Aggregated proteins in malignant and benign neoplasms
DOI:
https://doi.org/10.32471/exp-oncology.2312-8852.vol-41-no-1.12629Keywords:
benign neoplasms, keloids, malignant tumors, polyposis, protein aggregationAbstract
Summary. Aim: To evaluate the presence of the aggregated proteins in malignant and benign neoplasms for clarifying the role of impaired protein metabolism in the formation of the altered tissues. Object and Methods: The histological specimens prepared from the operative materials of 196 patients with different forms of malignant and benign neoplasms were stained with Congo red and Thioflavin T and studied under the light and polarization microscope. Results: The various forms of β-stacked protein aggregates (β-SPA) inclusions were detected in amyloids, keloid tissue, benign polyps, and several malignant tumors. Conclusion: The formation of non-functional protein aggregates proves the complex character of the impairment of protein metabolism resulting in local or systemic accumulation of secondary protein toxins results in β-SPA formation as the self-sustaining complex of parametabolic processes. The β-SPA formation is of considerable interest since their properties lead to the impairment of the normal physiological processes in adjacent tissues ensuring the chronic course of the pathology.
References
Halliwell B, Gutteridge MC. Free Radicals in Biology and Medicine, Oxford: University Press, 2007. 851 p.
Valko M, Leibfritz D, Moncol J, et al. Free radicals and antioxidants in normal physiological functions and human disease. Int J Biochem Cell Biol 2007; 39: 44–84.
Vlassara H, Bucala R, Striker L. Pathogenic effects of advanced glycosylation: biochemical, biologic, and clinical implications for diabetes and aging. Lab Invest 1994; 70: 138–51.
Vicente Miranda H, Outeiro T. The sour side of neurodegenerative disorders: the effect of protein glycation. J Pathol 2010; 221: 13–25.
Ahmed N, Thornalley P. Advanced glycation end products: what is their relevance to difbetic complications? Diabetes Obes Metab 2007; 9: 233–45.
Luthra M, Balasubramanian D. Nonenzymatic glycation alters protein structure and stability. A study of two eye lens crystallins. J Biol Chem 1993; 268: 18119–27.
Bouma B, Kroon-Batenburg L, Wu YP, et al. Glycation induces formation of amyloid cross-beta structure in albumin. J Biol Chem 2003; 278: 41810–9.
Bucciantini М, Giannoni Е, Chiti F, et al. Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases. Nature 2002; 416: 507–11.
Demchenko A. Protein folding and molecular chaperones: stochastic process under control. Biophysics 2000; 45: 404–10.
Fenton W, Horwich A. Chaperonin-mediated protein folding: fate of substrate polypeptide. Quart Rev Biophys 2003; 36: 229–56.
Popot J, Saraste M. Engineering membrane proteins. Curr Opin Biotechnol 1995; 6: 394–402.
Bechinger B. Understanding peptide interactions with the lipid bilayer: a guide to membrane protein engineering. Curr Opin Chem Biol 2000; 4: 639–44.
Bartels T, Ahlstrom L, Leftin A, et al. The N-terminus of the intrinsically disordered protein α-synuclein triggers membrane binding and helix folding. Biophys J 2010; 99: 2116–24.
Wahba K, Schwab D, Brunisma R. Statistical mechanics of integral membrane protein assembly. Biophys J 2010; 99: 2217–24.
Lee C, Sun Y, Huang H. Membrane-mediated peptide conformation change from α-monomers to β-aggregates. Biophys J 2010; 98: 2236–45.
Von Heijne G. Membrane protein structure prediction. Hydrophobicity analysis and the positive-inside rule. J Mol Biol 1992; 225: 487–92.
Bogdanov M, Xie J, Dowhan W. Lipid-protein interactions drive membrane protein topogenesis in accordance with positive inside rule. J Biol Chem 2009; 284: 9637–41.
Verevka SV, Grinenko TV. Pseudo-functional interactions of plasminogen: molecular mechanisms and pathologic appearance. In: Advances in Medicine and Biology. LV Berhardt, ed. NY: Nova Science Publishers, 2011; 34: 35–62.
Koga T, Taguchi K, Kogiso M, et al. Amyloid formation of native folded protein induced by peptide-based graft copolymer. FEBS Lett 2002; 531: 137–40.
Krebs M, Wilkins D, Chung E, et al. Formation and seeding of amyloid fibrils from wild-type hen lysocyme and a peptide fragment from the beta-domain. J Mol Biol 2000; 300: 541–9.
Sideras K, Gertz M. Amyloidosis. Adv Clin Chem 2009; 47: 1–44.
Jahn T, Radford S. The Yin and Yang of protein folding. FEBS J 2005; 272: 5962–70.
Husby G, Marhaug G, Dowton B, et al. Serum amyloid A (SAA): biochemistry, genetics and the pathogenesis of AA amyloidosis. Amyloid 1994; 1: 119–37.
Kelly JW. Alternative conformations of amyloidogenuc proteins governs their behavior. Curr Opin Struct Biol 1996; 6: 11–17.
Zabolotnyi DI, Belousova AA, Zaritskaya IS, Verevka SV. Autochthonic β-aggregation of proteins: cause, molecular mechanisms, and pathologic consequences. Zhurn NAMN Ukrainy 2014; 24: 385–92 (in Ukrainian).
Verevka S, Voroshylova N. Tumors and biofilms: too much coincidences to be casual. Biopol Cell 2018; 34: 72–81.
Krebs M, Bromley E, Rogers S, Donald A. The mechanism of amyloid spherolite formation by bovine insulin. Biophys J 2005; 88: 2013–21.
Brigger D, Muckle T. Comparison of Sirius red and Congo red as stains for amyloid in animal tissues. J Histochem Cytochem 1975; 23: 84–8.
Saeed SM, Fine G. Thioflavin-T for amyloid detection. Am J Chem Pathol 1967; 47: 588–93.
Buxbaum J, Linke R. A molecular history of the amyloidosis. J Mol Biol 2012; 421: 142–59.
Merkulov GA. Course of pathohystologic techniques. Leningrad: Medicina, 1969. 424 p. (in Russian).
Puchtler H, Sweat F, Levine M. On the binding of Congo red by amyloid. J Histochem Cytochem 1962; 10: 355–64.
Chin D, Harvey R. Nasal polyps: an inflammatory condition requiring effective anti-inflammatory treatment. Curr Opin Otolaryngol Head Neck Surg 2013; 21: 23–30.
Claus L, Van Zele T, Derycke L, et al. Local inflammation in chronic upper airway disease. Curr Pharm Des 2012; 18: 2336–46.
Mason S, Joyce J. Proteolytic networks in cancer. Trends Cell Biol 2011; 21: 118–36.
Klatskin G. Non-specific green birefringence in Congo red stained tissues. Am J Pathol 1969; 56: 1–13.
Hodds J, Morgan A. Fluorescence microscopy with thioflavin-T in the diagnostics of amyloid. J Pathol Bacterial 1963; 86: 437–42.
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