ADENOSINE-DEAMINASE, 5'NUCLEOTIDASE, XANTHINE-OXIDASE, SUPEROXIDE-DISMUTASE, AND CATALASE ACTIVITIES IN CANCEROUS AND NONCANCEROUS HUMAN BLADDER TISSUES

Citation
I. Durak et al., ADENOSINE-DEAMINASE, 5'NUCLEOTIDASE, XANTHINE-OXIDASE, SUPEROXIDE-DISMUTASE, AND CATALASE ACTIVITIES IN CANCEROUS AND NONCANCEROUS HUMAN BLADDER TISSUES, Free radical biology & medicine, 16(6), 1994, pp. 825-831
Citations number
40
Categorie Soggetti
Biology
ISSN journal
08915849
Volume
16
Issue
6
Year of publication
1994
Pages
825 - 831
Database
ISI
SICI code
0891-5849(1994)16:6<825:A5XS>2.0.ZU;2-J
Abstract
Activities of adenosine deaminase (ADA), 5'nucleotidase (5NT), xanthin e oxidase (XO), superoxide dismutase (SOD), and catalase (CAT) enzymes were measured in cancerous and cancer-free adjacent bladder tissues f rom 36 patients with bladder cancer and in control bladder tissues fro m 9 noncancer patients. Increased ADA and decreased XO, SOD, and CAT a ctivities were found in cancerous bladder tissues compared with those of cancer-free adjacent tissues and of control bladder tissues. Differ ences were also found between enzyme activities in the bladder of diff erent disease stages and grades. In the cancerous tissues, only positi ve intracorrelations were found, but in the cancer-free adjacent tissu es and control tissues, both positive and negative correlations were e stablished between enzyme activities. Results suggested that purine me tabolism and salvage pathway activity of purine nucleotides were accel erated in the cancerous human bladder tissues via increased ADA and de creased XO activities, probably together with changes in some other re lated enzyme activities and, free radical metabolising-enzyme activiti es were depressed in cancerous bladder tissues, which indicated exposu re of cancerous tissues to more radicalic stress.