PERSPECTIVE OF FIBRIN CAPSULE IN INHIBITION OF GROWTH AND METASTASIS OF MALIGNANT TUMORS

Kuryk M. I., Fomenko I. S.

PERSPECTIVE OF FIBRIN CAPSULE IN INHIBITION OF GROWTH AND METASTASIS OF MALIGNANT TUMORS


Show/Download

About the author:

Kuryk M. I., Fomenko I. S.

Heading:

LITERATURE REVIEWS

Type of article:

Scientific article

Annotation:

Cancer is the second leading cause of death in Ukraine, second only to cardiovascular disease. Unlike benign tumours, malignant tumours are highly aggressive, manifested by rapid growth, destruction of surrounding tissues and spread to distant areas. One of the main reasons for these differences is the different nature of tumour growth: expansive for benign and invasive for malignant ones. It is well known that benign neoplasia can malignantly transform into malignant ones. This process is considered to be one-sided. But what would the course of cancer be like if this transformation were reversed? This study aims to find an answer to this question. We propose to model the transformation of a malignant process into a benign one by forming an artificial fibrin capsule around a cancerous tumour. We assume that in this way, it is possible to turn the infiltrative growth of carcinoma into an expansive one for some time. The capsule formed around the cancerous tumour will mechanically prevent metastatic cells from entering the blood and lymphatic circulation. The RGD sequence, which is part of the molecular structure of fibrin and its precursor fibrinogen, will ensure the binding of integrins α5β1 and αVβ3 of cancer cells and thus block the formation of contacts with fibronectin molecules, which significantly reduces the invasiveness of the tumour and the number of its metastases. In addition, the capsule can partially inhibit the contact inhibition of carcinoma cells by increasing the intratumoral pressure to the new threshold. Limiting the tumour's size will reduce the progression rate of local cancer symptoms, as the last one is directly proportional to the growth rate of the tumour. Thus, this makes it possible to consider modelling a fibrin capsule around a tumour as a promising method of inhibiting the growth and metastasis of malignant tumours.

Tags:

capsule, contact inhibition, fibrin, malignant neoplasia, metastasis

Bibliography:

