Cancer therapy with engineered monoclonal antibodies

Binyamin, Liat; Borghaei, Hossein; Weiner, Louis M.

doi:10.1016/j.uct.2006.05.002

Cited by 15 publications

(15 citation statements)

References 90 publications

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“…Nonetheless, plant and insect cells resistant to the toxins have been developed, which are able to produce active recombinant toxins. The benefit of immunotoxins includes an exceptionally small amount of the protein needed to exterminate both resting and dividing cells and the chattels is obtained from the catalytic assests of the fusion proteins; a single molecule can assail multiple intracellular targets (Binyamin et al, 2006).…”

Section: Production Of Immunotoxinsmentioning

confidence: 99%

“…Immunotoxins have been found to be most advantageous for treating hematologic malignancies as the malignant cells are frequently intravascular and accessible to intravenously administered drug and also the patients repeatedly lack adequate immunity to make antibodies against the toxin. Thus, few antigens have been used to target hematologic malignancies by immunotoxins (Dosio et al, 2014;Wu, 1997;Pranchevicius and Vieira, 2013;May et al, 2012;Binyamin et al, 2006).…”

Section: Immunotoxins As Therapeutic Agentsmentioning

confidence: 99%

“…Quiescent HIV-infected T-cells competent in replication could be generated in vitro by transmitting infection to peripheral blood mononuclear cells (pBMC) with HIV and subsequently obliterating the HIV-producing cells with an anti-CD25 immunotoxin (IT). After that the CD25 -quiescent infected cells can be annihilated with an anti-CD45RO immunotoxin (May et al, 2012;Binyamin et al, 2006;Campbell and Marcus, 2003).…”

Section: Ll2 and Bl22mentioning

confidence: 99%

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Immune-O-Toxins as the magic bullet for therapeutic purposes

Srivastava

Luqman

2015

Biomed Res Ther

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Abstract-Immunotoxins are chimeric molecules embodied with a protein toxin and a ligand which is either a growth factor or an antibody. The ligand part of the immunotoxin recognizes and binds to an antigen of the target cell, allowing the internalization of the toxin-moiety and permitting its drift to the cytoplasm where it can destroy the cell. Target specificity of the chimeric protein is determined via the binding attributes of the chosen antibody. Predominantly, immunotoxins are purposefully constructed to slay cancer cells as part of novel treatment approach. In addition they are also used for various autoimmune, viral and other infectious diseases. With the advent of biotechnology, recombinant immunotoxins have been created and are clinically tested to target malignant cells. Our article summarizes foremost progress in the development of immunotoxin based therapeutics and presents a comprehensive portrayal of the immunotoxin generation.

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Section: Production Of Immunotoxinsmentioning

confidence: 99%

Section: Immunotoxins As Therapeutic Agentsmentioning

confidence: 99%

Section: Ll2 and Bl22mentioning

confidence: 99%

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Immune-O-Toxins as the magic bullet for therapeutic purposes

Srivastava

Luqman

2015

Biomed Res Ther

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“…In addition, anti-CD9 MAbs amplify the inherent tumour suppressor function of CD9 (Ovalle et al, 2007). (Binyamin et al, 2006). …”

Section: Therapeutic Targeting Of Proteinsmentioning

confidence: 99%

Development of monoclonal antibodies for the identification of novel invasion associated targets in human cancer

O'sullivan¹

2008

European Journal of Cancer Supplements

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“…These surface molecules include cell surface receptors, cluster designation molecules, oncofetal proteins, angiogenesis pathway proteins and tumor stromal cells (4). Attempts have been made to kill tumor cells through specific surface molecules (5). It has been found that a large variety of monoclonal antibodies (mAb) bind to antigens on cancer cells and kill cancer cells through apoptosis.…”

Section: Introductionmentioning

confidence: 99%

In vitro and in vivo antitumor effects of the recombinant immunotoxin IL6(T23)-PE38KDEL in multiple myeloma

Guo

Han

et al. 2012

Oncology Letters

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Abstract. IL6(T23)-PE38KDEL is a chimeric molecule composed of interleukin 6 (IL6), missing the N-terminal 23 amino acids, and fused to a truncated mutant form of Pseudomonas exotoxin (PE38KDEL). The aim of this study was to evaluate this recombinant immunotoxin in terms of its specific cytotoxicity to IL6R-overexpressing multiple myeloma (MM) cells in vitro, as well as its antitumor effects and side effects in vivo. IL6(T23)-PE38KDEL was expressed in Escherichia coli, refolded and purified from inclusion bodies. The purified IL6(T23)-PE38KDEL was found to be selectively cytotoxic to IL6 receptor-positive tumor cells in vitro. IC 50 values of IL6(T23)-PE38KDEL were evaluated by MTS assay. Toxicity and maximum-tolerated dose of IL6(T23)-PE38KDEL were determined in mice. The antitumor activity of IL6(T23)-PE38KDEL was evaluated in mice with MM through intravenous injection and interventional therapy. Intravenous administration of IL6(T23)-PE38KDEL caused a significantly increased survival time in treated mice, and exhibited dose-and time-dependent antitumor effects against MM mice. Moreover, complete tumor regression was observed in 30 and 80% of mice treated intravenously and intraperitoneally, respectively, with 0.4 mg/kg/day for 10 days. These results demonstrated that the recombinant immunotoxin IL6(T23)-PE38KDEL kills IL6R-overexpressing cancer cells, and causes significant tumor regression.

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Cancer therapy with engineered monoclonal antibodies

Cited by 15 publications

References 90 publications

Immune-O-Toxins as the magic bullet for therapeutic purposes

Immune-O-Toxins as the magic bullet for therapeutic purposes

Development of monoclonal antibodies for the identification of novel invasion associated targets in human cancer

In vitro and in vivo antitumor effects of the recombinant immunotoxin IL6(T23)-PE38KDEL in multiple myeloma

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