Cross-Reacting Material 197, a Specific Inhibitor of HB-EGF, and Its Anticancer Effects
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Abstract
Genetic heterogeneity accompanied by metastasis are the most important factors which have faced cancer treatment with the challenge. Recent studies have introduced a mutant of diphtheria toxin, cross-reacting materials 197 (CRM197), as a promising new biological anticancer drug to improve cancer therapy in patients who have previously resistant to chemotherapy. The weak toxicity of CRM197 accounts for the stimulation of cell apoptosis and the antitumor effect. Increasing evidence has indicated that the expression of Heparin-binding epidermal growth factor-like (HB-EGF) growth factor enhanced in most of the cancer cells and CRM197 is the specific inhibitor of it. The current study has focused on the structure, properties, and anticancer activity of CRM197.
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5. Collier R. Understanding the mode of action of diphtheria toxin: a perspective on progress during the 20th century. Toxicon. 2001; 39:1793-1803.
6. Kaczorek M, Delpeyroux F, Chenciner N, Streeck RE, Boquet P, Tiollais P. Nucleotide sequence and expression of the diphtheria tox228 gene in Escherichia coli. Science. 1983; 221:855-858.
7. Smith W, Tai P, Murphy J, Davis B. Precursor in cotranslational secretion of diphtheria toxin. J Bacteriol. 1980; 141:184-189.
8. Greenfield L, Bjorn MJ, Horn G, et al. Nucleotide sequence of the structural gene for diphtheria toxin carried by corynebacteriophage beta. Proc Natl Acad Sci. 1983; 80:6853-6857.
9. Zhang J, Wei H, Guo X, Hu M, Gao F, Li L, et al. Functional verification of the diphtheria toxin A gene in a recombinant system. J Anim Sci Biotechnol. 2012; 3:29.
10. Shafiee F, Aucoin MG, Jahanian Najafabadi A. Targeted Diphtheria Toxin Based Therapy: A Review Article. Front Microbiol. 2019; 10:2340.
11. Chenal A, Nizard P, Gillet D. Structure and function of diphtheria toxin: from pathology to engineering. J Toxicol. 2002; 21:321-359.
12. Holger B. uptake and trafficking of protein toxins book. springer international publishing; 2017.
13. Murphy JR. Mechanism of diphtheria toxin catalytic domain delivery to the eukaryotic cell cytosol and the cellular factors that directly participate in the process. Toxins. 2011; 3:294-308.
14. Louie GV, Yang W, Bowman ME, Choe S. Crystal structure of the complex of diphtheria toxin with an extracellular fragment of its receptor. Mol cell. 1997; 1:67-78.
15. Edwards JP, Zhang X, Mosser DM. The expression of heparin-binding epidermal growth factor-like growth factor by regulatory macrophages. J Immunol. 2009; 182:1929-1939.
16. Freeman MR, Yoo JJ, Raab G, Soker S, et al. Heparin-binding EGF-like growth factor is an autocrine growth factor for human urothelial cells and is synthesized by epithelial and smooth muscle cells in the human bladder. J Clin Invest. 1997; 99:1028-1036.
17. Thorne BA, Plowman GD. The heparin-binding domain of amphiregulin necessitates the precursor pro-region for growth factor secretion. Mol Cell biol. 1994; 14:1635-1646.
18. Lanzrein M, Garred O, Olsnes S, Sandvig K. Diphtheria toxin endocytosis and membrane translocation are dependent on the intact membrane-anchored receptor (HB-EGF precursor): studies on the cell-associated receptor cleaved by a metalloprotease in phorbol-ester-treated cells. Biochem J. 1995; 310:285-289.
19. Chiron MF, Fryling CM, FitzGerald DJ. Cleavage of pseudomonas exotoxin and diphtheria toxin by a furin-like enzyme prepared from beef liver. J Biol Chem. 1994; 269:18167-18176.
20. Lemichez E, Bomsel M, Devilliers G, et al. Membrane translocation of diphtheria toxin fragment A exploits early to late endosome trafficking machinery. Mol Microbiol. 1997; 23:445-457.
21. Watson P, Spooner RA. Toxin entry and trafficking in mammalian cells. Adv Drug Deliv Rev. 2006; 58:1581-1596.
22. Papini E, Rappuoli R, Murgia M, Montecucco C. Cell penetration of diphtheria toxin. Reduction of the interchain disulfide bridge is the rate-limiting step of translocation in the cytosol. J Biol Chem. 1993; 268:1567-1574.
23. Simon NC, Aktories K, Barbieri JT. Novel bacterial ADP-ribosylating toxins: structure and function. Nat Rev Microbiol. 2014; 12:599-611.
24. Collier RJ. Diphtheria toxin: mode of action and structure. Bacteriol rev. 1975; 39:54.
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| Files | ||
| Issue | Vol 13 No 1 (2021) | |
| Section | Reviews | |
| DOI | https://doi.org/10.18502/bccr.v13i1.8828 | |
| Keywords | ||
| cross-reacting materials (CRM197) diphtheria toxin (DT) heparin-binding EGF-like growth factor (HB-EGF) epidermal growth factor receptor (EGFR) cancer | ||
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How to Cite
1.
Aminian M, Tanhapour M, Golestani A, Vaisi-Raygani A. Cross-Reacting Material 197, a Specific Inhibitor of HB-EGF, and Its Anticancer Effects. Basic Clin Cancer Res. 2021;13(1):30-50.
