Biopolym. Cell. 2018; 34(1):72-81.
http://dx.doi.org/10.7124/bc.000972
Discussions
Tumors and biofilms: too much coincidences to be casual
1Verevka S. V., 1Voroshylova N. M.
  1. State institution “O. S. Kolomiychenko Institute of Otolaryngology Of National Academy of Medical Sciences of Ukraine”
    3, Zoologichna, Kyiv, Ukraine, 02000

Abstract

The existence of the majority of microorganisms in the form of three-dimensional associates on the phase interface proves the significant survivable advantages of such form of life at compare with monocellular planktonic ones. These advantages provided to biofilms a place of the most widely distributed form of life if not the dominative one. There is a strong similarity in properties of biofilms and malignant tumors that promotes considering the latter as some kind of biofilms. Such point of view facilitates understanding some features of carcinogenesis as well as the grounds for perspective directions in the prevention of metastases.
Keywords: biofilms, carcinogenesis, metastasis
Full text: (PDF, in English)

References

[1] Kornberg A. Centenary of the birth of modern biochemistry. Trends Biochem Sci. 1997;22(8):282-3.
[2] Stoodley P, Sauer K, Davies DG, Costerton JW. Biofilms as complex differentiated communities. Annu Rev Microbiol. 2002;56:187-209.
[3] Vert M, Doi Y, Hellwich K-H, Hess M, Hodge P, Kubisa P, Rinaldo M, Schue F. Terminology for biorelated polymers and applications (IUPAC Recommendations 2012). Pure Appl Chem. 2012; 84(2):377–410.
[4] Flemming HC, Wingender J, Szewzyk U, Steinberg P, Rice SA, Kjelleberg S. Biofilms: an emergent form of bacterial life. Nat Rev Microbiol. 2016;14(9):563-75.
[5] Nikolaev YuA, Plakunov VK. Biofilm – "City of Microbes" or an analogue of multicellular organisms? Microbilolgy. 2007; 76(2):125–38.
[6] Lozins'ka LM, Semchyshyn HM. [Biological aspects of non-enzymatic glycosylation]. Ukr Biokhim Zh (1999). 2012;84(5):16-37. Ukrainian.
[7] Verevka SV. Parametabolic β-aggregation of proteins: familiar mechanisms with diverse sequels. in: Ed Berhardt LV. Advances in Medicine and Biology. NY: Nova Science Publishers, 2013, 72: 29–48.
[8] Vicente Miranda H, Outeiro TF. The sour side of neurodegenerative disorders: the effects of protein glycation. J Pathol. 2010;221(1):13-25.
[9] Volinsky R, Kinnunen PK. Oxidized phosphatidylcholines in membrane-level cellular signaling: from biophysics to physiology and molecular pathology. FEBS J. 2013;280(12):2806-16.
[10] Hobley L, Harkins C, MacPhee CE, Stanley-Wall NR. Giving structure to the biofilm matrix: an overview of individual strategies and emerging common themes. FEMS Microbiol Rev. 2015;39(5):649-69.
[11] Sutherland I. Biofilm exopolysaccharides: a strong and sticky framework. Microbiology. 2001;147(Pt 1):3-9.
[12] Branda SS, Vik S, Friedman L, Kolter R. Biofilms: the matrix revisited. Trends Microbiol. 2005;13(1):20-6.
[13] Tielen P, Kuhn H, Rosenau F, Jaeger KE, Flemming HC, Wingender J. Interaction between extracellular lipase LipA and the polysaccharide alginate of Pseudomonas aeruginosa. BMC Microbiol. 2013;13:159.
[14] López D, Vlamakis H, Losick R, Kolter R. Cannibalism enhances biofilm development in Bacillus subtilis. Mol Microbiol. 2009;74(3):609-18.
[15] Abedon ST. Bacteriophage exploitation of bacterial biofilms: phage preference for less mature targets? FEMS Microbiol Lett. 2016;363(3). pii: fnv246.
[16] Cochran WL, McFeters GA, Stewart PS. Reduced susceptibility of thin Pseudomonas aeruginosa biofilms to hydrogen peroxide and monochloramine. J Appl Microbiol. 2000;88(1):22-30.
