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中国生物工程杂志

China Biotechnology
China Biotechnology  2009, Vol. 29 Issue (04): 98-103    DOI:
    
Application of IL-13Rα2-directed Toxin Fusion Protein in Tumor Therapy
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Abstract  The research of interleukin13 receptor α2 (IL-13Rα2) chain is a rising pop these years. Previous studies have shown that many human tumors overexpress IL-13Rα2 chain, while normal cells do not express this receptor or express very low level. This difference of express level is significant to diagnose and cure tumors by the IL-13Rα2-directed toxin fusion protein. During the past decade, the structure and the function of IL-13Rα2 together with the relationship between this receptor and tumors has been further developed. Therefore new therapies and theories can be proposed as the clinical tumor treatments. In this case,the expression in various tumor cell lines was not only focused on but also on the IL-13 and toxin fusion protein killing effect in both the cell level and the in vivo level. Besides,an overview of the mechanism in the treatment of IL-13Rα2-directed toxin fusion protein together with the improved methods for fusion protein purification and other relative tumor therapy was given. In conclusion,the current status and progress of IL-13Rα2 as well as IL-13Rα2-directed toxin fusion protein in tumor therapy were represented.

Key wordsCarcinoma;IL-13Rα2;Tumor therapy;Progress     
Received: 05 September 2008      Published: 27 April 2009
ZTFLH:  Q279  
Cite this article:

DU Juan- Hu-Gong-Gang- Hou-Ling-Ling. Application of IL-13Rα2-directed Toxin Fusion Protein in Tumor Therapy. China Biotechnology, 2009, 29(04): 98-103.

URL:

https://manu60.magtech.com.cn/biotech/     OR     https://manu60.magtech.com.cn/biotech/Y2009/V29/I04/98

