogenesis and cancer cell proliferation. Proc Natl Acad Sci USA 2006; 103: 14519–24.
Ibaragi S, Yoshioka N, Kishikawa H, et al. Angiogenin-stimulated rRNA transcription is essential for initiation and survival of AKT-induced prostate intraepithelial neoplasia. Mol Cancer Res 2009; 7: 415–24.
Polakowski IJ, Lewis MK, Muthukkaruppan VR, et al. A ribonuclease inhibitor expresses anti-angiogenic properties and leads to reduced tumor growth in mice. Am J Pathol 1993; 143: 507–17.
Polakowski IJ, Lewis K, Auerbach R. A protein RNase inhibitor (RNasin) expresses anti-angiogenic properties in mice. In: Steiner R, Weisz PB, Langer R, eds. Angiogenesis. Basel: Birkhäuser, 1992: Experientia Supplementum, 61.
Zhang L-N, Yan Y-B. Depletion of poly (A)-specific ribonuclease (PARN) inhibits proliferation of human gastric cancer cells by blocking cell cycle progression. Biochim Biophys Acta 2015; 1853: 522–34.
Balatsos N, Maragozidis P, Anastasakis D, et al. Modulation of poly (A)-specific ribonuclease (PARN): current knowledge and perspectives. Curr Med Chem 2012; 19: 4838–49.
Domachowske JB, Dyer KD, Adams AG, et al. Eosinophil cationic protein/RNase 3 is another RNase A-family ribonuclease with direct antiviral activity. Nucleic Acids Res 1998; 26: 3358–63.
Dyer KD, Rosenberg HF. The RNase a superfamily: Generation of diversity and innate host defense. Mol Divers 2006; 10: 585–97.
Lawal A, Jejelowo O, Chopra AK, et al. Ribonucleases and bacterial virulence. Microb Biotechnol 2011; 4: 558–71.
Rosenberg HF. RNase A ribonucleases and host defense: An evolving story. J Leukocyte Biol 2008; 83: 1079–87.
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