L. M. Dronko¹, T. M. Lutsenko¹*, N. V. Korotkevych²,
I. O. Vovk², D. A. Zhukova², S. I. Romaniuk²,
A. A. Siromolot², A. J. Labyntsev², D. V. Kolybo²

¹National Technical University of Ukraine “Igor Sikorsky Kyiv Polytechnic Institute”, Kyiv;
²Palladin Institute of Biochemistry, National Academy of Sciences of Ukraine, Kyiv;
*e-mail: lutsenko.tetiana@lll.kpi.ua

Received: 06 August 2024; Revised: 18 September 2024;
Accepted: 07 October 2024; Available on-line: 28 October 2024

The diphtheria toxin receptor on sensitive mammalian cells is known as the membrane anchored precursor of heparin-binding EGF-like growth factor (HB-EGF). When the precursor is cleaved by metalloproteinases, a soluble form (sHB-EGF) is formed that can bind to the EGF receptors, resulting in activation of signaling pathways that regulate cell proliferation, differentiation, migration, and inhibition of apoptosis. The ability of HB-EGF to cause both positive and negative consequences for organism underscores the complexity of its biological functions and the need for a nuanced understanding of its role in health and disease. In this review the data on the HB-EGF structure, biological activity, involvement in the mechanism of diphtheria toxin action, wound healing, tumor progression as well as the methods of HB-EGF delivery are summarized.