Advanced search
Publication Cover
Expert Opinion on Biological Therapy Volume 9, 2009 - Issue 1
Submit an article Journal homepage
492
Views
47
CrossRef citations to date
0
Altmetric
Reviews

Targeted therapeutic RNases (ImmunoRNases)

Thomas Schirrmann Technische Universität Braunschweig, Spielmannstr 7, 38106 Braunschweig, Germany +49 531 391 5760; +49 531 391 5763; [email protected]
, PhD,
Jürgen Krauss National Center for Tumor Diseases (NCT) Heidelberg, Medical Oncology, Im Neuenheimer Feld 350, 69120 Heidelberg, Germany
, MD PhD,
Michaela AE Arndt National Center for Tumor Diseases (NCT) Heidelberg, Medical Oncology, Im Neuenheimer Feld 410, 69120 Heidelberg, Germany
, PhD,
Susanna M Rybak Bionanomics, LLC, 411 Walnut Street, Green Cove Springs, FL 32043, USA
, PhD &
Stefan Dübel Technische Universität Braunschweig, Spielmannstr 7, 38106 Braunschweig, Germany +49 531 391 5760; +49 531 391 5763; [email protected]
, PhD
Pages 79-95 | Published online: 08 Dec 2008

Bibliography

  • Mathe G, Loc TB, Bernard H. Effet sur la leucemie L1201 de la souris d'une combinaison par diszotation d'A-methopterine et de gamma-globulines de hamsters porteur de cette leucemie par hereogreffe. C R 1958;246:1626-8
  • Köhler G, Milstein C. Continuous cultures of fused cells secreting antibody of predefined specificity. Nature 1975;256(5517):495-7
  • Handbook of Therapeutic Antibodies. Dübel S, editor, Wiley-VCH, Weinheim; 2007
  • Wu AM, Senter PD. Arming antibodies: prospects and challenges for immunoconjugates. Nat Biotechnol 2005;23(9):1137-46
  • Lambert JM. Drug-conjugated monoclonal antibodies for the treatment of cancer. Curr Opin Pharmacol 2005;5(5):543-9
  • Hamann PR, Hinman LM, Hollander I, et al. Gemtuzumab ozogamicin, a potent and selective anti-CD33 antibody-calicheamicin conjugate for treatment of acute myeloid leukemia. Bioconjug Chem 2002;13(1):47-58
  • Giles FJ, Kantarjian HM, Kornblau SM, et al. Mylotarg (gemtuzumab ozogamicin) therapy is associated with hepatic venoocclusive disease in patients who have not received stem cell transplantation. Cancer 2001;92(2):406-13
  • Sharma SK, Chester KA, Bagshawe KD. Emerging therapeutic concepts I: ADEPT. In: Dübel S, editor, Handbook of therapeutic antibodies. Wiley-VCH, Weinheim, Germany; 2007:501-13
  • Sharma SK, Bagshawe KD, Melton RG, Sherwood RF. Human immune response to monoclonal antibody-enzyme conjugates in ADEPT pilot clinical trial. Cell Biophys 1992;21(1-3):109-20
  • Bosslet K, Czech J, Hoffmann D. Tumor-selective prodrug activation by fusion protein-mediated catalysis. Cancer Res 1994;54(8):2151-9
  • Lowe H, Tolner B, Kogelberg H, et al. A novel mutated human enzyme with a bis-chloro-phenol prodrug for Antibody Directed Enzyme Prodrug Therapy (ADEPT). The National Cancer Research Institute (NCRI) Cancer Conference. Birmingham, UK; 2007
  • Pastan I, Willingham MC, Fitzgerald DJ. Immunotoxins. Cell 1986;47(5):641-8
  • Frankel AE, Kreitman RJ, Sausville EA. Targeted toxins. Clin Cancer Res 2000;6(2):326-34
  • Rybak SM, Newton DL. Immunotoxins and Beyond: Targeted RNases. In: Handbook of therapeutic antibodies. Dübel S, editor, WILEY-VCH, Weinheim; 2007:379-410
  • Johnson VG, Wrobel C, Wilson D, et al. Improved tumor-specific immunotoxins in the treatment of CNS and leptomeningeal neoplasia. J Neurosurg 1989;70(2):240-8
