Ribonucleases as a Novel Pro-Apoptotic Anticancer Strategy: Review of the Preclinical and Clinical Data for Ranpirnase

Costanzi, John J.; Sidransky, David; Navon, Ami; Goldsweig, Howard

doi:10.1080/07357900500283143

Cited by 100 publications

(107 citation statements)

References 47 publications

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“…In addition, blocking TNF-␣ may lead to novel preventive strategies for MM. Examples might include blocking TNF-␣ with etanercept (Enbrel), a recombinant decoy receptor for TNF-␣ that is under investigation in breast cancer patients (44) or disruption of the NF-B pathway, for example with Onconase (Ranpirnase), a drug that inhibits the NF-B pathway (45) and that has already shown favorable effects in some MM patients (46).…”

Section: Discussionmentioning

confidence: 99%

TNF-α inhibits asbestos-induced cytotoxicity via a NF-κB-dependent pathway, a possible mechanism for asbestos-induced oncogenesis

Yang

Bocchetta

Kroczyńska

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

281

248

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Section: Discussionmentioning

confidence: 99%

TNF-α inhibits asbestos-induced cytotoxicity via a NF-κB-dependent pathway, a possible mechanism for asbestos-induced oncogenesis

Yang

Bocchetta

Kroczyńska

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

281

248

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“…We have re-isolated full-length cDNAs of the two chicken leukocyte RNases by reverse transcription-PCR from RNA prepared from the bone marrow of White Leghorn chickens (G. gallus) and have deposited sequences into GenBank TM as chicken leukocyte RNase A-1 (DQ395275) and chicken leukocyte RNase A-2 (DQ395276). These sequences share 93% nucleotide sequence identity to one another and are identical to RNase A/angiogenin (19) and RSFR (20) Rabbit antibodies prepared against divergent peptides shown in Fig. 2A (anti-A-1, NH 2 -QPNRALRTTQQQLP-COOH; anti-A-2, NH 2 -DQALRRTRRHFRIT-COOH) were evaluated for activity and specificity by immunoblotting against recombinant carboxyl-terminal FLAG-tagged recombinant leukocyte RNase A-1 and A-2 (Fig.…”

Section: Rnase a Ribonucleases In The Genome Of The Domesticmentioning

confidence: 99%

“…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).…”

mentioning

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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“…[1][2][3][4][5] The antitumor activity was shown for BS-RNase from bovine seminal, [6][7][8][9] onconase from oocytes of Rana pipiens, [10][11][12] bovine pancreatic RNase A, 13 cSBL and jSBL RNases from Rana catesbeiana and Rana japonica, 14 microbial RNases [15][16][17] and conjugates of RNases with various molecules. [18][19][20] One of the properties that are important for potential therapeutic application of RNases is their ability to induce cancer cell death by apoptosis.…”

Section: Introductionmentioning

confidence: 99%

Ribonuclease binase inhibits primary tumor growth and metastases via apoptosis induction in tumor cells

et al. 2013

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Ribonucleases as a Novel Pro-Apoptotic Anticancer Strategy: Review of the Preclinical and Clinical Data for Ranpirnase

Cited by 100 publications

References 47 publications

TNF-α inhibits asbestos-induced cytotoxicity via a NF-κB-dependent pathway, a possible mechanism for asbestos-induced oncogenesis

TNF-α inhibits asbestos-induced cytotoxicity via a NF-κB-dependent pathway, a possible mechanism for asbestos-induced oncogenesis

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

Ribonuclease binase inhibits primary tumor growth and metastases via apoptosis induction in tumor cells

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