  1. Koten JW, Neijt JP, Zonnenberg BA, Den Otter W. The difference between benign and malignant tumours explained with the 4-mutation paradigm for carcinogenesis. Anticancer Res. 1993 Jul-Aug;13(4):1179-82.
  2.  Becker FF, editor. Cancer: a Comprehensive Treatise: 4. Biology of Tumours: Surfaces, Immunology and Comparative Pathology. New York: Plenum Press; 1975. 439 p.
  3. Haschek WM, Rousseaux CG, Wallig MA, Bolon B, Ochoa R (eds.). Haschek and Rousseaux’s Handbook of Toxicologic Pathology. 3rd ed. Elsevier Inc.; 2013. Chapter 5, Carcinogenesis: Mechanisms and Manifestations; p. 107-46. DOI: 10.1016/B978-0-12-415759-0.00001-7.
  4. Baba AI, Câtoi C. Comparative Oncology. Bucharest: The Publishing House of the Romanian Academy; 2007. Chapter 2, Carcinogenesis; Chapter 3: Tumor cell morphology.
  5. Nishida N, Yano H, Nishida T, Kamura T, Kojiro M. Angiogenesis in Cancer. Vasc Health Risk Manag. 2006 Sep;2(3):213-9. DOI: 10.2147/ vhrm. 2006.2.3.213.
  6. Malandrino A, Kamm RD, Moeendarbary E. In Vitro Modeling of Mechanics in Cancer Metastasis. ACS Biomater Sci Eng. 2018 Feb 12;4(2):294-301. DOI: 10.1021/acsbiomaterials.7b00041.
  7. Popper H. Primary tumor and metastasis—sectioning the different steps of the metastatic cascade. Transl Lung Cancer Res. 2020 Oct;9(5):2277-300. DOI: 10.21037/tlcr-20-175.
  8. Weisel JW, Litvinov RI. Fibrin Formation, Structure and Properties. Subcell Biochem. 2017 Jan 19;82:405-56. DOI: 10.1007/978-3-319- 49674-0_13.
  9. Chan LW-G, Wang X, Wei H, Pozzo LD, White NJ, Pun SH. A Synthetic Fibrin-Crosslinking Polymer for Modulating Clot Properties and Inducing Hemostasis. Sci Transl Med. 2015 Mar 4;7(277):277ra29. DOI: 10.1126/scitranslmed.3010383.
  10. Gopireddy DR, Soule E, Arif-Tiwari H, Sharma S, Kanmaniraja D, Jain K, et al. Spectrum of CT Findings Related to Bowel Adhesions Without Bowel Obstruction. J Clin Imaging Sci. 2020 Dec 10;10:80. DOI: 10.25259/JCIS_126_2020.
  11. Chekhun V, Nalieskina L, Zadvornyi T, Mushii O, Borikun T, Kunska L, et al. Markery remodeliuvannia kistkovoi tkanyny v kantserohenezi, pukhlynnii prohresii ta metastazuvanni: obgruntuvannia mozhlyvostei vykorystannia v klinichnii onkolohii. Naukovo-praktychnyi zhurnal «Onkolohiia». 2022;24(3). DOI: 10.32471/oncology.2663-7928.t-24-3-2022-g.10813. [in Ukrainian].
  12. Russo MA, Paolillo M, Sanchez-Hernandez Y, Curti D, Ciusani E, Serra M. A small-molecule RGD-integrin antagonist inhibits cell adhesion, cell migration and induces anoikis in glioblastoma cells. Int J Oncol. 2013 Jan;42(1):83-92. DOI: 10.3892/ijo.2012.1708.
  13. Schwager SC, Taufalele PV, Reinhart-Kingcorresponding CA. Cell–Cell Mechanical Communication in Cancer. Cell Mol Bioeng. 2019 Feb;12(1):1-14. DOI: 10.1007/s12195-018-00564-x.
  14. Ong MS, Deng S, Halim CE, Cai W, Tan TZ, Huang RY-J, et al. Cytoskeletal Proteins in Cancer and Intracellular Stress: A Therapeutic Perspective. Cancers (Basel). 2020 Jan;12(1):238. DOI: 10.3390/cancers12010238.
  15. Francis SL, Antonipillai J. Cytoskeletal Molecules Play a Major Role in Cancer Progression. Insights in Biomedicine. 2017 May 05;2(2):9. DOI: 10.21767/2572-5610.100009.
  16. Bearer EL. Cytoskeleton in Development. Curr Top Dev Biol. 1992;26:1-7.
  17. .Chow, AY. Cell Cycle Control by Oncogenes and Tumor Suppressors: Driving the Transformation of Normal Cells into Cancerous Cells. Nature Education. 2010;3(9):7. Available from: https://www.nature.com/scitable/ topicpage/cell-cycle-control-by-oncogenes-andtumor-14191459/.
  18. Xia S, Lim YB, Zhang Z, Wang Y, Zhang S, Lim CT, et al. Nanoscale Architecture of the Cortical Actin Cytoskeleton in Embryonic Stem Cells. Cell Rep. 2019 Jul 30;28(5):1251-67.e7. DOI: 10.1016/j.celrep.2019.06.089.
  19. Ding B, Narvaez-Ortiz HY, Singh Y, Hocky GM, Chowdhury S, Nolen BJ. Structure of Arp2/3 complex at a branched actin filament junction resolved by single-particle cryo-electron microscopy. Proc Natl Acad Sci U S A. 2022 May 31;119(22):e2202723119. DOI: 10.1073/ pnas.2202723119.
  20. Molinie N, Gautreau A. The Arp2/3 Regulatory System and Its Deregulation in Cancer. Physiol Rev. 2018 Jan 1;98(1):215-38. DOI: 10.1152/physrev. 00006.2017.
  21. Lunevicius R, Nakanishi H, Ito S, Kozaki K, Kato T, Tatematsu M, et al. Clinicopathological significance of fibrotic capsule formation around liver metastasis from colorectal cancer. J Cancer Res Clin Oncol. 2001;127(3):193-9. DOI: 10.1007/s004320000199.