  • Woo JH, Liu JS, Kang SH, et al. GMP production and characterization of the bivalent anti-human T cell immunotoxin, A-dmDT390-bisFv(UCHT1) for Phase I/II clinical trials. Protein Expr Purif 2008;58(1):1-11
  • Weaver M, Laske DW. Transferrin receptor ligand-targeted toxin conjugate (Tf-CRM107) for therapy of malignant gliomas. J Neurooncol 2003;65(1):3-13
  • Frankel AE, Powell BL, Lilly MB. Diphtheria toxin conjugate therapy of cancer. Cancer Chemother Biol Response Modif 2002;20:301-13
  • Pai LH, Wittes R, Setser A, et al. Treatment of advanced solid tumors with immunotoxin LMB-1: an antibody linked to Pseudomonas exotoxin. Nat Med 1996;23:350-3
  • Kreitman RJ, Wilson WH, Bergeron K, et al. Efficacy of the anti-CD22 recombinant immunotoxin BL22 in chemotherapy-resistant hairy-cell leukemia. N Engl J Med 2001;345(4):241-7
  • Kreitman RJ, Squires DR, Stetler-Stevenson M, et al. Phase I trial of recombinant immunotoxin RFB4(dsFv)-PE38 (BL22) in patients with B-cell malignancies. J Clin Oncol 2005;23(27):6719-29
  • Frankel AE, Neville DM, Bugge TA, et al. Immunotoxin therapy of hematologic malignancies. Semin Oncol 2003;30(4):545-57
  • Messmann RA, Vitetta ES, Headlee D, et al. A Phase I study of combination therapy with immunotoxins IgG-HD37-deglycosylated ricin A chain (dgA) and IgG-RFB4-dgA (Combotox) in patients with refractory CD19(+), CD22(+) B cell lymphoma. Clin Cancer Res 2000;6(4):1302-13
  • Onda M, Wang QC, Guo HF, et al. In vitro and in vivo cytotoxic activities of recombinant immunotoxin 8H9(Fv)-PE38 against breast cancer, osteosarcoma, and neuroblastoma. Cancer Res 2004;64(4):1419-24
  • D'alessio G. New and cryptic biological messages from RNases. Trends Cell Biol 1993;3(4):106-9
  • Boix E, Nogues MV. Mammalian antimicrobial proteins and peptides: overview on the RNase A superfamily members involved in innate host defence. Mol Biosyst 2007;3(5):317-35
  • Rybak SM, Newton DL.Immunoenzymes. In: Chamow SM, et al, editors, Antibody fusion proteins. ohn Whiley & Sons, New York; 1999:53-110
  • Aleksandrowicz J. Intracutaneous ribonuclease in chronic myelocytic leukemia. Lancet 1958;272(7043):420
  • Mikulski SM, Costanzi JJ, Vogelzang NJ, et al. Phase II trial of a single weekly intravenous dose of ranpirnase in patients with unresectable malignant mesothelioma. J Clin Oncol 2002;20(1):274-81
  • Glukhov BN, Jerusalimsky AP, Canter VM, Salganik RI. Ribonuclease treatment of tick-borne encephalitis. Arch Neurol 1976;33(9):598-603
  • Rybak SM, Saxena SK, Ackerman EJ, Youle RJ. Cytotoxic potential of ribonuclease and ribonuclease hybrid proteins. J Biol Chem 1991;266(31):21202-7
  • Newton DL, Walbridge S, Mikulski SM, et al. Toxicity of an antitumor ribonuclease to Purkinje neurons. J Neurosci 1994;14(2):538-44
  • Benito A, Ribo M, Vilanova M. On the track of antitumour ribonucleases. Mol Biosyst 2005;1(4):294-302
  • Ledoux L. Action of ribonuclease on certain ascites tumours. Nature 1955;175(4449):258-9
  • Ledoux L. Action of ribonuclease on two solid tumours in vivo Nature 1955;176(4470):36-7
  • Laccetti P, Spalletti-Cernia D, Portella G, et al. Seminal ribonuclease inhibits tumor growth and reduces the metastatic potential of Lewis lung carcinoma. Cancer Res 1994;54(16):4253-6
  • Rybak SM. Antibody-onconase conjugates: cytotoxicity and intracellular routing. Curr Pharm Biotechnol 2008;9(3):226-30
