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The FASEB Journal, Vol 3, 2647-2652, Copyright © 1989 by The Federation of American Societies for Experimental Biology

RESEARCH COMMUNICATIONS

Cytotoxic activities of a fusion protein comprised of TGF alpha and Pseudomonas exotoxin

CB Siegall, YH Xu, VK Chaudhary, S Adhya, D Fitzgerald and I Pastan
Laboratory of Molecular Biology, National Cancer Institute, Bethesda, Maryland 20892.

A cDNA encoding transforming growth factor type alpha (TGF alpha) was fused to the 5' end of a gene encoding a modified form of Pseudomonas exotoxin A (PE), which is devoid of the cell recognition domain (domain Ia). The chimeric molecule, termed TGF alpha-PE40, was expressed in Escherichia coli and isolated from the periplasm or inclusion bodies depending on the construction expressed. TGF alpha-PE40 was found to be extremely cytotoxic to cells displaying epidermal growth factor (EGF) receptors. Comparison with a similar molecule in which TGF alpha was placed at the carboxyl end of PE40 demonstrated the importance of the position of the cell recognition element; TGF alpha-PE40 was found to be about 30-fold more cytotoxic to cells bearing EGF receptors than PE40-TGF alpha. In addition, TGF alpha-PE40 was shown to be extremely cytotoxic to a variety of cancer cell lines including liver, ovarian, and colon cancer cell lines, indicating high levels of EGF receptor expression in these cells.


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Copyright © 1989 by The Federation of American Societies for Experimental Biology.