A Novel Cationic Ribonuclease with Antimicrobial Activity from Rana dybowskii

Tao, Fengyun; Fan, Meiyin; Wang, Zhao; Lin, Qiang; Ma, Rong

doi:10.1007/s10528-010-9414-4

Cited by 7 publications

(6 citation statements)

References 44 publications

(59 reference statements)

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“…Frog RNases are secreted by oocytes and early embryos and might protect the eggs against infection ( 237 – 241 ). The observed anti-proliferative properties of the RNases from early vertebrates have attracted the interest of pharmaceutical companies since their discovery ( 242 , 243 ).…”

Section: The Rnase a Superfamilymentioning

confidence: 99%

Immune Modulation by Human Secreted RNases at the Extracellular Space

et al. 2018

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The ribonuclease A superfamily is a vertebrate-specific family of proteins that encompasses eight functional members in humans. The proteins are secreted by diverse innate immune cells, from blood cells to epithelial cells and their levels in our body fluids correlate with infection and inflammation processes. Recent studies ascribe a prominent role to secretory RNases in the extracellular space. Extracellular RNases endowed with immuno-modulatory and antimicrobial properties can participate in a wide variety of host defense tasks, from performing cellular housekeeping to maintaining body fluid sterility. Their expression and secretion are induced in response to a variety of injury stimuli. The secreted proteins can target damaged cells and facilitate their removal from the focus of infection or inflammation. Following tissue damage, RNases can participate in clearing RNA from cellular debris or work as signaling molecules to regulate the host response and contribute to tissue remodeling and repair. We provide here an overall perspective on the current knowledge of human RNases’ biological properties and their role in health and disease. The review also includes a brief description of other vertebrate family members and unrelated extracellular RNases that share common mechanisms of action. A better knowledge of RNase mechanism of actions and an understanding of their physiological roles should facilitate the development of novel therapeutics.

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Section: The Rnase a Superfamilymentioning

confidence: 99%

Immune Modulation by Human Secreted RNases at the Extracellular Space

et al. 2018

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“…For example, the mouse ( Mus musculus ) has more than 20 (Rosenberg et al 2001; Nitto et al 2005, 2006; Pizzo et al 2006, 2008, 2011; Cho and Zhang 2007; Tao et al 2011). Using the RNases identified in the six mammalian genomes, including human, mouse, rat, cow, dog, and opossum, Cho and Zhang (2006) previously determined that the expansion of the RNase A superfamily occurred in the common ancestor of these six mammals before the divergence of the marsupial and the placental mammals (∼190 Ma).…”

Section: Introductionmentioning

confidence: 99%

The Expansion and Functional Diversification of the Mammalian Ribonuclease A Superfamily Epitomizes the Efficiency of Multigene Families at Generating Biological Novelty

Goo

Cho

2013

Genome Biology and Evolution

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The ribonuclease (RNase) A superfamily is a vertebrate-specific gene family. Because of a massive expansion that occurred during the early mammalian evolution, extant mammals in general have much more RNase genes than nonmammalian vertebrates. Mammalian RNases have been associated with diverse physiological functions including digestion, cytotoxicity, angiogenesis, male reproduction, and host defense. However, it is still uncertain when their expansion occurred and how a wide array of functions arose during their evolution. To answer these questions, we generate a compendium of all RNase genes identified in 20 complete mammalian genomes including the platypus, Ornithorhynchus anatinus. Using this, we delineate 13 ancient RNase gene lineages that arose before the divergence between the monotreme and the other mammals (∼220 Ma). These 13 ancient gene lineages are differentially retained in the 20 mammals, and the rate of protein sequence evolution is highly variable among them, which suggest that they have undergone extensive functional diversification. In addition, we identify 22 episodes of recent expansion of RNase genes, many of which have signatures of adaptive functional differentiation. Exemplifying this, bursts of gene duplication occurred for the RNase1, RNase4, and RNase5 genes of the little brown bat (Myotis lucifugus), which might have contributed to the species’ effective defense against heavier pathogen loads caused by its communal roosting behavior. Our study illustrates how host-defense systems can generate new functions efficiently by employing a multigene family, which is crucial for a host organism to adapt to its ever-changing pathogen environment.

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“…Moreover, ONC was found to be capable of fighting viral infections . Other amphibian RNase A homologues such as amphinase (from R. pipiens ) and RNases from bullfrog ( R. catesbeiana , RC‐RNases) , Japanese brown frog ( R. japonica ) or Dybowski's frog ( R. dybowskii ) have also been found to be cytotoxic.…”

Section: On the Cytotoxicity Of The Rnase A Homologues – A Brief Retrmentioning

confidence: 99%

“…In fact, they comprise the only enzyme family unique to vertebrates’ . The members of the RNase A superfamily are small, monomeric proteins ranging from 103 amino acid residues for ‘ Rana dybowskii onconase’ , 104 for ONC and 124 for RNase A to 134 amino acid residues for RNase 2 (eosinophil‐derived neurotoxin) (Figs ) . (A protein, which was denoted as ‘Train A’ and consists of 189 amino acid residues, shows some sequence homology to RNase A in its C‐terminal region, but lacks the highly conserved CKXXNTF and catalytic triad H–K–H motifs .)…”

Section: The Rnase a Superfamily – General Structural Featuresmentioning

confidence: 99%

Stability and folding of amphibian ribonuclease A superfamily members in comparison with mammalian homologues

Arnold

2014

The FEBS Journal

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Comparative studies on homologous proteins can provide knowledge on how limited changes in the primary structure find their expression in large effects on catalytic activity, stability or the folding behavior. For more than half a century, members of the ribonuclease A superfamily have been the subject of a myriad of studies on protein folding and stability. Both the unfolding and refolding kinetics as well as the structure of several folding intermediates of ribonuclease A have been characterized in detail. Moreover, the RNA-degrading activity of these enzymes provides a basis for their cytotoxicity, which renders them potential tumor therapeutics. Because amphibian ribonuclease A homologues evade the human ribonuclease inhibitor, they emerged as particularly promising candidates. Interestingly, the amphibian ribonuclease A homologues investigated to date are more stable than the mammalian homologues. Nevertheless, despite the generation of numerous genetically engineered variants, knowledge of the folding of amphibian ribonuclease A homologues remains rather limited. An exception is onconase, a ribonuclease A homologue from Rana pipiens, which has been characterized in detail. This review summarizes the data on the unfolding and refolding kinetics and pathways, as well on the stability of amphibian ribonuclease A homologues compared with those of ribonuclease A, the best known member of this superfamily.

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A Novel Cationic Ribonuclease with Antimicrobial Activity from Rana dybowskii

Cited by 7 publications

References 44 publications

Immune Modulation by Human Secreted RNases at the Extracellular Space

Immune Modulation by Human Secreted RNases at the Extracellular Space

The Expansion and Functional Diversification of the Mammalian Ribonuclease A Superfamily Epitomizes the Efficiency of Multigene Families at Generating Biological Novelty

Stability and folding of amphibian ribonuclease A superfamily members in comparison with mammalian homologues

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