ArticleNucleic acids research2000
Purification and cloning of cytotoxic ribonucleases from Rana catesbeiana (bullfrog).
Article in Nucleic acids research, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 46 citations in OpenAlex.
- Immune Modulation by Human Secreted RNases at the Extracellular Space.Frontiers in immunology · 2018Review
- Article
- Sialic acid-binding lectin (leczyme) induces apoptosis to malignant mesothelioma and exerts synergistic antitumor effects with TRAIL.International journal of oncology · 2014Article
- Leczyme: a new candidate drug for cancer therapy.BioMed research international · 2014Review
- Article
- Sialic acid-binding lectin (leczyme) induces caspase-dependent apoptosis-mediated mitochondrial perturbation in Jurkat cells.International journal of oncology · 2013Article
- Ribonucleases as potential modalities in anticancer therapy.European journal of pharmacology · 2009Review
- Evasion of ribonuclease inhibitor as a determinant of ribonuclease cytotoxicity.Current pharmaceutical biotechnology · 2008Review
- Structural basis for catalysis by onconase.Journal of molecular biology · 2008Article
- Molecular cloning and characterization of the human RNase kappa, an ortholog of Cc RNase.Nucleic acids research · 2007Article
- The RNase a superfamily: generation of diversity and innate host defense.Molecular diversity · 2006Review
- Removal of N-terminal methionine from recombinant proteins by engineered E. coli methionine aminopeptidase.Protein science : a publication of the Protein Society · 2004Article
- The structural integrity exerted by N-terminal pyroglutamate is crucial for the cytotoxicity of frog ribonuclease from Rana pipiens.Nucleic acids research · 2003Article
- Human RNase 7: a new cationic ribonuclease of the RNase A superfamily.Nucleic acids research · 2003Article
- Regulation of ribonuclease expression by estradiol in Rana catesbeiana (Bullfrog).Nucleic acids research · 2002Article
- 1H, 15N and 13C resonance assignments and secondary structure of the liver ribonuclease from bullfrog Rana catesbeiana.Journal of biomolecular NMR · 2001Article
- 1H, 13C and 15N resonance assignments and secondary structure of the cytotoxic protein RNase 4 from bullfrog Rana catesbeiana oocytes.Journal of biomolecular NMR · 2001Article
- 1H, 15N and 13C resonance assignments and secondary structure determination of the RC-RNase 2 from oocytes of bullfrog Rana catesbeiana.Journal of biomolecular NMR · 2001Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ribonucleases with antitumor activity are mainly found in the oocytes and embryos of frogs, but the role of these ribonucleases in frog development is not clear. Moreover, most frog ribonuclease genes have not been cloned and characterized. In the present study, a group of ribonucleases were isolated from Rana catesbeiana (bullfrog). These ribonucleases in mature oocytes, namely RC-RNase, RC-RNase 2, RC-RNase 3, RC-RNase 4, RC-RNase 5 and RC-RNase 6, as well as liver-specific ribonuclease RC-RNase L1, were purified by column chromatographs and detected by zymogram assay and western blotting. Characterization of these purified ribonucleases revealed that they were highly conserved in amino acid sequence and had a pyroglutamate residue at their N-termini, but possessed different specific activities, base specificities and optimal pH values for their activities. These ribonucleases were cytotoxic to cervical carcinoma HeLa cells, but their cytotoxicities were not closely correlated to their enzymatic specific activities. Some other amino acid residues in addition to their catalytic residues were implicated to be involved in the cytotoxicity of the frog ribonucleases to tumor cells. Because the coding regions lack introns, the ribonuclease genes were cloned by PCR using genomic DNA as template. Their DNA sequences and amino acid sequences are homologous to those of mammalian ribonuclease superfamily, approximately 50 and approximately 25%, respectively.
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