Identyfikatory
Warianty tytułu
Proteases: significance, role and determination
Języki publikacji
Abstrakty
Proteazy są związkami, które odgrywają bardzo istotną rolę w ludzkim organizmie. Regulują one wiele procesów przebiegających także w innych żywych organizmach, również w wirusach, bakteriach i pasożytach. Ich zwiększona lub obniżona ilość może wskazywać na nieprawidłowości w orgaznizmie, takie jak: rozwój zapalenia, nowotwory, nadciśnienie. W artykule opisano najistotniejsze z ludzkich proteaz, ich znaczenie, rolę w organizmie oraz pokrótce metody oznaczania.
Proteases are compounds that play an important role in the human body. They regulate many processes inside the living organisms, also in viruses, bacteria and parasites. Their increased or decreased level may indicate irregularities in the body, such as: the development of inflammation, cancer and others like hypertension. This article describes the most important of human proteases, their significance, roles in the organism and shortly methods of determination.
Czasopismo
Rocznik
Tom
Strony
81--88
Opis fizyczny
Bibliogr. 71 poz.
Twórcy
autor
- Zakład Elektrochemii, Instytut Chemii, Uniwersytet w Białymstoku, Białystok
autor
- Zakład Elektrochemii, Instytut Chemii, Uniwersytet w Białymstoku, Białystok
Bibliografia
- 1. S., Sánchez L. M., Overall, C. M., López-Otín, C.: Human and mouse proteases: a comparative genomic approach. Nat. Rev. Genet., 2003, 4, 544–58.
- 2. Hyperlink “http://www.enzyme-database.org/contents.php” ExploreEnzthe Enzyme database 11.09. 2014.
- 3. Gorodkiewicz E., Regulska E.: SPR Imaging Biosensor for Aspartyl Cathepsins: Sensor Development and Application for Biological Material. Protein Pept. Lett., 2010, 17, 1148–54.
- 4. Cottam D. W., Rees R. C.: Regulation of matrix metalloproteinases: their role in tumor invasion and metastasis. Int. J. Oncol., 1993, 2, 861–72.
- 5. Mignatti P., Rifkin D. B.: Biology and biochemistry of proteinases in tumor invasion. Phys. Rev., 1993, 73, 161–95.
- 6. Ferrier C. M., Van Muijen G. N. P., Ruiter D. J.: Proteases in cutaneous melanoma. Ann. Med. 1998, 30, 431–42.
- 7. Gołąb J., Jakóbisiak M., Lasek W., Stokłosa T.: Immunologia. PWN, 2007, 88, 247–249, 480.
- 8. Budihardjo I., Oliver H., Lutter M., Luo X., Wang X.: Biochemical pathways of caspase activation during apoptosis. Annu. Rev. Cell. Dev. Biol. 1999, 15, 269–90.
- 9. McIlwain D. R., Berger T., Mak T. W.: Caspase Functions in Cell Death and Disease. Cold Spring. Harb. Perspect. Biol., 2013, 1, 1–28.
- 10. Droga-Mazovec G., Bojic L., Petelin A., Ivanova S., et al: Cysteine cathepsins trigger caspase-dependent cell death through cleavage of bid and antiapoptotic bcl-2 homologue. J. Biol. Chem., 2008, 283, 19140–150.
- 11. Gorodkiewicz E.: Surface Plasmon Resonance Imaging sensor for cathepsin determination based on immobilized Cystatin. Protein Pept. Lett., 2009, 16, 1379–1385.
- 12. Broker L. E., Kruyt F. A. E., Giaccone G.: Cell Death Independent of Caspases: A Review. Clin. Cancer. Res., 2005, 11, 3155-62.
- 13. Szajda S. D., Zalewska, B., Michalak K., Skrzydlewski Z.: Cathepsin D activity in women in cases of uterine fibroids. Contemp. Oncol., 2004, 8, 266–68.
- 14. Szajda S. D., Roszkowska-Jakimiec W., Snarska J., Zwierz K.: Cathepsin D activity in serum and urine of patients with colorectal cancer. Contemp. Oncol., 2006, 10, 321–23.
- 15. Garcia M., Derocq D., Pujol P., Rochefort H.: Overexpression of transfected cathepsin D in transformed cells increases their malignant phenotype and metastatic potency. Oncogene, 1990, 5, 1809–14.
- 16. Szajda S. D., Jankowski M., Zalewska B., Kożuszko B., Gabrylewski W., Skrzydlewski Z.: The cancer procoagulant activity of cathepsin D in breast cancer cases. Contemp. Oncol., 2004, 8, 132–35.
