Cytotoxicity and specificity of directed toxins composed of diphtheria toxin and the EGF-like domain of heregulin beta1.

@article{Landgraf1998CytotoxicityAS,
  title={Cytotoxicity and specificity of directed toxins composed of diphtheria toxin and the EGF-like domain of heregulin beta1.},
  author={Ralf Landgraf and Mark Pegram and Dennis J. Slamon and David S Eisenberg},
  journal={Biochemistry},
  year={1998},
  volume={37 9},
  pages={3220-8}
}
As a step in the design of directed toxins, aimed at cells that overexpress HER receptors, particularly breast carcinoma cells, we studied the properties of a chimera of diphtheria toxin (DT) and heregulin beta1. The EGF-like growth hormone heregulin is a ligand for the HER3 and HER4 receptors and their heterodimers with HER2. The 60-residue EGF-like domain (hrg) of heregulin elicits a biological response and binds to these receptors primarily through its N terminus. We tested a fusion protein… CONTINUE READING