[1] Lebman D A, Coffman R L. Interleukine-4 causes isotype switching to IgE in T cell-stimulated clonal B cell cultures. J Exp Med, 1988, 168(3): 853~862 [2] Ihle J N, Witthuhn B A, Quelle F W, et al. Signaling through the hematopoietic cytokine receptors. Annu Rev Immunol, 1995, 13(1): 369~398 [3] Rahaman S O, Sharma P, Harbor P C, et al. IL-13Rα2, a decoy receptor for IL-13 acts as an inhibitor or IL-4-dependent signal transduction in glioblastoma cells. Cancer Research, 2002, 62(4): 1103~1109 [4] Nelms K, Keegan A D, Zamorano J, et al. The IL-4 receptor: signaling mechanisms and biologic functions. Annu Rev Immunol, 1999, 17(1): 701~738 [5] Joshi B H, Plautz G E,Puri R K. Interleukin-13 receptor α chain: A novel tumor-associated transmembrane protein in primary explants of human malignant gliomas. Cancer Research, 2000, 60(5): 1168~1172 [6] Kawakami M, Kawakami K, Kasperbauer J L, et al. Interleukin-13 receptor α2 chain in human head and neck cancer serves as a unique diagnostic marker. Clin Cancer Research, 2003, 9(17): 6381~6388 [7] Kawakami M, Kawakami K, Takahashi S, et al. Analysis of interleukin13 receptor α2 expression in human pediatric brain tumors. Cancer, 2004, 101(5): 1036-1042 [8] Kioi M, Kawakami M, Shimamura T, et al. Interleukin13 receptor α2 china a potential biomarker and molecular target for ovarian cancer therapy. Cancer, 2006, 107(6): 1407~1418 [9] Obiri N I, Debinski W, Leonard W J, et al. Receptor for interleukin 13. Interaction with interleukin 4 by a mechanism that does not involve the common gamma chain shared by receptors for interleukins 2, 4, 7, 9, and 15. J Biol Chem, 1995, 270(15): 8797~8804 [10] Debinski W, Obiri N I, Powers S K, et al. A novel chimeric protein composed of interleukin 13 and Pseudomonas exotoxin is highly cytotoxic to human carcinoma cells expressing receptors for interleukin 13 and interleukin 4. J Biol Chem, 1995, 270(28): 16775~16780 [11] Obiri N I, Leland P, Murata T. The IL-13 receptor structure differs on various cell types and may share more than one component with IL-4 receptor. J Immunol, 1997, 158(2): 756~764 [12] Husain S R, Puri R K. Interleukin13 fusion cytotoxin as a potent targeted agent for AIDSKaposi’s sarcoma xenograft. Blood, 2000, 95(11): 3506~3513 [13] Maini A, Hillman G, Haas G P, et al. Interleukin13 receptors on human prostate carcinoma cell lines represent a novel target for a chimeric protein composed of IL13 and a mutated form of Pseudomonas exotoxin. J Urol, 1997, 158(3 Pt 1): 948~953 [14] Kornmann M, Kleeff J, Debinski W, et al. Pancreatic cancer cells express interleukin13 and 4 receptors, and their growth is inhibited by Pseudomonas exotoxin coupled to interleukin13 and 4. Anticancer Res, 1999, 19(1A): 125~131 [15] Debinski W, Obiri N I, Powers S K, et al. Human glioma cells overexpress receptors for interleukin 13 and are Extremely sensitive to a novel chimeric protein composed of interleukin 13 and pseudomonas exotoxin. Clin Cancer Research, 1995, 1(11): 1253~1258 [16] Husain S R, Obiri N I, Gill P, et al. Receptor for interleukin 13 on AIDSassociated Kaposi’s sarcoma cells serves as a new target for a potent Pseudomonas exotoxinbased chimeric toxin protein. Clin Cancer Research, 1997, 3(2): 151~156 [17] Puri R K, Leland P, Obiri N I, et al. Targeting of interleukin13 receptor on human renal cell carcinoma cells by a recombinant chimeric protein composed of interleukin13 and a truncated form of Pseudomonas exotoxin A (PE38QQR). Blood, 1996, 87(10): 43334339 [18] Husain S R, Joshi B H, Puri R K. Interleukin13 receptor as a unique target for antiglioblastoma therapy. Int J Cancer, 2001, 92(2): 168~175 [19] Debinski W, Gibo D M, Obiri N I,et al. Novel antibrain tumor cytotoxins specific for cancer cells. Nat Biotechnol, 1998, 16(5): 449~453 [20] Debinski W, Gibo D M, Puri R K. Novel way to increase targeting specificity to a human glioblastomaassociated receptor for interleukin 13. Int J Cancer, 1998, 76(4): 547~551 [21] Li C, Hall W A, Jin N, et al. Targeting glioblastoma multiforme with an IL13/diphtheria toxin fusion protein in vitro and in vivo in nude mice. Protein Engineering, 2002, 15(5): 419~427 [22] Mintz A, Gibo D M, SlagleWebb B, et al. IL13Rα2 is a Gliomarestricted receptor for interleukin13. Neoplasia, 2002, 4(5): 388~399 [23] Kawakami K, Kawakami M, Sony P J, et al. In vivo overexpression of IL13 receptor α2 chain inhibits tumorigenicity of human breast and pancreatic tumors in immunodeficient mice. J Exp Med, 2001, 194(12): 1743~1754 [24] Kawakami K, Kioi M, Liu Q, et al. Evidence that IL13Rα2 chain in human glioma cells is responsible for the antitumor activity mediated by receptordirected cytotoxin therapy. J Immunother, 2005, 28(3): 193~202 [25] LeMaistre C F, Saleh M N, Kuzel T M, et al. Phase Ⅰ trial of ligand fusionprotein (DAB389IL2) in lymphomas expressing the receptor for interleukin2. Blood, 1998, 91(2): 399~405 [26] Kawakami K, Kawakami M,Puri R K.Specifically targeted killing of interleukin13(IL13) receptorexpressing breast cancer by IL13 fusion cytotoxin in animal model of human disease. Molecular Cancer Therapeutics, 2004, 3(2): 137~147 [27] Weingart J, Strauss L C, Grossman S A, et al. Phase Ⅰ/Ⅱ study: intratumoral infusion of IL13PE38QQR cytotoxin for recurrent supratentorial malignant glioma. NeuroOncology, 2002, 4: 379 [28] Wu Ah,Low W C. Molecular cloning of the rat IL13 alpha 2 receptor cDNA and its expression in rat tissues. Journal of NeuroOncology, 2002, 59(2): 99~105 [29] Mintz A, Gibo D M, Madhankumar A B, et al. Molecular targeting with recombinant cytotoxins of interleukin13 receptor α2expressing glioma. Journal of NeuroOncology, 2003, 64(1): 117~123 [30] Joshi B H, Puri R K. Optimization of expression and purification of two biologically active chimeric fusion proteins that consist of human interleukin13 and Pseudomonas exotoxin in Escherichia coli. Protein Expression and Purification, 2005, 39(2): 189~198 [31] Zhou G, Roizman B. Construction and properties of a herpes simplex virus 1 designed to enter cells solely via the IL13 {alpha} 2 receptor. PNAS, 2006, 103(14): 5508~5513 [32] Murata T, Obiri N I, Debinski W, et al. Structure of IL13 receptor: analysis of subunit composition in cancer and immune cells. Biochem Biophy Res Commun, 1997, 238(1): 90~94 [33] Oshima Y, Puri R K. Suppression of an IL13 autocrine growth loop in a human Hodgkin/ReedSternberg tumor cell line by a novel IL13 antagonist. Cell Immunology, 2001, 211(1): 37~42 [34] Oshima Y, Puri R K. Characterization of a powerful high affinity antagonist that inhibits biological activities of human interleukin13. J Biol Chem, 2001, 276(18): 15185~15191 [35] Honjo Y, Bian Y, Kawakami K, et al. TGFbeta receptor I conditional knockout mice develop spontaneous squamous cell carcinoma. Cell Cycle, 2007, 6(11): 1360~1366 [36] Kawakami M, Kawakami K,Puri R K.Tumor regression mechanisms by IL13 receptortargeted cancer therapy involve apoptotic pathways. Int J Cancer, 2003, 103(1): 45~52 [37] Han J, Yang L, Puri R K. Analysis of target genes induced by IL13 cytotoxin in human glioblastoma cells. Journal of NeuroOncology, 2005, 72(1): 35~46 [38] Kioi M, Seetharam S, Puri R K. Nlinked glycosylation of IL13Rα2 is essential for optimal IL13 inhibitory activity. Faseb J, 2006, 20(13): 2378~2380
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