  • Griffiths SJ, Adams DJ, Talbot SJ. Ribonuclease inhibits Kaposi's sarcoma. Nature 1997;390(6660):568
  • Sakakibara R, Hashida K, Tominaga N, et al. A putative mouse oocyte maturation inhibitory protein from urine of pregnant women: N-terminal sequence homology with human nonsecretory ribonuclease. Chem Pharm Bull (Tokyo) 1991;39(1):146-9
  • Newton DL, Rybak SM. Unique recombinant human ribonuclease and inhibition of Kaposi's sarcoma cell growth. J Natl Cancer Inst 1998;90(23):1787-91
  • Chang C, Newton DL, Rybak SM, Wlodawer A. Crystallographic and functional studies of a modified form of eosinophil-derived neurotoxin (EDN) with novel biological activities. J Mol Biol 2002;317(1):119-30
  • Beintema JJ, Kleineidam RG. The ribonuclease a superfamily: general discussion. Cell Mol Life Sci 1998;54(8):825-32
  • Canals A, Ribo M, Benito A, et al. Production of engineered human pancreatic ribonucleases, solving expression and purification problems, and enhancing thermostability. Protein Expr Purif 1999;17(1):169-81
  • Dübel S. Reconstitution of human RNaseA from two separate fragments fused to different single chain antibody fragments: On the way to binary immunotoxins. Tumor Target 1999;4:37-46
  • Fett JW, Strydom DJ, Lobb RR, et al. Isolation and characterization of angiogenin, an angiogenic protein from human carcinoma cells. Biochemistry 1985;24(20):5480-6
  • Tello-Montoliu A, Patel JV, Lip GY. Angiogenin: a review of the pathophysiology and potential clinical applications. J Thromb Haemost 2006;4(9):1864-74
  • Rugeles MT, Trubey CM, Bedoya VI, et al. Ribonuclease is partly responsible for the HIV-1 inhibitory effect activated by HLA alloantigen recognition. Aids 2003;17(4):481-6
  • Saxena SK, Rybak SM, Davey RT JR, et al. Angiogenin is a cytotoxic, tRNA-specific ribonuclease in the RNase A superfamily. J Biol Chem 1992;267(30):21982-6
  • Rybak SM, Hoogenboom HR, Meade HM, et al. Humanization of immunotoxins. Proc Natl Acad Sci USA 1992;89(8):3165-9
  • Darzynkiewicz Z, Carter SP, Mikulski SM, et al. Cytostatic and cytotoxic effects of Pannon (P-30 Protein), a novel anticancer agent. Cell Tissue Kinet 1988;21(3):169-82
  • Lee I, Lee YH, Mikulski SM, et al. Tumoricidal effects of onconase on various tumors. J Surg Oncol 2000;73(3):164-71
  • Costanzi J, Sidransky D, Navon A, Goldsweig H. Ribonucleases as a novel pro-apoptotic anticancer strategy: review of the preclinical and clinical data for ranpirnase. Cancer Invest 2005;23(7):643-50
  • Vogelzang NJ, Aklilu M, Stadler WM, et al. A Phase II trial of weekly intravenous ranpirnase (Onconase), a novel ribonuclease in patients with metastatic kidney cancer. Invest New Drugs 2001;19(3):255-60
  • Vogelzang NJ, Porta C, Mutti L. New agents in the management of advanced mesothelioma. Semin Oncol 2005;32(3):336-50
  • Pavlakis N, Vogelzang NJ. Ranpirnase – an antitumour ribonuclease: its potential role in malignant mesothelioma. Expert Opin Biol Ther 2006;6(4):391-9
  • Halicka DH, Pozarowski P, Ita M, et al. Enhancement of activation-induced apoptosis of lymphocytes by the cytotoxic ribonuclease onconase (Ranpirnase). Int J Oncol 2002;21(6):1245-50
  • Wu Y, Mikulski SM, Ardelt W, et al. A cytotoxic ribonuclease. Study of the mechanism of onconase cytotoxicity. J Biol Chem 1993;268(14):10686-93
