THE IMPORTANCE OF URATE PATHWAY ENZYMES ACTIVITY AND ITS RELATION WITH OXIDATIVE STRESS IN PROGRESSION AND INVASION OF HUMAN COLORECTAL CANCER
Urate pathway in colon cancer
Abstract
Background and objectives: Colorectal cancer (CRC) is one of the most often diagnosed cancers and the main reason for mortality connected with tumor diseases. There is still a shortage of examination including the influence of urate pathway enzymes in progressiveness and invasion of CRC, so the present study investigated the role of Adenosine deaminase (ADA), 5′-nucleotidase (5′-NT) and Xanthine oxidase (XO) activity, concerning TBA-reactive substances (TBARS) as a marker of oxidative stress in progression and invasion of human colorectal cancer.
Materials and Methods: We took cancer tissue specimens, and also a healthy control tissue and tissue surrounding the tumor from 50 patients with primary colorectal cancers in all four TNM clinical stages of the disease. We made 10% homogenates in which we conducted the study with proper methods.
Results: The activity of ADA and XO in tumor tissue and tissue adjacent to the tumor was significantly higher when compared to healthy colon tissue. The 5′-NT is not significantly higher in carcinoma tissue. The highest activity of ADA and XO is in T2 and T3 tumor stadiums. TBARS has the highest concentration in T3 and T4 stadiums of the tumor.
Conclusions: Presented results suggest that one of the possible causes of oxidative stress in colon carcinoma could be high XO and ADA activity. It may include those enzymes in the malignant transformation of the colon epithelium, as well as in the progression and invasion of human colon cancer. In this way, the estimation of ADA and XO activity could help in assessing the margins to establish the extensiveness of colon resection. They can have significance in diagnosis, but in the prognosis of the disease also.
References
Aghaei M, Karami-Tehrani F, Salami S, Atri M. Adeno-sine deaminase activity in the serum and malignant tumors of breast cancer; the assessment of isoenzy-me ADAI and ADA2 activities. Clin Biochem 2005; 38(10):887-91. [CrossRef] [PubMed]
Al-Haj L, Khabar KSA. The intracellular pyrimidine 5'-nucleotidase NT5C3A is a negative epigenetic factor in interferon and cytokine signaling. Sci Signal 2018; 11(518):l2434. [CrossRef] [PubMed]
Balamurugan K. HIF-1 at the crossroads of hypoxia, inflammation, and cancer. Int J Cancer 2016;138: 1058-66. [CrossRef] [PubMed]
Balis EM. Adenosine deaminase and malignant cells. Ann NY Acad Sci 1985;451:142-9. [CrossRef] [PubMed]
Banihani SA. Role of uric acid in semen. Biomolecules 2018;8(3):E65. [CrossRef] [PubMed]
Bemi V, Tazzini N, Banditelli S, Giorgelli F, Pesi R, Turchi G, et al. Deoxyadenosine metabolism in a human colon-carcinoma cell line (LoVo) in relation to its cytotoxic effect in combination with deoxycofor-mycin. In J Cancer 1998;75:713-20. [CrossRef] [PubMed]
Bray F, Ferlay J, Soerjomataram I, Siegel RL, Torre LA, Jemal A. Global cancer statistics 2018: GLOBOCAN estimates of incidence and mortality worldwide for 36 cancers in 185 countries. Ca A Cancer J Clin 2018; 68:394-424. [CrossRef] [PubMed]
