Abstract
We measured activities of some DNA turnover enzymes in 9 breast tissues with stage II cancer, 6 breast tissues with stage IIIa cancer, and 9 non-cancerous adjacent breast tissues from the same patients with stage II cancer. We found higher Adenosine Deaminase (ADA) and 5′-Nucleotidase (5′NT) and lower Guanase (GUA) activities in the cancerous tissues compared with the non-cancerous ones. No meaningful differences were however found between Cytidine Deaminase (CD) activities. Regarding the correlation analysis, positive correlations were established between ADA and 5′NT activities of the cancerous tissues (r = 0.45 for the tissues with stage II and r = 0.60 for the tissues with stage IIIa cancer). No meaningful correlations were however found between other enzyme activities. Relating to activity ratios, no meaningful differences were found between ADA/5′NT values in the tissues. GUA/CD ratios were however lower and the other ratios higher in the cancerous tissues.
Results indicated that ADA and 5′NT activities increased and GUA activity decreased in the cancerous breast tissues but CD activities did not change in the tissues affected. It has been suggested that increased ADA and 5′NT together with decreased GUA activities might be a physiologic attempt of the cancer cells to provide more substrates needed by cancer cells to accelerate the salvage pathway activity. Furthermore, high ADA activity might also play part in the detoxication process of high amounts of toxic adenosine and deoxyadenosine substrates produced from accelerated purine metabolism in the cancerous tissues.
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References
Lizuka H, Koizumi H, Kamikagi Ket al.: Two forms of adenosine deaminase in pig epidermis. J Dermatol 8: 91–95, 1981
Koizumi H, Lizuka H, Auyagi T, Miura Y: Characterization of adenosine deaminase from human epidermis and squamous cell carcinoma of the skin. J Inv Derm 84: 199–202, 1985
Camici M, Tozzi MG, Allergrini Set al.: Purine salvage enzyme activity in normal and neoplastic human tissues. Cancer Biochem Biophys 11: 201–209, 1990
Sufrin G, Tritsch GL, Mittelman A, Murphy GP: Adenosine deaminase in patients with carcinoma of the bladder. J Urol 119: 343–346, 1978
Durak I, Isik AÜ, Canbolat Oet al.: Adenosine deaminase, 5′ nucleotidase, superoxide dismutase and catalase activities in cancerous and non cancerous human laryngeal tissues. Free Radic Biol & Med 15: 681–684, 1993
Donofrio J, Coleman MS, Hutton JJet al.: Overproduction of adenosine deoxynucleotides in adenosine deaminase deficiency with severe combined immunodeficiency disease. J Clin Invest 62: 884–887, 1978
Hershfield MS, Kredich NM: Resistance of a adenosine kinase deficient human lymphoblastoid cell line to effects of deoxyadenosine on growth. S-adenosylhomocysteine hydrolase inactivation and dATP accumulation. Proc Natl Acad Sci 77: 4292–4296, 1980
Kim U, Baumler A, Carruthers C, Bielat Ket al.: Immunological escape mechanism in spontaneously metastasizing mammary tumors. Proc Nat Acad Sci 72: 1012–1016, 1975
Dornand J, Bonnafous JC, Favero J, Mani JCet al.: Ecto 5′nucleotidase and adenosine deaminase activities of lymphoid cells. Biochemical Medicine 28: 144–156, 1982
Durak I, Perk H, Kavutou Met al.: Adenosine deaminase, 5′Nucleotidase, xanthine oxidase, superoxide dismutase and catalase activities in cancerous and non-cancerous human bladder tissues. Free Radic Biol & Med 16: 825–831, 1994
Martin DW: Metabolism of purine and pyrimidine nucleotides. In: Martin DW, Mayes PA and Rodwell VW (eds): ‘Harper's Review of Biochemistry’ Los Altos California, Lange Medical Publications, 1983, 342–359
Thompson PW, Kirwan JR, Jones DD, Currey HHL: Serum cytidine deaminase level after withdraw of non-steroidal anti inflammatory treatment in rheumatoid arthritis. Ann Rheum Disease 47: 308–312, 1988
Guisti G: Enzyme activities. In: Bergmeyer UH (ed): ‘Methods of enzymatic analysis. Weinheim, Bergest, Verlag Chemia. 1974, 1092–1098
Donald WM: Enzymes. In: Tietz NW (ed.) Text Book of Clinical Chemistry, Philadelphia, WB Saunders Company, 1986, 718–720
Guisti G: Enzyme activities. In: Bergmeyer UH (ed). ‘Methods of enzymatic analysis’ Weinheim, Bergest, Verlag Chemia, 1974, 1087–1091
Thompson PW, James IT, Rowell L, Jones DD: Evaluation of a simple method for the measurement of cytidine deaminase in serum and comparison with a reference method. Clin Chim Acta 192: 55–60, 1990
Lowry O, Rosenbraugh N, Farr L, Randall R: Protein measurement with folin phenol reagent. J Biol Chem 182: 265–275, 1951
Ballett JJ, Insel R, Merler E, Rosen FS: Inhibition of maturation of human precursor lymphocytes by coformysin, an inhibitor of the enzyme adenosine deaminase. J Exp Med 143: 1271–1276, 1976
Havi T, Smyth JF, Allison AC, Williams SCW: Role of adenosine deaminase in lymphocyte proliferation. Clin Exp Immunol 23: 395–403, 1976
Koizumi H, Lizuka H, Aoyagi T, Miura Y: Two forms of adenosine deaminase in pig epidermitis (II). J Dermatol 9: 29–35, 1982
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Canbolat, O., Durak, I., Çetin, R. et al. Activities of adenosine deaminase, 5′-nucleotidase, guanase, and cytidine deaminase enzymes in cancerous and non-cancerous human breast tissues. Breast Cancer Res Tr 37, 189–193 (1996). https://doi.org/10.1007/BF01806500
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DOI: https://doi.org/10.1007/BF01806500