  • Wu Y, Saxena SK, Ardelt W, et al. A study of the intracellular routing of cytotoxic ribonucleases. J Biol Chem 1995;270(29):17476-81
  • Iordanov MS, Ryabinina OP, Wong J, et al. Molecular determinants of apoptosis induced by the cytotoxic ribonuclease onconase: evidence for cytotoxic mechanisms different from inhibition of protein synthesis. Cancer Res 2000;60(7):1983-94
  • Saxena SK, Sirdeshmukh R, Ardelt W, et al. Entry into cells and selective degradation of tRNAs by a cytotoxic member of the RNase A family. J Biol Chem 2002;277(17):15142-6
  • Grabarek J, Ardelt B, Du L, Darzynkiewicz Z. Activation of caspases and serine proteases during apoptosis induced by onconase (Ranpirnase). Exp Cell Res 2002;278(1):61-71
  • Ardelt B, Ardelt W, Darzynkiewicz Z. Cytotoxic ribonucleases and RNA interference (RNAi). Cell Cycle 2003;2(1):22-4
  • Tsai SY, Hsieh TC, Ardelt B, et al. Combined effects of onconase and IFN-beta on proliferation, macromolecular syntheses and expression of STAT-1 in JCA-1 cancer cells. Int J Oncol 2002;20(5):891-6
  • Lee I, Lee YH, Mikulski SM, Shogen K. Effect of ONCONASE +/- tamoxifen on ASPC-1 human pancreatic tumors in nude mice. Adv Exp Med Biol 2003;530:187-96
  • Rybak SM, Pearson JW, Fogler WE, et al. Enhancement of vincristine cytotoxicity in drug-resistant cells by simultaneous treatment with onconase, an antitumor ribonuclease. J Natl Cancer Inst 1996;88(11):747-53
  • Haigis MC, Kurten EL, Raines RT. Ribonuclease inhibitor as an intracellular sentry. Nucleic Acids Res 2003;31(3):1024-32
  • Gaur D, Swaminathan S, Batra JK. Interaction of human pancreatic ribonuclease with human ribonuclease inhibitor. Generation of inhibitor-resistant cytotoxic variants. J Biol Chem 2001;276(27):24978-84
  • Leland PA, Schultz LW, Kim BM, Raines RT. Ribonuclease A variants with potent cytotoxic activity. Proc Natl Acad Sci USA 1998;95(18):10407-12
  • Hayashida T, Ueda M, Aiura K, et al. Anti-angiogenic effect of an insertional fusion protein of human basic fibroblast growth factor and ribonuclease-1. Protein Eng Des Sel 2005;18(7):321-7
  • Lee JE, Raines RT. Contribution of active-site residues to the function of onconase, a ribonuclease with antitumoral activity. Biochemistry 2003;42(39):11443-50
  • Klink TA, Raines RT. Conformational stability is a determinant of ribonuclease A cytotoxicity. J Biol Chem 2000;275(23):17463-67
  • Rybak SM, Newton DL, Mikulski SM, et al. Cytotoxic Onconase and ribonuclease A chimeras: Comparison and in vitro characterization. Drug Deliv 1993;1:3-10
  • Rodriguez M, Torrent G, Bosch M, et al. Intracellular pathway of Onconase that enables its delivery to the cytosol. J Cell Sci 2007;120(Pt 8):1405-11
  • Bosch M, Benito A, Ribo M, et al. A nuclear localization sequence endows human pancreatic ribonuclease with cytotoxic activity. Biochemistry 2004;43(8):2167-77
  • Futami J, Maeda T, Kitazoe M, et al. Preparation of potent cytotoxic ribonucleases by cationization: enhanced cellular uptake and decreased interaction with ribonuclease inhibitor by chemical modification of carboxyl groups. Biochemistry 2001;40(25):7518-24
  • De Lorenzo C, Di Malta C, Cali G, et al. Intracellular route and mechanism of action of ERB-hRNase, a human anti-ErbB2 anticancer immunoagent. FEBS Lett 2007;581(2):296-300
  • Hust M, Jostock T, Menzel C, et al. Single chain Fab (scFab) fragment. BMC Biotechnol 2007;7:14