[17] Verevka SV. Formation and recognition of superficial microclusters as the integral part of processing of proteins. in: Eds. Boscoe AB, Listov CR, Protein Research Progress: New Research. NY: Nova Science Publishers, 2008:9–15.
[18] Askers J. Normal immune responses to protosoal infections. In: Ed. Dick G. Immunological aspects of infectious diseases. Lancaster: MTP Press, 1979:77–115.
[19] Kurkina T, Sambur M, Verevka S. Activating action of streptokinase and its rile in the injury of immune homeo-stasis. in: Ed. Zabolotny DI. Molecular Pathology of Proteins. N.Y.: Nova Science Publishers, 2009, 153–8.
[20] Balsalobre C, Silván JM, Berglund S, Mizunoe Y, Uhlin BE, Wai SN. Release of the type I secreted alpha-haemolysin via outer membrane vesicles from Escherichia coli. Mol Microbiol. 2006;59(1):99-112.
[21] Odenyo AA, Mackie RI, Stahl DA, White BA. The use of 16S rRNA-targeted oligonucleotide probes to study competition between ruminal fibrolytic bacteria: development of probes for Ruminococcus species and evidence for bacteriocin production. Appl Environ Microbiol. 1994;60(10):3688-96.
[22] Flemming HC. EPS-Then and Now. Microorganisms. 2016;4(4). pii: E41. Review.
[23] Chikina A, Alexandrova A. The cellular mechanisms and regulation of metastasis formation. Mol Biol. 2014; 48(2): 165–80.
[24] Alizadeh AM, Shiri S, Farsinejad S. Metastasis review: from bench to bedside. Tumour Biol. 2014;35(9):8483-523.
[25] Verevka S, Grinenko T. Pseudo-functional interactions of plasminogen: molecular mechanisms and pathologic appearance. In: Ed. Berhardt LV. Advances in medicine and biology. NY: Nova Science Publishers, 2011; 34: 35–62.
[26] Chekhun VF. Stroma – regulator of cancer cell progression. Onkologia. 2009; 11(3): 164–5.
[27] Nyberg P, Xie L, Kalluri R. Endogenous inhibitors of angiogenesis. Cancer Res. 2005;65(10):3967-79.
[28] Tykhomyrov AA, Vovchuk IL, Grinenko TV. PLASMINOGEN AND ANGIOSTATIN LEVELS IN FEMALE BENIGN BREAST LESIONS. Ukr Biochem J. 2015;87(5):103-12.
[29] Kessenbrock K, Plaks V, Werb Z. Matrix metalloproteinases: regulators of the tumor microenvironment. Cell. 2010;141(1):52-67. PubMed Central PMCID: PMC2862057.
[30] Yurchenko O, Todor I, Tryndyak V, Tregubova N, Kovtonyuk O, Solyanuk G, Kulik G, Chekhun V. Resistance of Guerin’s carcinoma cell to cisplatin: biochemical and morphological aspects. Exp Oncol. 2003; 25(1):64–8.
[31] Nosko MM, Pivnyuk VM, Solyanik GI, Kulik GI, Todor IN, Momot VY, Melnikov OR, Ponomareva OV, Chekhun VF. Biodistribution analysis of cisplatin in liposomal form in animals with cisplatin-resistant and cisplatin-sensitive carcinoma. Exp Oncol. 2010;32(1):40-3.
[32] Naleskina LA, Todor IN, Nosko MM, Lukianova NY, Pivnyuk VM, Chekhun VF. Alteration in lipid composition of plasma membranes of sensitive and resistant Guerin carcinoma cells due to the action of free and liposomal form of cisplatin. Exp Oncol. 2013;35(3):192-7.
[33] Chekhun VF, Kovtonyuk OV, Todor IN, Kulik GI. Total proteolytic activity and levels of the main proteinase inhibitors in blood plasma of mice bearing Lewis lung carcinoma upon development of resistance to cisplatin. Exp Oncol. 2005;27(4):286-9.
[34] Guo RR, Liu Y, Lu WL, Zhao JH, Wang XQ, Zhang H, Wang JC, Zhang X, Zhang Q. A recombinant peptide, hirudin, potentiates the inhibitory effects of stealthy liposomal vinblastine on the growth and metastasis of melanoma. Biol Pharm Bull. 2008;31(4):696-702.
[35] Lu Q, Lv M, Xu E, Shao F, Feng Y, Yang J, Shi L. Recombinant hirudin suppresses the viability, adhesion, migration and invasion of Hep-2 human laryngeal cancer cells. Oncol Rep. 2015;33(3):1358-64.