Canbolat O, Durak I, Cetin R, Kavutcu M, Demirci S, Oztürk S. Activities of adenosine deaminase, 5'- nucleotidase, guanase, and cytidine deaminase enzy-mes in cancerous and non-cancerous human breast tissues. Breast Cancer Res Treat 1996;37:189-93. [CrossRef] [PubMed]
Cronstein BN, Kubersky SM, Weissmann G, Hirschhorn R. Engagement of adenosine receptors inhibits hydro-genperoxide release by activated human neutrophils. Clin Immunol Immunopathol 1987;42:4276-85. [CrossRef] [PubMed]
Cummins E, Doherty G, Taylor C. Hydroxylases as therapeutic targets in inflammatory bowel disease. Laboratory Investigation 2013;93(4):378-83. [CrossRef] [PubMed]
Daddona PE, Kelley WN. Analysis of normal and mutant forms of human adenosine deaminase - a review. Mol Cell Biochem 1980;29(2):91-101. [CrossRef] [PubMed]
Di Virgilio F. Purines, purinergic receptors, and cancer. Cancer research 2012;72:5441-7. [CrossRef] [PubMed]
Durak I, Isik AU, Canbolat O, Akyol B, Kavutcu M. Adenosine deaminase, 5'-nucleotidase, xanthine oxi-dase, superoxide dismutase and catalase activities in cancerous and noncancerous human laryngeal tissues. Free Radic Biol Med 1993;15:681-4. [CrossRef] [PubMed]
Eltzschig HK, Weissmuller T, Mager A, Eckle T. Nucleo-tide metabolism and cell cell interactions. Methods Mol Biol 2006;341:73-87. [CrossRef] [PubMed]
Erkiliç K, Evereklioglu C. Çekmen M, Özkiris A, Duygulu F, Dogan H. Adenosine deaminase enzyme activity is increased and negatively correlates with catalase, superoxide dismutase and glutathione per-oxidase in patients with Behçet’s disease: original con-tributions/clinical and laboratory investigations. Mediators Inflamm 2003;12(2):107-16. [CrossRef] [PubMed]
Eroglu A, Canbolat O, Demirci S, Kocaoglu H, Eryavuz Y, Akgul H. Activities of adenosine deaminase and 5'-nucleotidase in cancerous and noncancerous human colorectal tissues. Med Oncol 2000;17(4):319-24. [CrossRef] [PubMed]
Fishman P, Bar-Yehuda S, Vagman L. Adenosine and other low molecular weight factors released by muscle cells inhibit tumor cell activities of adenosine deami-nase, 5V-nucleotidase, guanase, and cy-growth. Cancer Res 1998;58:3181-7. [PubMed]
Flamand N, Boudreault S, Picard S, Austin M, Surette ME, Plante H, et al. Adenosine, a potent natural suppressor of arachidonic acid release and leukotriene biosynthesis in human neutrophils. Am J Respir Crit Care Med 2000;161(2):S88-S94. [CrossRef] [PubMed]
Hirata BKB, Oda JMM, Guembarovski RL, Ariza CB, de Oliveira CEC, Watanabe MAE. Molecular markers for breast cancer: prediction on tumor behavior. Disease Markers 2014;2014:513158. [CrossRef] [PubMed]
Hofbrand AV, Janossy G. Enzyme and membrane markers in leukemia: recent developments. J Clin Pathol 1981;34:254-62. [CrossRef] [PubMed]
Ikegami T, Natsumeda Y, Weber G. Decreased con-centration of xanthine dehydrogenase (EC 1.1.1.204) in rat hepatomas. Cancer Res 1986;46(8):3838-41. [PubMed]
Kate J, Ingh HF, Khan PM, Bosman FT. Adenosine deaminase complexing protein (ADCP) immuno-reactivity in colorectal adenocarcinoma. Int J Cancer 1986;15:479-85. [CrossRef] [PubMed]
Kate J, Wijnen JT, Herbschleb-Voogt E, Griffionen G, Bosman FT, Khan PM. Adenosine deaminase (ADA, E.C. no 3.5.4.4.) In colorectal adenocarcinoma in man. Adv Exp Biol Med 1984;165:299-303. [CrossRef] [PubMed]