  • Carter P. Improving the efficacy of antibody-based cancer therapies. Nat Rev Cancer 2001;1(2):118-29
  • Schirrmann T, Al-Halabi L, Dübel S, Hust M. Production systems for recombinant antibodies. Frontiers in Bioscience. Front Biosci 2008;13:4576-94
  • Yokota T, Milenic DE, Whitlow M, Schlom J. Rapid tumor penetration of a single-chain Fv and comparison with other immunoglobulin forms. Cancer Res 1992;52(12):3402-8
  • Wu AM, Chen W, Raubitschek A, et al. Tumor localization of anti-CEA single-chain Fvs: improved targeting by non-covalent dimers. Immunotechnology 1996;2(1):21-36
  • Colcher D, Bird R, Roselli M, et al. In vivo tumor targeting of a recombinant single-chain antigen-binding protein. J Natl Cancer Inst 1990;82(14):1191-7
  • Milenic DE, Yokota T, Filpula DR, et al. Construction, binding properties, metabolism, and tumor targeting of a single-chain Fv derived from the pancarcinoma monoclonal antibody CC49. Cancer Res 1991;51(23 Pt 1):6363-71
  • Hudson PJ, Souriau C. Engineered antibodies. Nat Med 2003;9(1):129-34
  • Adams GP, Mccartney JE, Tai MS, et al. Highly specific in vivo tumor targeting by monovalent and divalent forms of 741F8 anti-c-erbB-2 single-chain Fv. Cancer Res 1993;53(17):4026-34
  • Nielsen UB, Adams GP, Weiner LM, Marks JD. Targeting of bivalent anti-ErbB2 diabody antibody fragments to tumor cells is independent of the intrinsic antibody affinity. Cancer Res 2000;60(22):6434-40
  • Krauss J, Arndt MA, Dübel S, Rybak SM. Antibody-targeted RNase fusion proteins (immunoRNases) for cancer therapy. Curr Pharm Biotechnol 2008;9(3):231-4
  • Newton DL, Ilercil O, Laske DW, et al. Cytotoxic ribonuclease chimeras. Targeted tumoricidal activity in vitro and in vivo. J Biol Chem 1992;67(27):19572-8
  • De Lorenzo C, Arciello A, Cozzolino R, et al. A fully human antitumor immunoRNase selective for ErbB-2-positive carcinomas. Cancer Res 2004;64(14):4870-4
  • Menzel C, Schirrmann T, Konthur Z, et al. Human antibody RNase fusion protein targeting CD30+ lymphomas. Blood 2008;111(7):3830-7
  • Newton DL, Xue Y, Olson KA, et al. Angiogenin single-chain immunofusions: influence of peptide linkers and spacers between fusion protein domains. Biochemistry 1996;35(2):545-53
  • Vasandani VM, Wu YN, Mikulski SM, et al. Molecular determinants in the plasma clearance and tissue distribution of ribonucleases of the ribonuclease A superfamily. Cancer Res 1996;56(18):4180-6
  • Haigis MC, Raines RT. Secretory ribonucleases are internalized by a dynamin-independent endocytic pathway. J Cell Sci 2003;116(Pt 2):313-24
  • Newton DL, Hansen HJ, Mikulski SM, et al. Potent and specific antitumor effects of an anti-CD22-targeted cytotoxic ribonuclease: potential for the treatment of non-Hodgkin lymphoma. Blood 2001;97(2):528-35
  • Newton DL, Pearson JW, Xue Y, et al. Anti-tumor ribonuclease combined with or conjugated to monoclonal antibody MRK16, overcomes multidrug resistance to vincristine in vitro and in vivo. Int J Oncology 1996;8:1095-104
  • Newton DL, Pollock D, Ditullio P, et al. Antitransferrin receptor antibody-RNase fusion protein expressed in the mammary gland of transgenic mice. J Immunol Methods 1999;231(1-2):159-67
  • Debinski W, Pastan I. Monovalent immunotoxin containing truncated form of Pseudomonas exotoxin as potent antitumor agent. Cancer Res 1992;52(19):5379-85
