Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0024623 (gastric cancer)
 36,219 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Adenosine deaminase activity, the key enzyme of adenosine inactivation, was studied in slices taken endoscopically from gastric cancer and macroscopically unchanged gastric mucosa surrounding the cancer. The activity of the enzyme was measured in mucosa homogenates by determination of ammonia liberated from substrate. It was found that adenosine deaminase activity in neoplastic lesions did not differ significantly from normal mucosa and that the gastric region studied (antrum, corpus) did not have an impact. A significant difference in enzyme activity was noticed between intestinal and diffuse-type gastric carcinoma (according to Lauren's classification); the intestinal type was characterized by lower adenosine deaminase activity than was the diffuse type. Since the activity of adenosine deaminase in gastric cancer did not exhibit significant differences from normal mucosa the diagnostic value of its determination is of less importance.
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PMID:Adenosine deaminase activity in gastric cancer. 803 75

The activities of some of the enzymes participating in nucleotide metabolism were measured in cancerous and noncancerous gastric tissues from patients with gastric cancer. The enzyme activities measured were found to be higher in the cancerous tissues than in the non-cancerous tissues. Adenosine deaminase (ADA), 5'-nucleotidase (5'-NT), guanase (GUA) and cytidine deaminase (CD) activities in the cancerous tissues were 56.0 +/- 24.0, 45.0 +/- 20.0, 0.34 +/- 0.16 and 4.65 +/- 2.04, respectively. The activities in non-cancerous tissues were 13.2 +/- 6.0, 19.8 +/- 8.3, 0.12 +/- 0.06 and 1.65 +/- 0.8, respectively. Cancerous tissues consisted of 7 gastric tissues with Grade I-II and 8 tissues with Grade III-IV adeno cancer. Non-cancerous adjacent tissues were obtained from the same patients with Grade I-II cancer. There were no meaningful differences between enzyme activities of the gastric tissues with Grade I-II and Grade III-IV cancer. Enzyme activity ratios indicates that ADA activity increased by the highest amount relative to other enzyme activities in the cancerous tissues. In the correlation analysis, we found positive correlations between some of the enzyme activities in the cancerous tissues. Results suggest that increased activities of these enzymes might play a part in the accelerated nucleotide metabolism in the cancerous gastric tissues.
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PMID:Adenosine deaminase, 5'-nucleotidase, guanase and cytidine deaminase activities in gastric tissues from patients with gastric cancer. 807 77

Adenosine deaminase (ADA), 5'-Nucleotidase (5NT), Xanthine oxidase (XO), Cu-Zn Superoxide dismutase (SOD) and Catalase (CAT) activities were determined in gastric juices from patients with gastric cancer, ulcer, gastritis and from healthy subjects. Enzyme activities were given as units per ml gastric juice and units per mg protein in gastric juice. ADA, 5NT and XO activities were found lower and protein concentrations were found higher in the cancer group than controls. There was however no significant difference between Cu-Zn SOD activities of the cancer and control groups. In all groups including control one, we could not find catalase activities in most of the samples. On the other hand, ADA, 5NT activities and protein concentrations in the gastric juice were lower in the gastritis group than control group. In the ulcer group, we found higher Cu-Zn SOD and XO activities and lower 5NT activity and protein concentrations compared with control values. In an attempt to establish statistical correlations between mean enzyme activities, pH and protein concentrations in the gastric juices of the groups, we found noticeable intra and inter-correlations, which indicated possible relations between DNA and free radical metabolizing enzymes.
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PMID:Adenosine deaminase, 5'-nucleotidase, xanthine oxidase, superoxide dismutase, and catalase activities in gastric juices from patients with gastric cancer, ulcer, and atrophic gastritis. 814 35

Adenosine deaminase activity was studied in tissue slices taken endoscopically from gastric mucosa of patients with the intestinal type of gastric carcinoma. The enzyme activity was measured in mucosal homogenates by determination of ammonia liberated from substrate during 10-min incubation. It was found that: (1) the enzyme activity of de novo gastric cancer was significantly lower than that of recurrent cancer of the gastric remnant; and (2) the enzyme activity of uninvaded gastric mucosa surrounding the neoplastic lesion of non-operated stomach was significantly lower than of the gastric mucosa of partially resected stomach due to malignancy. Since the enzyme activity in gastric cancer and surrounding uninvaded gastric mucosa correlated well with the advance of neoplastic disease estimated by ultrasonography examination, we speculate that some systemic factors associated with tumor progression might be implicated in the regulation of adenosine deaminase activity.
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PMID:Adenosine deaminase activity in patients with the intestinal type of gastric carcinoma. 902 Sep 21