Kazemi MH, Mohseni SR, Hojjat‐Farsangi M, Anvari E, Ghalamfarsa G, Mohammadi H, et al. Adenosine and adenosine receptors in the immunopathogenesis and treatment of cancer. J Cell Physiol 2018;233(3): 2032-57. [CrossRef] [PubMed]
Kimoloi S. Modulation of the de novo purine nucleotide pathway as a therapeutic strategy in mitochondrial myopathy. Pharmacol Res 2018;138:37-42. [CrossRef] [PubMed]
Kocic G, Vlahovic P, Djordjevic V, Bjelakovic G, Koracevic D, Savic V. Effect of growth factors on the enzymes of purine metabolism in culture of regene-rating rat liver cells. Arch Physiol Biochem 1995;103: 715-19. [CrossRef] [PubMed]
Lauber K. Photometric determination of nitrogen: Wet incineration followed by formation of indophenol blue with salicylate/hypochlorite. Clin Chem 1976;67:107-10. [CrossRef] [PubMed]
Lokshin A, Tatiana R, Huang X, Zacharia LC, Jackson ED, Gorelik E. Adenosine-mediated inhibition of the cytotoxic activity and production by activated natural killer cells. Cancer Res 2006;66:7758-65. [CrossRef] [PubMed]
Longhi MS, Robson SC, Bernstein SH, Serra S, Deaglio S. Biological functions of ecto-enzymes in regulating extracellular adenosine levels in neoplastic and in-flammatory disease states. Journal of Molecular Medi-cine 2013;91:165-72. [CrossRef] [PubMed]
Lowry OH, Rosebrough NJ, Farr AL, Randall RJ. Protein measurement with the Folin phenol reagent, The Journal of Biological Chemistry 1951;193(1):265-75. [CrossRef] [PubMed]
Mahajan M, Tiwari N, Sharma R, Kaur S, Singh N. Oxidative Stress and Its Relationship With Adenosine Deaminase Activity in Various Stages of Breast Cancer. Indian Journal of Clinical Biochemistry 2013; 28(1):51-4. [CrossRef] [PubMed]
Nabavi SM, Nabavi SF, Eslami S, Moghaddam AH. In vivo protective effects of quercetin against sodium fluoride-induced oxidative stress in the hepatic tissue. Food Chem 2012;132:931-5. [CrossRef]
Nath K, Fischerder M, Hostetter HT. The role of oxi-dants in progressive renal injury. Kidney Int 1994;45: S-111—S-115. [PubMed]
Natsumeda Y, Prajda N, Donohue JP, Glover JL, Weber G. Enzymic capacities of purine de novo and salvage pathways for nucleotide synthesis in normal and neo-plastic tissues. Cancer Res 1984;44:2475-9. [PubMed]
Pederson RC, Berry AJ. Sensitive, optimised assay for serum AMP deaminase. Clin Chem 1997;23:1726-33. [CrossRef] [PubMed]
Pedley AM, Benkovic SJ. A new view into the regula-tion of purine metabolism: The purinosome. Trends Biochem Sci 2017;42:141-54. [CrossRef] [PubMed]
Piggot CO, Brady TG. Purification of multiple forms of adenosine deaminase from rabbit inetstine. Bioch Biophys Acta 1976;429:600-7. [CrossRef] [PubMed]
Pueyo M, Chen Y, Dangelo G. Regulation of vascular endothelial qrowth factor expression by cAMP in rat aortic smooth muscle cells. Exp Cell Res 1998; 238: 354-8. [CrossRef] [PubMed]
Romagnoli M, Gomez-Cabrera MC, Perrelli MG, Biasi F, Pallard´o FV, Sastre J, et al. Xanthine oxidase-induced oxidative stress causes activation of NF-kappaB and inflammation in the liver of type I diabetic rats. Free Radic Biol Med 2010;49:171-7. [CrossRef] [PubMed]
Sanfilippo O, Camici M, Tozzi MG, Turriani M, Faranda A, Ipata L, et al. Relationship between the levels of purine salvage pathway enzymes and clinical/biolo-gical aggressiveness of human colon carcinoma. Cancer Biochemistry Biophysics 1994;14(1):57-66. [PubMed]
