Have a personal or library account? Click to login
Proteolytic parameter changes in the plasma of patients with bladder cancer – depending on tumor stage Cover

Proteolytic parameter changes in the plasma of patients with bladder cancer – depending on tumor stage

Open Access
|Jun 2020

References

  1. 1. Ploeg M, Aben KK, Kiemeney LA. The present and future burden of urinary bladder cancer in the world. World J Urol. 2009;27(3):289-93.10.1007/s00345-009-0383-3269432319219610
  2. 2. Murta-Nascimento C, Schmitz-Dräger BJ, Zeegers MP, Kogevinas G, Steineck M, Real FX, Malats N. Epidemiology of urinary bladder cancer: from tumor development to patient’s death. World J Urol. 2007;25:285-9510.1007/s00345-007-0168-517530260
  3. 3. Aggarwal N, Sloane BF. Сathepsin B: multiple roles in cancer. Proteomics Clin Appl. 2014;8(5-6):427-37.10.1002/prca.201300105420594624677670
  4. 4. Wolf K, Friedl P. Extracellular matrix determinants of proteolytic and non-proteolytic cell migration. Trends Cell Biol. 2011;21(12):736-44.10.1016/j.tcb.2011.09.00622036198
  5. 5. Heutinck KM, Berge IJ, Hack CE, Hamann J, Rowshani AT. Serine proteases of the human immune system in health and disease. Mol Immunol. 2010;47(11-12):1943-5510.1016/j.molimm.2010.04.02020537709
  6. 6. Hummel BC. Amodified spectrophotometric determination of chymotrypsin, trypsin and thrombin. Can J Biochem and Physiol. 1959;37:1393-9.10.1139/o59-157
  7. 7. Nartykova VF, Paskhina TS. Unified method for determining the activity of α1-antitrypsin and α2-macroglobulin in serum (plasma) of human blood. Questions Med Chem. 1979;25(4):494-9.
  8. 8. Nikolaichik VV, Moin VM, Kirasky VV. A method for the detection of “meddle-size molecules”. Lab Delo. 1993;10:11-8.
  9. 9. Hoffman BD, Grashoff C, Schwartz MA. Dynamic molecular processes mediate cellular mechanotransduction. Nature. 2011;475:316-2310.1038/nature10316644968721776077
  10. 10. Pranjol MZ, Gutowski N, Hannemann M, Whatmore J. The potential role of the proteases cathepsin D and cathepsin L in the progression and metastasis of epithelial ovarian cancer. Biomolecules. 2015;5(4):3260-79.10.3390/biom5043260469327726610586
  11. 11. Wojtukiewicz MZ, Hempel D, Sierko E, Tucker SC, Honn KV. Protease-activated receptors (PARs)--biology and role in cancer invasion and metastasis. Cancer Metastasis Rev. 2015;34(4):775-96.10.1007/s10555-015-9599-4466121826573921
  12. 12. Pavón MS, Arroyo-Solera I, Céspedes MV, Casanova I, León X, Mangues R. Silencing of plasminogen activator inhibitor-1 suppresses colorectal cancer progression and liver metastasis. Surgery. 2015;158(6):1704-13.10.1016/j.surg.2015.04.05326275833
  13. 13. Mason SD, Joyce JA. Proteolytic networks in cancer. Trends Cell Biol. 2011;21(4):228-37.10.1016/j.tcb.2010.12.002384071521232958
  14. 14. Ulrich D, Ulrich F, Unglaub F, Piatkowski A, Pallua N. Matrix metalloproteinases and tissue inhibitors of metalloproteinases in patients with different types of scars and keloids. J Plast Reconstr Aesthet Surg. 2010;63(6):1015-21.10.1016/j.bjps.2009.04.02119464975
  15. 15. Rakashanda S, Rana F, Rafiq S, Masood A, Amin S. Role of proteases in cancer: A review. Biotechnol Mol Biol Rev. 2012;7(4):90-101.10.5897/BMBR11.027
  16. 16. Anariba DEI. Alpha1-Antitrypsin Deficiency. Medscape Reference. 2017. Available online at http://emedicine.medscape.com/article/295686-overview. Accessed February 2017.
  17. 17. El-Akawi ZJ, Nusier MK, Sawalha DH. Alpha-1 antitrypsin genotypes in breast cancer patients. J Health Sci. 2008;54(4):493-6.10.1248/jhs.54.493
  18. 18. Ahmed A Rehman, Haseeb Ahsan, Fahim HK. Alpha-2-macroglobulin: A physiological guardian. J Cell Physiol. 2013;228(8):1665-75.10.1002/jcp.2426623086799
  19. 19. Ferrer IG, Marrero A, Xavier F, Gomis-Rüth, Goulas T. α2-Macroglobulins: Structure and Function. Macromolecular Protein Complexes. 2017;83:14983.
  20. 20. Scherbina IN. The study of the diagnostic value of immunoregulatory proteins to assess the functional capacity of the fetoplacental complex with intrauterine infection. Br J Educ Scient Stud. 2016;1(23):833-8.
  21. 21. Rehman AA, Ahsan H, Khan FH. Alpha-2-macroglobulin: a physiological guardian. J Cell Physiol. 2013;228:1665-75.10.1002/jcp.24266
  22. 22. Zorin NA, Zorina VN, Zorina RM. Role of proteins of the macroglobulin family in regulation of tumor growth. Ontogenez. 2006;37(1):12-9.10.1134/S1062360406010024
  23. 23. Lindner L, Hemdan NYA, Buchold M, Huse K, Bigl M, Oerlecke I, et al. α2-Macroglobulin inhibits the malignant properties of astrocytoma cells by impeding β-Catenin signaling. Ther Targets Chem Biol. 2010;70(1):277-87.10.1158/0008-5472.CAN-09-146220048078
  24. 24. Korobov V, Bolesta I, Dika A, Korobova O, Savitsky V. Optical analysis of middle-molecular mass molecules of blood of individuals suffering from myocardial ischemia. Ukr J Phys Opt. 2012;3(1):35-42.10.3116/16091833/3/1/35/2002
  25. 25. Chmielewski M, Cohen G, Wiecek A, Carrero J. The peptidic middle molecules: is a molecular weight doing the trick? Semin Nephrol. 2014;34:118-34.10.1016/j.semnephrol.2014.02.005
  26. 26. Ishchuk TV, Raetska YaB, Savchuk OM, Ostapchenko LI. Changes blood protein composition under experimental chemical burns of esophageal development in rats. Biomed Res Ther. 2015;3(4):241-9.10.7603/s40730-015-0009-x
  27. 27. Nagoev BS, Nagoeva MK. Implication of middle-mass molecule peptides of blood plasma in assessment of intoxication syndrome in patients with bacterial tonsillitis. Vestn Otorinolaringol. 2016;6:41-4.
DOI: https://doi.org/10.2478/cipms-2020-0013 | Journal eISSN: 2300-6676 | Journal ISSN: 2084-980X
Language: English
Page range: 67 - 71
Submitted on: May 28, 2019
|
Accepted on: Aug 12, 2019
|
Published on: Jun 25, 2020
Published by: Sciendo
In partnership with: Paradigm Publishing Services
Publication frequency: 4 issues per year

© 2020 Viktor Dmytryk, Tetiana Luhovska, Pavel Yakovlev, Olexiy Savchuk, Tetiana Halenova, Nataliia Raksha, Ludmila Ostapchenko, published by Sciendo
This work is licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 License.