Purification and cloning of cytotoxic ribonucleases from Rana catesbeiana (bullfrog)

Liao, You‐Di; Huang, Huey-Chung; Leu, Yin-Jen; Wei, Chyou-Wei; Tang, Pin‐Chi; Wang, Sui-Chi

doi:10.1093/nar/28.21.4097

Cited by 44 publications

(64 citation statements)

References 31 publications

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“…The novel sequences are those of the 200 series: rc-203, rc-204, rc-208, rc-212, and rc-218. Several of these sequences were also identified by PCR amplification but not reported in the studies performed by Liao et al (2000). The amino terminal "Q" of these novel sequences has been inferred based on similarity to the amino acid sequence of rc-RNase (rc-RN), whose terminus was determined directly via protein sequencing (Titani et al 1987); the 22 amino acid signal sequences encoded by the full length cDNAs are not shown.…”

Section: Identification Of Novel Ribonucleasementioning

confidence: 99%

“…Liao et al (Huang et al 1998) were the first to isolate a cDNA encoding a Rana ribonuclease (rc-RNase), and found mRNA expression in the liver rather than in oocytes where the protein is ultimately localized. Most recently, Liao et al (2000) reported five novel cDNA sequences encoding R. catesbeiana ribonucleases (rc-01 encoding rc-L1, and rc-02, rc-03, rc-04, and rc-06) found in oocyte yolk granule extracts and liver and Chen et al (2000) described a gender-specific cytotoxic ribonuclease (rp-rap) from R. pipiens.…”

Section: Introductionmentioning

confidence: 99%

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Rapid Diversification of RNase A Superfamily Ribonucleases from the Bullfrog, Rana catesbeiana

et al. 2001

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Abstract. We present sequences of five novel RNase A superfamily ribonuclease genes of the bullfrog, Rana catesbeiana. All five genes encode ribonucleases that are similar to Onconase, a cytotoxic ribonuclease isolated from oocytes of R. pipiens. With amino acid sequence data from 14 ribonucleases from three Rana species (R. catesbeiana, R. japonica, and R. pipiens), we have constructed bootstrap-supported phylogenetic trees that reorganize these ribonucleases into five distinct lineagesthe pancreatic ribonucleases (RNases 1), the eosinophilassociated ribonucleases (RNases 2, 3, and 6), the ribonucleases 4, the angiogenins (RNases 5) and the Rana ribonucleases-with the Rana ribonucleases no more closely related to the angiogenins than they are to any of the other ribonuclease lineages shown. Further phylogenetic analysis suggests the division of the Rana ribonucleases into two subclusters (A and B), with positive (Darwinian) selection (d N /d S > 1.0) and an elevated rate of radical nonsynonymous substitution (d R ) contributing to the rapid diversification of ribonucleases within each cluster. This pattern of evolution-rapid diversification via positive selection among sequences of a multigene cluster-bears striking resemblance to what we have described for the eosinophil-associated ribonuclease genes of the rodent Mus musculus, a finding that may have implications with respect the physiologic function of this unique family of proteins.

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Section: Identification Of Novel Ribonucleasementioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Rapid Diversification of RNase A Superfamily Ribonucleases from the Bullfrog, Rana catesbeiana

et al. 2001

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“…Several RNase A ribonucleases of the frog genus Rana have been isolated (15)(16)(17)(18), including the cancer biotherapeutic agent, onconase (19). Also characterized are several RNase A ribonucleases from birds (14, 20 -22) and reptiles (23)(24)(25).…”

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confidence: 99%

Evolution and Function of Leukocyte RNase A Ribonucleases of the Avian Species, Gallus gallus

