Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.3.5 (5'-nucleotidase)
 3,167 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Biopsy specimens from 29 adenomas, 17 adenocarcinomas, and 6 synchronous adenomas in cancer patients and from uninvolved mucosa of all main segments of the large bowel were examined histologically and assayed for a series of organelle marker enzymes. Six enzymes--lactase, sucrase, alkaline phosphatase, 5'-nucleotidase, acid phosphatase, and N-acetyl-beta-D-glucosaminidase--showed less activity in adenomas than in adjacent uninvolved mucosa and in specimens from controls. Cancer tissue had higher gamma-glutamyltransferase and lower lactase, alkaline and acid phosphatases, and N-acetyl-beta-D-glucosaminidase activities than specimens from uninvolved mucosa in cancer patients and control patients. Enhanced alkaline phosphatase and N-acetyl-beta-D-glucosaminidase activities were seen in uninvolved mucosa of cancer patients as compared with those of adenoma and control patients. Evidence has been found for multienzyme analysis to identify adenomas with signs of malignant transformation and carcinomas with poor prognosis.
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PMID:Enzyme activities in biopsy specimens from large-bowel mucosa in colorectal adenomas and carcinomas. 362 77

The distribution of a series of mucosal enzymes along the large bowel was studied by analysis of homogenized biopsy specimens from five different segments, obtained from 20 control patients. The activities varied significantly between the segments for the membrane enzymes lactase (p less than 0.005), alkaline phosphatase (p less than 0.0005), leucyl-beta-naphthylamidase (p less than 0.0001), and 5'-nucleotidase (p less than 0.001) and the mitochondrial enzyme monoamine oxidase (p less than 0.0005) when tested by analysis of variance modified for repeated measurements. When paired comparisons between segments were evaluated, the enzyme activities of the proximal large bowel were significantly higher than those of distal segments. The levels of sucrase, neutral-alpha-glucosidase, gamma-glutamyltransferase, and lysosomal enzymes remained unchanged throughout the large intestine, as did the protein to DNA ratio. The results are compatible with the theory that different segments of the large bowel have different functions.
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PMID:Longitudinal distribution of mucosal enzymes in the human large bowel. 377 57

A series of mucosal enzymes were estimated by analysis of homogenized biopsy specimens from the lower duodenal flexure, obtained from 10 large-bowel carcinoma patients, 15 patients with morbid obesity, and 15 controls. In 11 subjects the distribution along the upper small intestine was determined. The activities of the brush border enzymes lactase (p less than 0.01), neutral-alpha-glucosidase (p less than 0.01), and alkaline phosphatase (p less than 0.05) were significantly lower in the large-bowel carcinoma patients than in the controls. In obese subjects significantly lower activities (p less than 0.05) were demonstrated for the basolateral membrane enzyme 5'-nucleotidase and the lysosomal enzymes N-acetyl-beta-D-glucosaminidase and acid beta-glucuronidase, when compared with those in controls. Compared with the enzyme levels of the duodenal bulb, significantly higher activities of a series of enzymes were demonstrated at both the lower duodenal flexure and the angle of Treitz.
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PMID:Influence of remote cancer and obesity on, and distribution of mucosal enzymes in, the upper small intestine. 377 58

Biopsy specimens from the antral and body part of the stomach were studied for a range of marker enzymes in 11 patients with superficial gastritis, 9 patients with atrophic gastritis, and 31 Billroth-II-resected patients and compared with activities found in controls with normal gastric mucosa. In the antral part of the stomach increased gamma-glutamyltransferase activity was found in superficial (p less than 0.01) and atrophic gastritis (p less than 0.05), whereas monoamine oxidase activity was decreased in superficial (p less than 0.01) and atrophic gastritis (p less than 0.05). In the body part, increased activity of gamma-glutamyltransferase (p less than 0.01) and acid-beta-glucuronidase (p less than 0.01) was found in superficial gastritis. In atrophic gastritis increased activities for lactase (p less than 0.01), alkaline phosphatase (p less than 0.05), leucyl-beta-naphthylamidase (p less than 0.05), gamma-glutamyltransferase (p less than 0.05), 5'-nucleotidase (p less than 0.01), N-acetyl-beta-D-glucosaminidase (p less than 0.05), and acid-beta-glucuronidase (p less than 0.01) were found. Specimens from the gastric remnant showed an enzyme activity pattern similar to that seen in the body in atrophic gastritis, apart from a significantly decreased monoamine oxidase activity (p less than 0.004). Specimens with dysplasia in the gastric remnant showed decreased monoamine oxidase activity when compared with specimens without dysplasia (p less than 0.01).
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PMID:Enzyme activities in human gastric mucosa in gastritis and resected stomachs. 381

The distribution of a series of marker enzymes in the gastric mucosa was studied by analysis of homogenized biopsy specimens from the lesser and greater curvature of the body and antrum, respectively, obtained from 11 control patients. The activities varied significantly between the regions for the membrane enzymes lactase (p less than 0.0001), neutral-alpha-glucosidase (p less than 0.005), alkaline phosphatase (p less than 0.01), leucyl-beta-naphthylamidase (p less than 0.005), and 5'-nucleotidase (p less than 0.0001) and the lysosomal enzymes N-acetyl-beta-D-glucosaminidase (p less than 0.0001) and acid beta-glucuronidase (p less than 0.0001), using analysis of variance modified for repeated measurements. When paired comparisons between regions were evaluated, the enzyme activities of the antral regions were significantly higher than those of the body stomach. The activities of gamma-glutamyltransferase, acid phosphatase, and the mitochondrial enzyme monoamine oxidase did not alter between regions, nor did the protein to DNA ratio. The demonstrated biochemical distinction between antrum and body of the stomach may be explained by different physiological and histological properties of the two parts.
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PMID:Enzyme activities in biopsy specimens from human gastric mucosa. 381 4

