NDLI: Cytotoxic activity of a recombinant fusion protein between interleukin 4 and Pseudomonas exotoxin.

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Cytotoxic activity of a recombinant fusion protein between interleukin 4 and Pseudomonas exotoxin.

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Cytotoxic activity of a recombinant fusion protein between interleukin 4 and Pseudomonas exotoxin.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Ogata, M. Fitzgerald, D. J. Pastan, I. Chaudhary, V. K.
Description	Author Affiliation: Ogata M ( Laboratory of Molecular Biology, National Institutes of Health, Bethesda, MD 20892.);
Abstract	A recombinant chimeric toxin in which the cell binding domain of Pseudomonas exotoxin (PE) was replaced by murine interleukin 4 (IL-4) was produced in Escherichia coli. This chimeric protein, IL-4-PE40, was cytotoxic to murine IL-4 receptor-bearing cell lines but had little effect on human cell lines lacking receptors capable of binding murine IL-4. A mutant form of IL-4-PE40 (termed IL-4-PE40 asp553) with very low ADP-ribosylating activity displayed mitogenic activity similar to that of IL-4 rather than cytotoxic activity. Because the cytotoxic effects of IL-4-PE40 were blocked by excess IL-4 or by neutralizing antibody to IL-4 (11B11), we conclude that the cytotoxic effect of IL-4-PE40 is specifically mediated through IL-4 receptors. IL-4-PE40 could be a useful reagent for specific elimination of cells bearing IL-4 receptors.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	11
Volume Number	86
Language	English
Publisher	National Academy of Sciences
Publisher Date	1989-07-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	ADP Ribose Transferases Bacterial Toxins Cell Survival Drug Effects Exotoxins Genetics Interleukins Virulence Factors Animals B-Lymphocytes Immunology Cell Line Chimera Escherichia Coli Isolation & Purification Pharmacology Interleukin-4 Molecular Sequence Data Recombinant Fusion Proteins Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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