  22. Gulubova MV, VlaykovaTI. Significance of tenascin-C, fibronectin, laminin, collagen IV, alpha5beta1 and alpha9beta1 integrins and fibrotic capsule formation around liver metastases originating from cancers of the digestive tract. Neoplasma. 2006;53(5):372-83.
  23. Palumbo JS, Potter JM, Kaplan LS, Talmage K, Jackson DG, Degen JL. Spontaneous hematogenous and lymphatic metastasis, but not primary tumor growth or angiogenesis, is diminished in fibrinogen-deficient mice. Cancer Res. 2002 Dec 1;62(23):6966-72.
  24. Costantini V, Zacharski LR. The role of fibrin in tumor metastasis. Cancer Metastasis Rev. 1992 Nov;11(3-4):283-90. DOI: 10.1007/ BF01307183.
  25. Costello RA, Nehring SM. Disseminated Intravascular Coagulation. StatPearls [Internet]. Treasure Island (FL): StatPearls Publishing; 2023 Jan. Available from: https://www.statpearls.com/point-of-care/20610.
  26. Chiu S-J, Ueno NT, Lee RJ. Tumor-targeted gene delivery via anti-HER2 antibody (trastuzumab, Herceptin®) conjugated polyethylenimine. J Control Release. 2004 June 18;97(2):357-69. DOI: 10.1016/j.jconrel.2004.03.019.
  27. Moasser MM. The oncogene HER2; Its signaling and transforming functions and its role in human cancer pathogenesis. Oncogene. 2007 Oct 4;26(45):6469-87. DOI: 10.1038/sj.onc.1210477.
  28. Feng Y, Spezia M, Huang S, Yuan C, Zeng Z, Zhang L, et al. Breast cancer development and progression: Risk factors, cancer stem cells, signaling pathways, genomics, and molecular pathogenesis. Genes & Diseases. 2018 June;5(2):77-106. DOI: 10.1016/j. gendis.2018.05.001.
  29. Iqbal N, Iqbal N. Human Epidermal Growth Factor Receptor 2 (HER2) in Cancers: Overexpression and Therapeutic Implications. Mol Biol Int. 2014:2014:852748. DOI: 10.1155/2014/852748.
  30. Burris HA3rd, Tibbitts J, Holden SN, Sliwkowski MX, Lewis Phillips GD. Trastuzumab emtansine (T-DM1): a novel agent for targeting HER2+ breast cancer. Clin Breast Cancer. 2011 Oct;11(5):275-82. DOI: 10.1016/j.clbc. 2011.03.018.
  31. Martin CE, List K. Cell-surface anchored serine proteases in cancer progression and metastasis. Cancer Metastasis Rev. 2019 Sep;38(3):357-87. DOI: 10.1007/s10555-019-09811-7.
  32. BelitškinShishir D, Pant SM, Munne P, Suleymanova I, Belitškina K, Hongisto H-A, et al. Hepsin regulates TGFβ signaling via fibronectin proteolysis. EMBO Reports. 2021 Nov 4;22(11):e52532. DOI: https://doi.org/ 10.15252/embr.202152532.
  33. Tzavlaki K, Moustakas A. TGF-β Signaling. Biomolecules. 2020 Mar;10(3):487. DOI: https://doi.org/10.3390%2Fbiom10030487.
  34. Cabezas F, Farfán P, Marzolo M-P. Participation of the SMAD2/3 signalling pathway in the down regulation of megalin/LRP2 by transforming growth factor beta (TGF-ß1). PLoS One. 2019 May 23;14(5):e0213127. DOI: 10.1371/journal.pone.0213127.
  35. Sadeghi S, Olevsky O, Hurvitz SA. Profiling and targeting HER2-positive breast cancer using trastuzumab emtansine. Pharmacogenomics and Personalized Medicine. 2014 Oct 15;7(default):329-38. DOI: 10.2147/ PGPM.S47524.
  36. Hunter FW, Barker HR, Lipert B, Rothé F, Gebhart G, Piccart-Gebhart MJ, et al. Mechanisms of resistance to trastuzumab emtansine (TDM1) in HER2-positive breast cancer. Br J Cancer. 2020 Mar;122(5):603-12; DOI: 10.1038/s41416-019-0635-y.
  37. Lim YJ, Lau PSC, Low SX, Li Ng S, Ong MY, Pang HM, et al. How Far Have We Developed Antibody–Drug Conjugate for the Treatment of Cancer? Drugs Drug Candidates. 2023;2(2):377-421. DOI: https://doi.org/10.3390/ ddc2020020.
  38. Jang JH, Han SJ, Kim JY, Kim KI, Lee KC, Kang CS. Synthesis and Feasibility Evaluation of a new Trastuzumab Conjugate Integrated with Paclitaxel and 89Zr for Theranostic Application Against HER2-Expressing Breast Cancers. ChemistryOpen. 2019 Apr;8(4):451-6. DOI: 10.1002/open. 201900037.
  39. Kikuchi W, Nishimura M, Kuga T, Tsuchida S, Saito T, Satoh M, et al. Fibrinogen alpha C chain 5.9 kDa fragment (FIC5.9), a biomarker for various pathological conditions, is produced in post-blood collection by fibrinolysis and coagulation factors. Clinical Proteom. 2016 Dec;13(1):27. DOI: 10.1186/s12014-016-9129-6.

Publication of the article:

«Bulletin of problems biology and medicine», 2023 Issue 4, 171, 30-41 pages, index UDC 616-006.6-018.1:612.115.1

DOI:

10.29254/2077-4214-2023-4-171-30-41

Was this article helpful?

Leave a Reply

Your email address will not be published. Required fields are marked *


The reCAPTCHA verification period has expired. Please reload the page.