SULM – Schweizerische Union für Labormedizin | Union Suisse de Médecine de Laboratoire | Swiss Union of Laboratory Medicine

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İlker Durak1 , Recep Çetin2 , Aslihan Avci1

1Ankara University School of Medicine, Biochemistry Department, Sıhhıye, Ankara- Turkey., 2Oncology Hospital, Department of Surgery, Ankara, Turkey

Objective: Adenosine deaminase, 5’nucleotidase and xanthine oxidase are the important enzymes in the degradation of purine nucleotides (1). In the present study, activities of purine nucleotide metabolising enzymes were measured in cancerous and non cancerous human colon tissues.
Methods: Twenty tissue samples were obtained from 10 patients with colon cancer. Of the 20 samples, 10 were removed from cancerous region and 10 from non cancerous adjacent region. Adenosine deaminase (ADA), 5’ Nucleotidase (5’NT) and xanthine oxidase (XO) enzyme activities were measured in the tissues (1,2,3).
Results: ADA and 5’NT activities were found significantly increased (8.67±1.72vs.15.46±9.15, p < 0.01 for ADA and 10.72±6.96 vs. 20.17±16.35, p < 0.01 for 5’NT) and that of XO decreased (0.043±0.020 vs. 0.021±0.008, p < 0.05) in the cancerous tissues relative to non cancerous ones.
Summary-Conclusion: Our results suggest that nucleotide catabolism and salvage pathway nucleotide synthesis are both activated in the cancerous colon tissues due to increased ADA and 5’ NT activities which lead to accelerated purine nucleotide turn-over, and to lowered XO activity which leads to accumulation of hypoxanthine which is the main substrate of hypoxanthine guanine phospohoribosyl transferase (HGPRT), the key enzyme of salvage pathway nucleotide metabolism.

References:

1. Durak I, Bedük Y, Kavutcu M, Süzer O et al. Cancer Invest 1997;15:212-16.
2. Donald WM. In: Tietz NW ed. Text Book of Clinical Chemistry. 1986:718-20.
3. Hashimato S. Anal Biochem 1974;62:425-35.

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