Schulte G, Fredholm BB. Signalling from adenosine receptor to mitogen activated protein kinases. Cell Signalling 2003;15:15813-27. [CrossRef] [PubMed]
Se-Hyun O, Soon-Youn C, Hyo-Jung C, Hye-Myung R, You-Jin K, Hee-Yeon J, et al. The emerging role of xanthine oxidase inhibition for suppression of breast cancer cell migration and metastasis associated with hypercholesterolemia. FASEB Journal 2019;33(6): 7301-14. [CrossRef] [PubMed]
Sitkovsky MV, Kjaergaard J, Lukashev D, Ohta A. Hypoxia-adenosinergic immunosuppression: tumor protection by T regulatory cells and cancerous tissue hypoxia. Clinical Cancer Research 2008;14:5947-52. [CrossRef] [PubMed]
Smelcerovic Z, Veljkovic A, Kocic G, Yancheva D, Petronijevic Z, Anderluh M, et al. Xanthine oxidase inhibitory properties and anti-inflammatory activity of 2-amino-5-alkylidene-thiazol-4-ones. Chemico-Biolo-gical Interactions 2015;229:73-81. [CrossRef] [PubMed]
Solomon H, Brosh R, Buganim Y, Rotter V. Inactiva-tion of the p53 tumor suppressor gene and activation of the Ras oncogene: cooperative events in tumorige-nesis. Discovery Medicine 2010;9(48):448-54. [PubMed]
Spychala J. Tumour-promoting function of adenosine. Pharmacol Therapy 2000;87:161-73. [CrossRef] [PubMed]
Tayyar Kalcioglu M, Kizilay A, Ramazan Yilmaz H, Uz E, Gulec M, Ozturan O, et al. Adenosine deaminase, xanthine oxidase, superoxide dismutase, glutathione peroxidase activities and malondialdehyde levels in the sera of patients with head and neck carcinoma. Kulak Burun Bogaz Ihtis Derg 2004;12(1-2):16-22. [PubMed]
Veljkovic A, Hadzi-Djokic J, Sokolovic D, Cukuranovic R, Cukuranovic-Kokoris J, Basic D, et al. Local and Systemic Oxidative Stress in Balkan Endemic Ne-phropathy Is Not Associated with Xanthine Oxidase Activity. Oxid Med Cell Longev 2020;8209727. [CrossRef] [PubMed]
Veljković A, Hadži-Dokić J, Sokolović D, Bašić D, Veličković-Janković L, Stojanović M, et al. Xanthine Oxidase/Dehydrogenase Activity as a Source of Oxida-tive Stress in Prostate Cancer Tissue. Diagnostics 2020;10(9):668. [CrossRef] [PubMed]
Veljković A, Stanojević G, Branković B, Pavlović D, Stojanović I, Cvetković T, et al. Parameters of oxi-dative stress in colon cancer tissue. Acta Medica Medianae 2016;55:32-7. [CrossRef]
Viviani LG, Piccirillo E, Cheffer A, de Rezende L, Ulrich H, Carmona-Ribeiro AM, et al. Be aware of aggre-gators in the search for potential human ecto-5'-nucleotidase inhibitors. Molecules 2018;23(8):E1876. [CrossRef] [PubMed]
Weisman GA, Lustig KD, Lane E, Huang NN, Belzer I, Friedberg I. Growth inhibition of transformed mouse fibroblasts by adenine Nucleotides occurs via gene-ration of extracellular adenosine. J Biol Chem 1988; 263:12367-72. [CrossRef] [PubMed]
Wood RJ, Williams DG. Colorimetric determination of serum 5'-nucleotidase without deproteinization. Clin Chem 1981;27(3):464-5. [CrossRef] [PubMed]
Zeleznikar RJ, Heyman RA, Graeff RM, Walseth TF, Dawis SM, Butz EA, et al. Evidence for com-partmentalized adenylate kinase catalysis serving a high energy phosphoryl transfer function in rat ske-letal muscle. J Biol Chem 1990;265:300-11. [CrossRef] [PubMed]