Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P47989 (xanthine oxidase)
 8,633 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Adenosine produced from 5'-AMP has been proposed as a mediator of intrinsic renal regulation. The rates of 5'-AMP and adenosine metabolism are dependent on the activities of enzyme involved in purine metabolism. The activities of adenosine kinase (AK), adenosine deaminase (ADA), 5'-nucleotidase (5'-NT), AMP deaminase, xanthine oxidase and purine nucleoside phosphorylase were measured in cytosolic and membrane fractions from glomeruli, cortical tubules, medullary thick ascending limb of Henle (MTAL) and collecting duct prepared from rat kidney by combinations of sieving and sucrose density gradient centrifugation techniques. In the cytoplasm of glomeruli cells, the activity ratios of ADA/AK and AMP deaminase/5'-NT were 70 and 2.4, respectively. The highest activity of 5'-NT was found in membrane fractions of cortical tubules where it was equally distributed between luminal and antiluminal membranes. Membrane fractions of MTAL did not contain detectable amounts of adenosine deaminase activity. The highest activity of xanthine oxidase and purine nucleoside phosphorylase was in the cytoplasm fraction of glomeruli. These results suggest that deamination of AMP and adenosine may be favored in the cytoplasm of glomeruli cells. In contrast, in the extracellular space of glomeruli and especially in the cortical tubule, AMP can be converted preferentially to adenosine by 5'-NT.
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PMID:The distribution of enzymes involved in purine metabolism in rat kidney. 161 Aug 88

In this study, activity of some of the key enzymes participating in purine metabolism was measured in cancerous and noncancerous human kidney tissues from 18 patients with renal cell carcinoma. Twelve cancerous tissues were at stage T1-T2 and 6 tissues were at stage T3-T4. Adenosine deaminase (ADA) and guanase (GUA) activity was increased and xanthine oxidase (XO) activity decreased in cancerous tissues compared to noncancerous ones. No difference was, however, found between 5'-Nucleotidase (5'-NT) activity of the tissues. There were also no statistically meaningful differences between the enzyme activities of the cancerous tissues at stage T1-2 and T3-4. Results suggest that the changes observed in the activity of the enzymes participating in purine metabolism result from accelerated DNA turnover in the cancerous tissues and cells, and these changes might provide selective advantage, possibly by causing acceleration of salvage pathway activity, to the cancer cells to grow and develop more rapidly.
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PMID:Activity of the enzymes participating in purine metabolism of cancerous and noncancerous human kidney tissues. 917 54

The aim of the present study is to investigate possible effects of static magnetic field (SMF) on 5' nucleotidase (5'NT-CD73) and xanthine oxidase (XO) activities in cancerous and non-cancerous human gastric tissues in order to contribute to the elucidation of the anticancer activity of SMF. Cancerous and non-cancerous human gastric tissues removed from patients by surgical operations were used in the studies. SMF was created using two static magnets. Before and after treatment with SMF, 5'NT and XO activities in the tissue samples were measured. 5'NT activity was found to be lowered, but no significant change was observed in XO activity in the gastric tissues treated with the SMF. Our results suggest that SMF inhibits 5'NT enzyme in gastric tissues significantly. It is supposed that in addition to other proposed mechanisms, inhibition of purine catabolic activity due to inhibition of some key enzymes in the DNA turn-over like 5'NT might also play part in the anticancer activity of SMF.
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PMID:Static magnetic field inhibits 5' nucleotidase activity in cancerous and non-cancerous human gastric tissues. 2537 49