- 17. Lodice A. A.: The inhibition by pepstatin of cathepsin D and autolysis of dystrophic muscle. Life Sci. 1976, 19, 1351–58.
- 18. Warwas M., Turowska E.: The importance of cathepsin D in the diagnosis of cancer. Postepy Hig. Med. Dosw., 1993, 47, 277–88.
- 19. Sukoh N., Abe S., Ogura S., Isobe H., Takekawa H., Inoue K., Kawakami Y.: Immunohistochemical study of cathepsin B. Prognostic significance in human lung cancer. Cancer, 1994, 1, 46–51.
- 20. Wyrwińska A., Torliński L.: Cystatin and cysteine proteases in cancer. Part I. Diagnostic and prognostic value of the determination of Cystatin and/ or cysteine proteases. Now. Lek., 2003, 72, 228–23.
- 21. Sinha A. A., Quast B. J., Wilson M. J., Fernandes E. T., Reddy P. K., Ewing S. L., Gleason D. F.: Prediction of pelvic lymphnode metastasis by the ratio of cathepsin B to stefin A in patients with prostate carcinoma. Cancer, 2002, 15, 3141–9
- 22. Levicar N., Strojnik T., Kos J., Dewey R. A., Pilkington G. J., Lah T. T.: Lysosomal enzymes, cathepsins in brain tumour invasion. J. Neuro. Oncol., 2002, 58, 21–32;
- 23. Gorodkiewicz E., Regulska E., Wojtulewski K.: Development of an SPR imaging biosensor for determination of cathepsin G in saliva and white blood cell. Microchim. Acta, 2011, 173, 407–13.
- 24. Kudo T., Kigoshi H., Hagiwara T., Takino T., Yamazaki M., Yui. S.: Cathepsin G, a Neutrophil Protease, Induces Compact Cell-Cell Adhesion in MCF-7 Human Breast Cancer Cells. Mediators Inflam., 2009, 2009, 1–11.
- 25. Korkmaz B., Horwitz M. S., Jenne D. E., Gauthier F.: Neutrophil Elastase, Proteinase 3, and Cathepsin G as Therapeutic Targets in Human Diseases. Pharmacol. Rev., 2010, 62, 726–759.
- 26. Kierszenbaum A. L.: Histology and cell biology: an introduction to pathology. Mosby Elsevier 2007, 596.
- 27. Imai T., Miyazaki H., Hirose S., Hori H., Hayashi T., et al.: Cloning and sequence analysis of cDNA for human renin precursor. Proc. Nat. Acad. Sci. USA., 1983, 80, 7405–9.
- 28. Hyperlink “http://www.rcsb.org/pdb/101/motm.do?momID=6” Proteine data bank- HIV-1 protease, 24.09.2014.
- 29. Gulnik S., Erickson J. W., Xie D:HIV protease: enzyme function and drug resistance. Vitam. Horm., 2000, 58, 213–56.
- 30. Moore J. P., Stevenson M.: New targets for inhibitors of HIV-1 replication. Nat. Rev. Mol. Cell Biol. 2000, 1, 40–9.
- 31. Eron J. J.: HIV-1 Protease Inhibitors. Clin. Infect. Dis., 2000, 30, 160–70.
- 32. Lawitz E., Sulkowski M., Jacobson I., Kraft W. K., Maliakkal B., et al: Characterization of vaniprevir, a hepatitis C virus NS3/4A protease inhibitor, in patients with HCV genotype 1 infection: Safety, antiviral activity, resistance and pharmacokinetics. Antiviral Res., 2013, 99, 214–20.
- 33. Li X., Zhang Y. K., Liu Y., Zhang S., Ding C. Z., Zhou Y., et al: Synthesis of new acylosulfamoyl benzoxaboroles as potent inhibitors of HCV NS3 protease. Bioorg. Med. Chem. Lett., 2010, 20, 7493–97.
- 34. Giombini E., Zaccaro P., Selleri M., Rozera G., Abbate I.: Extent of HCV NS3 protease variability and resistance- associated mutations assessed by next generation sequencing in HCV monoinfected and HIV/HCV coinfected patients. Virus Res., 2013, 177, 205–8.
- 35. Fatima K., Tahir M., Qadri I.: Development of robust in vitro serine protease assay based on recombinant Pakistani HCV NS3-4A protease. Virus Res., 2011, 160, 230–7.