  • Schroff RW, Foon KA, Beatty SM, et al. Human anti-murine immunoglobulin responses in patients receiving monoclonal antibody therapy. Cancer Res 1985;45(2):879-85
  • Chen S, Le SY, Newton DL, et al. A gender-specific mRNA encoding a cytotoxic ribonuclease contains a 3′ UTR of unusual length and structure. Nucleic Acids Res 2000;28(12):2375-82
  • Arndt MA, Krauss J, Schwarzenbacher R, et al. Generation of a highly stable, internalizing anti-CD22 single-chain Fv fragment for targeting non-Hodgkin's lymphoma. Int J Cancer 2003;107(5):822-9
  • Krauss J, Arndt MA, Martin AC, et al. Specificity grafting of human antibody frameworks selected from a phage display library: generation of a highly stable humanized anti-CD22 single-chain Fv fragment. Protein Eng 2003;16(10):753-9
  • Boix E, Wu Y, Vasandani VM, et al. Role of the N terminus in RNase A homologues: differences in catalytic activity, ribonuclease inhibitor interaction and cytotoxicity. J Mol Biol 1996;257(5):992-1007
  • Shapiro R, Harper JW, Fox EA, et al. Expression of Met-(-1) angiogenin in Escherichia coli: conversion to the authentic less than Glu-1 protein. Anal Biochem 1988;175(2):450-61
  • Russo N, Nobile V, Di Donato A, et al. The C-terminal region of human angiogenin has a dual role in enzymatic activity. Proc Natl Acad Sci USA 1996;93(8):3243-7
  • Krauss J, Arndt MA, Vu BK, et al. Targeting malignant B-cell lymphoma with a humanized anti-CD22 scFv-angiogenin immunoenzyme. Br J Haematol 2005;128(5):602-9
  • Arndt MA, Krauss J, Vu BK, et al. A dimeric angiogenin immunofusion protein mediates selective toxicity toward CD22+ tumor cells. J Immunother 2005;28(3):245-51
  • Krauss J, Arndt MA, Vu BK, et al. Efficient killing of CD22+ tumor cells by a humanized diabody-RNase fusion protein. Biochem Biophys Res Commun 2005;331(2):595-602
  • Carnahan J, Wang P, Kendall R, et al. Epratuzumab, a humanized monoclonal antibody targeting CD22: characterization of in vitro properties. Clin Cancer Res 2003;9(10 Pt 2):S3982-90
  • Falini B, Flenghi L, Fedeli L, et al. In vivo targeting of Hodgkin and Reed-Sternberg cells of Hodgkin's disease with monoclonal antibody Ber-H2 (CD30): immunohistological evidence. Br J Haematol 1992;82(1):38-45
  • Renner C, Stehle I, Lee FT, et al. Targeting properties of an anti-CD16/anti-CD30 bispecific antibody in an in vivo system. Cancer Immunol Immunother 2001;50(2):102-8
  • Schnell R, Staak O, Borchmann P, et al. A Phase I study with an anti-CD30 ricin A-chain immunotoxin (Ki-4.dgA) in patients with refractory CD30+ Hodgkin's and non-Hodgkin's lymphoma. Clin Cancer Res 2002;8(6):1779-86
  • Braschoss S, Hirsch B, Dübel S, et al. New anti-CD30 human pancreatic ribonuclease-based immunotoxin reveals strong and specific cytotoxicity in vivo. Leuk Lymphoma 2007;48(6):1179-86
  • Huhn M, Sasse S, Tur MK, et al. Human angiogenin fused to human CD30 ligand (Ang-CD30L) exhibits specific cytotoxicity against CD30-positive lymphoma. Cancer Res 2001;61(24):8737-42
  • Barth S, Matthey B, Huhn M, et al. CD30L-ETA': a new recombinant immunotoxin based on the CD30 ligand for possible use against human lymphoma. Cytokines Cell Mol Ther 1999;5(2):69-78
  • Stocker M, Tur MK, Sasse S, et al. Secretion of functional anti-CD30-angiogenin immunotoxins into the supernatant of transfected 293T-cells. Protein Expr Purif 2003;28(2):211-9