Preparations of isolated brush border plasma membrane of Hymenolepis diminuta and H. microstoma possess the following enzymatic activities: alkaline phosphohydrolase (E.C. 3.1.3.1); Type I phosphodiesterase (E.E. 3.1.4.1); ribonuclease (E.C. 3.1.4.22); adenosine triphosphatase (E.C. 3.6.1.3); and 5'-nucleotidase (E.C. 3.1.3.5). The following enzymatic activities could not be demonstrated in either membrane preparation: Type II phosphodiesterase (E.C. 3.1.4.18); cyclic adenosine-3', 5'-monophosphate phosphodiesterase (E.C. 3.1.4.17); leucine aminopeptidase (E.C. 3.4.11.1); maltase (alpha-glucosidase; E.C. 3.2.1.20); and lactase (beta-galactosidase; E.C. 3.2.1.23). These data generally agree with those of previous studies in which similar membrane-bound enzymes were demonstrated in intact (living) worms.
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PMID:A comparison of membrane-bound enzymes of the isolated brush border plasma membranes of the cestodes of Hymenolepis diminuta and H. microstoma. 628 Jan 22

Highly sensitive techniques have been used for the assay of a range of marker enzymes including lactase, sucrase, alkaline phosphatase, leucyl-beta-naphthylamidase (brush border), and 5'-nucleotidase (basolateral membrane) in jejunal biopsy homogenates from patients with adult coeliac disease with and without steatorrhoea and from a control group. The absorption of D-xylose and vitamin B12 was compared in the two groups with coeliac disease. All enzymes assayed were equally depressed in both groups of coeliac disease as compared with the controls. The absorption of D-xylose and vitamin B12 were reduced in the patients with steatorrhoea compared with those without steatorrhoea. The findings suggest that lack of steatorrhoea in some patients with coeliac disease is due to better preservation of the ileal function rather than to a less severe jejunal mucosal injury.
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PMID:Enzyme activities in jejunal biopsy samples from patients with adult coeliac disease with and without steatorrhoea. 632 31

To define reproducible conditions for the homogenization of small-intestinal biopsy samples, tissue homogenization has been studied by the use of three different homogenizers. Tissue samples of increasing wet weights (0.5-10.8 mg) were homogenized in a fixed volume (1 ml) before DNA and protein were determined. The DNA to protein ratio was calculated for all wet weights and used as a measure for reproducible homogenization. The minimum tissue wet weight needed for analysis (2 mg) was determined from the values obtained for the DNA to protein ratio. Highly sensitive techniques are described in detail for the assay of brush border (maltase, lactase, sucrase, neutral alpha-glucosidase, alkaline phosphatase, gamma-glutamyl transferase, leucyl-beta-naphthylamidase), basolateral membrane (5'-nucleotidase), and mitochondrial (succinate dehydrogenase) marker enzymes and for four acid hydrolases (acid phosphatase, acid beta-D-galactosidase, N-acetyl-beta-D-glucosaminidase, acid diesterase) in human and rat jejunal mucosa. Linear kinetics have been established for all enzyme assays. The optimal dilution of tissue homogenate for the assay of the various enzymes has been determined to enable the determination of a maximum number of enzymes in each homogenate. The range of enzyme activities in samples of human and rat jejunal mucosa has been determined.
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PMID:Enzyme activities in human and rat jejunal mucosa. 667 54

A series of marker enzymes for brush borders, basolateral membrane, and lysosomes were assayed in mucosal biopsy specimens from patients with untreated and treated coeliac disease and from controls. The brush border enzymes lactase, sucrase, neutral alpha-glucosidase, alkaline phosphatase, and leucyl-beta-naphthylamidase showed reduced activities in the untreated state and complete or partial normalization during treatment. The lysosomal marker enzyme acid phosphatase increased in activity in untreated coeliac disease and was normalized by treatment. The brush border enzyme gamma-glutamyl transferase was nearly normal in untreated patients and slightly increased in treated patients. The basolateral membrane marker, 5'-nucleotidase, was reduced both in untreated and treated patients, whereas the lysosomal marker N-acetyl-beta-glucosaminidase was normal in the untreated state and decreased during treatment. The possible pathogenetic role of the three latter enzymes in coeliac disease is discussed. The patterns of the other enzymes are suggested to be attributable to the morphologic changes in the mucosa.
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PMID:Jejunal mucosal enzymes in untreated and treated coeliac disease. 667 55

Microvillus membrane vesicles from pig small intestine, isolated by hypotonic lysis, Mg2+ aggregation of contaminants and differential centrifugation, have been further purified by immunoadsorbent chromatography. The vesicles adhere to an immunoadsorbent prepared by coupling antibodies raised against three of the principal proteins of the brush border membrane (aminopeptidase, sucrase-isomaltase and lactase) to Sepharose 4B. After the contaminants are removed by washing, the adherent vesicles are released from the immunoabsorbent by applying shear forces. The purity of the immunoadsorbed vesicles has been established by electron microscopy and by measuring the activity of marker enzymes. The enrichment factor is 1.17 +/- 0.02 for aminopeptidase and 0.70 +/- 0.05 for 5'-nucleotidase. The contamination of the preparation before immunoadsorption constitutes 10% of the membrane protein and consists mainly of basolateral membrane fragments as judged from marker enzyme determinations and the lipid composition.
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PMID:Purification of microvillus membrane vesicles from pig small intestine by immunoadsorbent chromatography. 710 46


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