- 36. Franco S., Clotet B., Martínez M. A.: A wide range of NS3/4A protease catalytic efficiencies in HCV- infected individuals. Virus Res., 2008, 131, 260–70.
- 37. Chase R., Skelton A., Xia E., Curry S., Liu S., McMonagle P., Huang H. C., Tong X.: A novel HCV NS3 protease mutation selected by combination treatment of the boceprovir and NS5B polymerase inhibitors. Antiviral Res., 2009, 84, 178–184.
- 38. Wardlaw J. M., Murray V., Berge E., del Zoppo G., Sandercock P., Lindley R. L., Cohen G.: Recombinant tissue plasminogen activator for acute ischaemic stroke: an updated systematic review and meta-analysis. Lancet 2012, 379, 2364–72.
- 39. DeMers G., Meurer W. J., Shih R., Rosenbaum S., Vilke G. M.: Tissue plasminogen activator and stroke: review of the literature for the clinician. J. Emerg. Med. 2012, 43, 1149–54.
- 40. Peters J. M., Franke W. W., Kleinschmidt J. A.: Distinct 19 S and 20 S subcomplexes of the 26 S proteasome and their distribution in the nucleus and the cytoplasm. J. Biol. Chem., 1994, 269, 7709–18.
- 41. Voges D., Zwickl P., Baumeister W.: The 26S Proteasome: A Molecular Machine Designed for Controlled Proteolysis. Annu. Review. Biochem., 1999, 68, 1015–1068.
- 42. Kostur A., Kulczyńska A., Kłoczko J.: Proteasomes– a new target for anticancer therapy. Acta Hematol. Pol., 2010, 41, 261–269
- 43. Hyperlink“http://www.ihcworld.com/_intro/intro.htm”IHCWorld- Immunohistochemistry, 17.11.2014
- 44. Li T., Huang S., Dong M., Gui Y., Wu D.: Prognostic impact of SUMO-specific protease 1 (SENP1) in prostate cancer patients undergoing radical prostatectomy. Urol. Oncol.- Semi. O. I., 2013, 31, 1539–1545
- 45. Martins P. R., Nascimento R. D., Lisboa A. S., Martinelli P. M., Reis D.: Neuroimmunopathology of Trypanosoma cruzi-induced megaoesophagus: Is there a role for mast cell proteases? Hum. Immunol., 2014, 75, 302–305.
- 46. Wang Q., Zhang S., Luo X., Hou J., Zhu X., Cai X.: Cloning and characterization of a cathepsin L-like cysteine protease from Taenia pisiformis. Vet. Parasitol., 2013, 194, 26–34.
- 47. Bando Y., Ito S., Nagai Y., Terayama R., Kishibe M., Ying-Ping Jiang Y. P., Mitrovic B., Takahashi T., Yoshida S.: Implications of protease m/neurosin in myelination during experimental demyelination and remyelination. Neurosci. Lett., 2006, 405, 175–180.
- 48. Puthiyachirakkal M., Lemerand K., Kumar D., Moore R., Philipson E., Mercer B. M., Mansour J. M., Hauguel-de Mouzon S., Moore J. J.: Thrombin weakens the amnion extracellular matrix (ECM) directly rather than through protease activated receptors. Placenta, 2013, 34, 924–931.
- 49. Creemers L. B., Hoeben K. A., Jansen D. C., Buttle D. J., Beertsez W., Everts V.: Participation of intracellular cysteine proteinases, in particular cathepsin B, in degradation of collagen in periosteal tissue explants. Matrix Biol., 1998, 16, 575–584.
- 50. Hyperlink “http://hylostet.pl/igm/article/70/” Hylostet 17.11.2014
- 51. Shin S. P., Han S. Y., Han J. E., Jun J. W., Kim J. H., Park S. C.: Expression and characterization of cathepsin L-like cysteine protease from Philasterides dicentrarchi. Parasitol. Int., 2014, 63, 359–365.
- 52. Lequin R.: Enzyme immunoassay (EIA)/ enzyme-linked immunosorbent assay (ELISA). Clin. Chem. 2005, 51, 2415– 2418.
- 53. Anuracpreeda P., Chawengkirtikul R., Tinikul Y., Poljaroen J., Chotwiwatthanakun C., Sobhon P.: Diagnosis of Fasciola gigantica infection using a monoclonal antibody-based sandwich ELISA for detection of circulating
- cathepsin B3 protease. Acta Trop., 2013, 127, 38–45.