  • Zewe M, Rybak SM, Dübel S, et al. Cloning and cytotoxicity of a human pancreatic RNase immunofusion. Immunotechnology 1997;3(2):127-36
  • Suzuki M, Saxena SK, Boix E, et al. Engineering receptor-mediated cytotoxicity into human ribonucleases by steric blockade of inhibitor interaction. Nat Biotechnol 1999;17(3):265-70
  • Newton DL, Nicholls PJ, Rybak SM, Youle RJ. Expression and characterization of recombinant human eosinophil-derived neurotoxin and eosinophil-derived neurotoxin-anti-transferrin receptor sFv. J Biol Chem 1994;269(43):26739-45
  • Rybak SM, Hoogenboom HR, Newton DL, et al. Rational immunotherapy with ribonuclease chimeras. An approach toward humanizing immunotoxins. Cell Biophys 1992;21(1-3):121-38
  • Gho YS, Chae CB. Luteinizing hormone releasing hormone-RNase A conjugates specifically inhibit the proliferation of LHRH-receptor-positive human prostate and breast tumor cells. Mol Cells 1999;9(1):31-6
  • Psarras K, Ueda M, Tanabe M, et al. Targeting activated lymphocytes with an entirely human immunotoxin analogue: human pancreatic RNase1-human IL-2 fusion. Cytokine 2000;12(6):786-90
  • Deonarain MP, Epenetos AA. Design, characterization and anti-tumour cytotoxicity of a panel of recombinant, mammalian ribonuclease-based immunotoxins. Br J Cancer 1998;77(4):537-46
  • Jinno H, Ueda M, Ozawa S, et al. Epidermal growth factor receptor-dependent cytotoxic effect by an EGF-ribonuclease conjugate on human cancer cell lines–a trial for less immunogenic chimeric toxin. Cancer Chemother Pharmacol 1996;38(4):303-8
  • Jinno H, Ueda M, Ozawa S, et al. Epidermal growth factor receptor-dependent cytotoxicity for human squamous carcinoma cell lines of a conjugate composed of human EGF and RNase 1. Life Sci 1996;58(21):1901-8
  • Jinno H, Ueda M, Ozawa S, et al. The cytotoxicity of a conjugate composed of human epidermal growth factor and eosinophil cationic protein. Anticancer Res 2002;22(6C):4141-5
  • Yoon JM, Han SH, Kown OB, et al. Cloning and cytotoxicity of fusion proteins of EGF and angiogenin. Life Sci 1999;64(16):1435-45
  • Psarras K, Ueda M, Yamamura T, et al. Human pancreatic RNase1-human epidermal growth factor fusion: an entirely human ‘immunotoxin analog’ with cytotoxic properties against squamous cell carcinomas. Protein Eng 1998;11(12):1285-92
  • De Lorenzo C, Nigro A, Piccoli R, D'alessio G. A new RNase-based immunoconjugate selectively cytotoxic for ErbB2-overexpressing cells. FEBS Lett 2002;516(1-3):208-12
  • Lee I. Ranpirnase (Onconase), a cytotoxic amphibian ribonuclease, manipulates tumour physiological parameters as a selective killer and a potential enhancer for chemotherapy and radiation in cancer therapy. Expert Opin Biol Ther 2008;8(6):813-27

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Order Reprints Request Corporate Permissions

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

Request Academic Permissions

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.

Related research

People also read lists articles that other readers of this article have read.

Recommended articles lists articles that we recommend and is powered by our AI driven recommendation engine.

Cited by lists all citing articles based on Crossref citations.
Articles with the Crossref icon will open in a new tab.