Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.2.1.26 (invertase)
 4,927 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

This study was performed to determine whether the addition of alanyl-glutamine (Ala-Gln) can prevent intestinal mucosal atrophy induced by standard solution of total parenteral nutrition (S-TPN). Forty-one male Sprague-Dawley rats weighing 250 g were randomly divided into four groups: group I was killed after overnight fasting; group II received S-TPN. The other groups received S-TPN supplemented with amino acids other than glutamine (group III) or supplemented with Ala-Gln 2 g/100 mL (group IV); both solutions were isocaloric and isonitrogenous. After 1 week of TPN the rats were killed, and the duodenum, proximal jejunum, mid-small bowel, and distal ileum were obtained for morphologic and functional analysis. Weight gain did not differ significantly among these four groups, and there was no difference in nitrogen balance between groups III and IV. Serum glutamine in group IV (102.8 +/- 13.3 mumol/dL) was significantly increased (p less than .05) compared with groups I, II, and III (66.2 +/- 3.9, 55.7 +/- 7.8, and 61.3 +/- 10.8 mumol/dL, respectively). Mucosal wet weight, protein, RNA, sucrase, and maltase of group IV were significantly increased (p less than .05) compared with groups II and III. Villus height was significantly increased (p less than .05) in the jejunum of group IV rats compared with groups II and III, but not in any other segments of the intestine. No significant changes were observed in crypt depth among all groups. Diamine oxidase in groups II, III, and IV was significantly decreased (p less than .05) compared with group I in all segments except for the ileum.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:The dipeptide alanyl-glutamine prevents intestinal mucosal atrophy in parenterally fed rats. 137 46

The human colon carcinoma cell line CaCo-2, grown in vitro under standard culture conditions and in the absence of differentiation inducers, spontaneously exhibits structural and functional characteristics of mature small bowel enterocytes. Differentiation is complete at late confluency. High activities of ornithine decarboxylase and diamine oxidase are present in enterocytes. Although these enzymes are involved in polyamine metabolism and therefore in cell replication, their function in small bowel epithelium remains to be defined. In this study ornithine decarboxylase and diamine oxidase activities were assessed in CaCo-2 cells at different stages of proliferation and differentiation. Diamine oxidase was also assayed in spent culture media to assess its spontaneous release by CaCo-2 cells. The trigger effect of medium replacement on ornithine decarboxylase activity was also investigated. Cell growth and cell cycle kinetics were determined by hemocytometric cell count and [3H]thymidine labeling index. Sucrase activity was assayed to evaluate brush-border functional maturation. Elevated ornithine decarboxylase activity was recorded during the replication phase (highest value 0.3 +/- 0.02 U/mg) characterized by high thymidine labeling index (43%), and was greatly enhanced by medium replacement (2.1 +/- 0.3 U/mg). Diamine oxidase activity was low in both cells and medium during the active phase of cell growth, and during the differentiation period it progressively increased (highest value 499 +/- 78 U/mg) along with sucrase activity. The high diamine oxidase activity recorded in the medium (highest value 1292 +/- 310 U/ml) and the evidence of diamine oxidase secretion through the basolateral membrane of the cells cultured on porous filters support the hypothesis of an extracellular role of intestinal diamine oxidase. The CaCo-2 cell line, which shows several analogies with small bowel enterocytes, can be proposed as an interesting in vitro model for studying many aspects of cell replication and differentiation depending on polyamine metabolism.
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PMID:Ornithine decarboxylase and diamine oxidase in human colon carcinoma cell line CaCo-2 in culture. 250

There is a reported association between administration of prenatal glucocorticoids and a decreased incidence of necrotizing enterocolitis in human infants. In rats, the degree of ischemic bowel disease correlates negatively with intestinal diamine oxidase (E.C. 1.4.3.6) activity. Since the administration of hydrocortisone, thyroxine, or phenobarbital to newborn rat pups affects the development of intestinal enzymes, we were interested in knowing whether hydrocortisone, thyroxine, or phenobarbital specifically affect intestinal diamine oxidase activity. We injected rat pups with hydrocortisone sodium succinate, 1-thyroxine pentahydrate, sodium salt, sodium phenobarbital, or the control solution on days 4, 6, 8, or 10 of life (phenobarbital, days 3, 5, 7, or 9). Pups were injected 3 days consecutively (phenobarbital, 4 days), and all were sacrificed on days 7, 9, 11, and 13. Intestinal diamine oxidase and intestinal invertase (E.C. 3.2.1.26) activities were measured. Invertase was used as a control enzyme because it is known to be induced by glucocorticoid hormones. We found that the hydrocortisone-injected pups had 10-fold higher specific activity of invertase than the saline-injected animals. Diamine oxidase activity was significantly higher in the group receiving hydrocortisone and sacrificed on days 7, 9, and 11. Enzyme activity in both the hydrocortisone-injected and saline-injected groups was equal on day 13, as was enzyme activity on all days in the thyroxine-injected and sodium hydroxide-injected groups, and the phenobarbital-injected and the saline-injected groups. Our results suggest that diamine oxidase activity may be induced by hydrocortisone, but is not affected by thyroxine or phenobarbital.
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PMID:The effect of hydrocortisone, thyroxine, and phenobarbital on diamine oxidase activity in newborn rat intestine. 310 23

Diamine oxidase (histaminase) is an enzyme found in high concentrations in the intestinal mucosa of humans and other mammalian species. We investigated whether plasma and mucosal levels of diamine oxidase activity reflect both the maturational status of the mucosa during its development in the newborn rate and the degree of mucosal damage during its injury in the adult rat. Litter mates were reared under identical conditions and killed at different ages from day 0 to day 40 after birth. Diamine oxidase in the small intestine was low at birth, increased gradually with age, reached a peak at 22 d, and then remained at normal adult levels, similar to the developmental patterns of maltase and sucrase. Plasma diamine oxidase rose in parallel with intestinal levels (n = 500, r = 0.84, P less than 0.001), reached a peak at 24 d, and then remained at normal adult levels. Diamine oxidase activity in 15 nonintestinal tissues was less than 5% of ileal mucosal activity, and no nonintestinal activities showed increase with age. Adult rat intestinal loops were perfused with hyperosmolar sodium sulfate solutions to produce selective damage to villus mucosa. With increasing mucosal damage, there was a progressive decrease in the enzyme activities studied; first, lactase levels fell, then maltase and sucrase, and finally mucosal and plasma diamine oxidase activity levels fell. The decrease in plasma diamine oxidase reflected the degree of mucosal damage (n = 29, P less than 0.04). Diamine oxidase activity is thus unique among intestinal mucosal enzymes studied to date in that circulating levels can serve as a marker of mucosal maturation and integrity.
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PMID:Diamine oxidase (histaminase). A circulating marker for rat intestinal mucosal maturation and integrity. 677 69