- 54. Srip J., Brindley P. J., Srip B., Loukas A., Kaewkes S., Laha T.: Evaluation of liver fluke recombinant cathepsin B-1 protease as a serodiagnostic antigen for human opisthorchiasis. Parasitol. Int., 2012, 61, 191–195.
- 55. Tripathi P., Nair S., Singh B.P., Arora N.: Molecular and immunological characterization of subtilisin like serine protease, a major allergen of Curvularia lunata. Immunobiology, 2011, 216, 402–408.
- 56. Alaee M., Rajabi P., Sharifi Z., Farajollah M. M. Immunoreactivity assessment of hepatitis C virus NS3 protease and NS5A proteins expressed in TOPO cloning system; J. Microbiol. Immunol. Inf., 2014, 47, 282–291.
- 57. Hyperlink „http://www.5wszk.com.pl/nucmed/nuklearna.htm” 5 Wojskowy Szpital w Karkowie ,17.11.2014
- 58. Edston E., Hage-Hamsten M.: β-Tryptase measurements post-mortem in anaphylactic deaths and in controls. Forensic Sci. Int., 1998, 93, 135–142.
- 59. Grasser E. K., Goswami N., Rössler A., Vrecko K., Hinghofer-Szalkay H.: Hemodynamic and neurohormonal responses to extreme orthostatic stress in physically fit young adults: Acta Astronaut., 2009, 64, 688–696.
- 60. Iervasi A., Zucchelli G. C., Turchi S., Emdin M., Passino C., Ripoli A., Clerico A.: Analytical and clinical performance of an automated chemiluminescent immunoassay for direct renin measurement: comparison with PRA and aldosterone assays. Immuno-Anal. Biol. Spe., 2005, 20, 257–262.
- 61. Veyradier A., Girma J. P.: Assays of ADAMTS-13 activity. Semin. Hematol., 2004, 41, 41–47.
- 62. Marangon M., Van Sluyter S. C., Robinson E. M., Muhlack R. A., Holt H. E., Haynes P. A., Godden P. W., Smith P. A., Waters E. J.: Degradation of white wine haze proteins by Aspergillopepsin I and II during juice flash pasteurization. Food Chem., 2012, 135, 1157–1165.
- 63. Chow B. F., Peticolas M. A.: A rapid method for the determination of proteolytic activities of enzyme preparations. J. Gen. Physiol., 1948, 10, 17-24.
- 64. Schroeder J., Heckeroth A. J., Noack S., Gassel M., Mottrama J. C., Selzer P. M., Coombs G. H.: Identification of Lead Compounds Targeting the Cathepsin B-Like Enzyme of Eimeria tenella; Antimicrob. Agents Ch., 2012, 56, 1190–1201.
- 65. Lipiec T., Szmal Z. S.: Analytical chemistry of elements of instrumental analysis, textbook for students of pharmacy; National Institute of Medical Publications 1980, 524–525.
- 66. Walker M. B., Retzinger A. C., Retzinger G. S.: A turbidimetric method for measuring the activity of trypsin and its inhibition. Anal. Biochem., 2006, 351, 114–112.
- 67. Steiner G.: Surface plasmon resonance imaging; Ann. Bioanal. Chem. 2004, 379, 328-31.
- 68. Gorodkiewicz E., Regulska E., Wojtulewski K.: Development of an SPR imaging biosensor for determination of cathepsin G in saliva and white blood cells. Microchim Acta. 2011, 173, 407–413.
- 69. Laudanski P., Gorodkiewicz E., Ramotowska B., Charkiewicz R., Kuzmicki M., Szamatowicz J.: Determination of cathepsins B, D and G concentration in eutopic proliferative endometrium of women with endometriosis by the surface plasmon resonance imaging (SPRI) technique. Eur. J. Obstet. Gyn. R. B. 2013, 169, 80–83.
- 70. Gorodkiewicz E., Regulska E., Roszkowska-Jakimiec W.: Determination of the active form concentration of cathepsins D and B by SPRI biosensors. J. Lab. Diag., 2010, 46, 107–109.
- 71. Inoue Y., Mori T., Yamanouchi G., Han X., Sonoda T., Niidome T., Katayama Y.: Surface plasmon resonance imaging measurements of caspase reactions on peptide microarrays. Anal. Biochem. 2008, 375, 147–149.
Typ dokumentu
Bibliografia
Identyfikator YADDA
bwmeta1.element.baztech-68c84ab0-9614-4fde-a919-441b5604c1fd