Nitto

Dyer

Czapiga

et al. 2006

Journal of Biological Chemistry

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In this study, we explore the evolution and function of two closely related RNase A ribonucleases from the chicken, Gallus gallus. Separated by ϳ10 kb on chromosome 6, the coding sequences of RNases A-1 and A-2 are diverging under positive selection pressure (d N > d S ) but remain similar to one another (81% amino acid identity) and to the mammalian angiogenins. Immunoreactive RNases A-1 and A-2 (both ϳ16 kDa) were detected in peripheral blood granulocytes and bone marrow. Recombinant proteins are ribonucleolytically active (k cat ‫؍‬ 2.6 and 0.056 s ؊1 , respectively), and surprisingly, both interact with human placental ribonuclease inhibitor. RNase A-2, the more cationic (pI 11.0), is both angiogenic and bactericidal; RNase A-1 (pI 10.2) has neither activity. We demonstrated via point mutation of the catalytic His 110 that ablation of ribonuclease activity has no impact on the bactericidal activity of RNase A-2. We determined that the divergent domains II (amino acids 71-76) and III (amino acids 89 -104) of RNase A-2 are both important for bactericidal activity. Furthermore, we demonstrated that these cationic domains can function as independent bactericidal peptides without the tertiary structure imposed by the RNase A backbone. These results suggest that ribonucleolytic activity may not be a crucial constraint limiting the ongoing evolution of this gene family and that the ribonuclease backbone may be merely serving as a scaffold to support the evolution of novel, nonribonucleolytic proteins.The RNase A ribonuclease gene family has been a tremendous source of information on unusual evolutionary constraints and their effects on protein structure and function at the molecular level. Although RNase A ribonucleases maintain invariant disulfide bonds and catalytic components that are necessary for RNA degradation, other regions have diverged dramatically. RNase A ribonucleases have been implicated in a wide variety of physiologic functions and have been observed to promote angiogenesis, cellular apoptosis, and anti-tumor and anti-pathogen host defense via a complex array of seemingly unrelated molecular mechanisms (reviewed in Refs. 1-8).The specific patterns of diversification are best understood among the RNase A ribonucleases of mammalian species. Four major RNase A lineages have been described in mammals (6) as follows: the pancreatic RNases, or RNases 1, which include the prototype, bovine pancreatic RNase A; a second group, including the eosinophil ribonucleases EDN (RNases 2), ECP (RNases 3), and RNases 6, 7, and 8; a third group that includes the RNases 4; and a final group that includes the angiogenins (RNases 5). There are also several genes, such as RNases 9 -13 in the human genome, that are distantly related to the RNase A family based on amino acid sequence homology but that are missing one or more elements necessary for enzymatic activity (9 -13). Interestingly, not all RNase A lineages are found in every mammalian species, and there are some recently described mammalian RNase A ribonucleases that...

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“…(10,11,16,17). Notably, it has been revealed that RC-RNase is not cytotoxic to normal cells (10,15). However, the ability of RC-RNase to inhibit glioblastoma cell growth is not clear.…”

Section: Statistical Analysis Student's T-testmentioning

confidence: 99%

“…RC-RNase and Onconase have been revealed to demonstrate antitumor activity (10)(11)(12)(13). Previous studies have reported that RC-RNase is able to exert cytotoxic effects in various tumor cells, including cervical cancer, leukemia, hepatoma and breast cancer cells (11,(14)(15)(16). In addition, numerous studies have indicated that RC-RNase is able to trigger distinct cell death mechanisms in various tumor cell types (10,11,14,17).…”

Section: Introductionmentioning

confidence: 99%

Rana catesbeiana ribonuclease induces cell apoptosis via the caspase-9/-3 signaling pathway in human glioblastoma DBTRG, GBM8901 and GBM8401 cell lines

Chen¹,

Yiang²,

Lin³

et al. 2015

Oncology Letters

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Abstract. Human glioblastoma multiforme is one of the most aggressive malignant brain tumor types, and the mean survival time of patients with a brain tumor is <2 years when traditional therapies are administered. Thus, numerous studies have focused on the development of novel treatments for brain tumors. Frog ribonucleases, such as Onconase and Rana catesbeiana ribonuclease (RC-RNase), exert antitumor effects on various tumor cells, including cervical cancer, breast cancer, hepatoma, leukemia, pancreatic cancer and prostate cancer cells. In addition, frog Onconase has been applied as a treatment in clinical trials. However, the antitumor effects of frog ribonucleases on brain tumors are unclear. Previous studies have indicated that RC-RNase demonstrates a decreased cytotoxic effect in normal cells compared with Onconase. Therefore, the present study investigated the ability of RC-RNase to exert antitumor activities on human glioblastoma.It was found that RC-RNase inhibits the growth of the human glioblastoma DBTRG, GBM8901 and GBM8401 cells. In addition, the present study revealed that RC-RNase induces caspase-9/-3 activity and triggers the apoptotic cell death pathway in human glioblastoma cells. Notably, it was also demonstrated that RC-RNase effectively inhibits the growth of human glioblastoma tumors in a nude mouse model. Overall, the present study indicates that RC-RNase may be a potential agent for the treatment of human glioblastoma.

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Purification and cloning of cytotoxic ribonucleases from Rana catesbeiana (bullfrog)

Cited by 44 publications

References 31 publications

Rapid Diversification of RNase A Superfamily Ribonucleases from the Bullfrog, Rana catesbeiana

Rapid Diversification of RNase A Superfamily Ribonucleases from the Bullfrog, Rana catesbeiana

Evolution and Function of Leukocyte RNase A Ribonucleases of the Avian Species, Gallus gallus

Rana catesbeiana ribonuclease induces cell apoptosis via the caspase-9/-3 signaling pathway in human glioblastoma DBTRG, GBM8901 and GBM8401 cell lines

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