Heparin-binding EGF-like growth factor: mechanisms of biological activity and potential therapeutic applications
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 activati...
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| Format: | Article |
| Language: | English |
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National Academy of Sciences of Ukraine, Palladin Institute of Biochemistry
2024-10-01
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| Series: | The Ukrainian Biochemical Journal |
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| Online Access: | http://ukrbiochemjournal.org/wp-content/uploads/2024/10/Dronko_96_5.pdf |
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| author | L. M. Dronko T. M. Lutsenko N. V. Korotkevych I. O. Vovk D. A. Zhukova S. I. Romaniuk A. A. Siromolot A. J. Labyntsev D. V. Kolybo |
| author_facet | L. M. Dronko T. M. Lutsenko N. V. Korotkevych I. O. Vovk D. A. Zhukova S. I. Romaniuk A. A. Siromolot A. J. Labyntsev D. V. Kolybo |
| author_sort | L. M. Dronko |
| collection | DOAJ |
| description | 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. |
| format | Article |
| id | doaj-art-2a96eba2c0404b60b189779061e3b87a |
| institution | Kabale University |
| issn | 2409-4943 2413-5003 |
| language | English |
| publishDate | 2024-10-01 |
| publisher | National Academy of Sciences of Ukraine, Palladin Institute of Biochemistry |
| record_format | Article |
| series | The Ukrainian Biochemical Journal |
| spelling | doaj-art-2a96eba2c0404b60b189779061e3b87a2025-08-20T03:49:40ZengNational Academy of Sciences of Ukraine, Palladin Institute of BiochemistryThe Ukrainian Biochemical Journal2409-49432413-50032024-10-0196552010.15407/ubj96.05.005Heparin-binding EGF-like growth factor: mechanisms of biological activity and potential therapeutic applicationsL. M. Dronko0T. M. Lutsenko1https://orcid.org/0000-0002-6023-0428N. V. Korotkevych2I. O. Vovk3D. A. Zhukova 4S. I. Romaniuk5https://orcid.org/0000-0002-3900-6755A. A. Siromolot6https://orcid.org/0000-0002-2180-3545 A. J. Labyntsev7https://orcid.org/0000-0002-1793-4630D. V. Kolybo8National Technical University of Ukraine “Igor Sikorsky Kyiv Polytechnic Institute”, Kyiv, UkraineNational Technical University of Ukraine “Igor Sikorsky Kyiv Polytechnic Institute”, Kyiv, UkrainePalladin Institute of Biochemistry, National Academy of Sciences of Ukraine, Kyiv, UkrainePalladin Institute of Biochemistry, National Academy of Sciences of Ukraine, Kyiv, UkrainePalladin Institute of Biochemistry, National Academy of Sciences of Ukraine, Kyiv, UkrainePalladin Institute of Biochemistry, National Academy of Sciences of Ukraine, Kyiv, UkrainePalladin Institute of Biochemistry, National Academy of Sciences of Ukraine, Kyiv, UkrainePalladin Institute of Biochemistry, National Academy of Sciences of Ukraine, Kyiv, UkrainePalladin Institute of Biochemistry, National Academy of Sciences of Ukraine, Kyiv, UkraineThe 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.http://ukrbiochemjournal.org/wp-content/uploads/2024/10/Dronko_96_5.pdfcell proliferationdiphtheria toxinegf receptorheparin-binding egf-like growth factorsignal transductionwound healing |
| spellingShingle | L. M. Dronko T. M. Lutsenko N. V. Korotkevych I. O. Vovk D. A. Zhukova S. I. Romaniuk A. A. Siromolot A. J. Labyntsev D. V. Kolybo Heparin-binding EGF-like growth factor: mechanisms of biological activity and potential therapeutic applications The Ukrainian Biochemical Journal cell proliferation diphtheria toxin egf receptor heparin-binding egf-like growth factor signal transduction wound healing |
| title | Heparin-binding EGF-like growth factor: mechanisms of biological activity and potential therapeutic applications |
| title_full | Heparin-binding EGF-like growth factor: mechanisms of biological activity and potential therapeutic applications |
| title_fullStr | Heparin-binding EGF-like growth factor: mechanisms of biological activity and potential therapeutic applications |
| title_full_unstemmed | Heparin-binding EGF-like growth factor: mechanisms of biological activity and potential therapeutic applications |
| title_short | Heparin-binding EGF-like growth factor: mechanisms of biological activity and potential therapeutic applications |
| title_sort | heparin binding egf like growth factor mechanisms of biological activity and potential therapeutic applications |
| topic | cell proliferation diphtheria toxin egf receptor heparin-binding egf-like growth factor signal transduction wound healing |
| url | http://ukrbiochemjournal.org/wp-content/uploads/2024/10/Dronko_96_5.pdf |
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