Cytotoxic activity of an interleukin 6-Pseudomonas exotoxin fusion protein on human myeloma cells. | Zendy

Clay B. Siegall | Zendy; V K Chaudhary | Zendy; David Fitzgerald | Zendy; Ira Pastan | Zendy

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Cytotoxic activity of an interleukin 6-Pseudomonas exotoxin fusion protein on human myeloma cells.

Author(s) -

Clay B. Siegall,

V K Chaudhary,

David Fitzgerald,

Ira Pastan

Publication year - 1988

Publication title -

proceedings of the national academy of sciences

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.011

H-Index - 771

eISSN - 1091-6490

pISSN - 0027-8424

DOI - 10.1073/pnas.85.24.9738

Subject(s) - pseudomonas exotoxin , exotoxin , cytotoxic t cell , fusion protein , biology , immunotoxin , cytotoxicity , receptor , antibody , interleukin 6 receptor , microbiology and biotechnology , cell culture , interleukin 2 , interleukin 6 , immunology , toxin , monoclonal antibody , cytokine , biochemistry , in vitro , gene , recombinant dna , genetics

A chimeric toxin composed of human interleukin 6 (IL-6) attached to a portion of Pseudomonas exotoxin (PE) devoid of its own cell recognition domain has been produced in Escherichia coli. The fusion protein (IL-6-PE40) is cytotoxic to a human myeloma cell line expressing IL-6 receptors but has no effect on IL-6 receptor-negative cells. The specificity of IL-6-PE40 cytotoxicity was demonstrated through competition with excess IL-6 and neutralization with an antibody to IL-6. IL-6-PE40 may be useful in the selective elimination of myeloma cells and other cells with high numbers of IL-6 receptors.

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