Short‐term effect of acarbose on specific intestinal disaccharidase activities and hyperglycaemia in CBA diabetic mice
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Summary The purpose of this study was to examine the short‐term effects of 75, 100 and 150 mg of acarbose mixed in 100 g standard laboratory chow on specific intestinal disaccharidase activities and on hyperglycaemia in diabetic CBA strain mice on standard diet. The small intestine was excised and divided into three segments, from pylorus to duodenum, and two equal lengths of the jejunum and ileum of control and diabetic mice with or without added acarbose. Specific maltase and sucrase activities were determined using maltose and sucrose as substrates respectively. Increased specific activities of maltase and sucrase were detected in the intestines of CBA mice on standard laboratory diet seven days after alloxan‐induced diabetes. Feeding for 7 days with 75, 100 or 150 mg acarbose uniformly mixed in 100 g standard laboratory chow, induced a decrease in the specific maltase and sucrase activities, compared with diabetic mice on standard laboratory diet. Feeding with 75 mg acarbose mixed in 100 g standard laboratory chow caused a statistically significant decrease of maltase in the duodenum and of sucrase in duodenum and jejunum, without a antihyperglycaemic effect. Feeding with 100 or 150 mg caused statistically significant decreases in specific maltase and sucrase activities in duodenum, jejunum and ileum. An antihyperglycaemic effect was observed only in the group of diabetic mice fed with 100 mg acarbose. This indicates that the antihyperglycaemic effect of acarbose involves factors other than these, related only to its inhibitory effect on disaccharidase activities.Keywords:
Acarbose
Disaccharidase
Sucrase
Maltase
Jejunum
The small intestinal disaccharidase activity and its daily variation in the diabetic rat have not been well described. Therefore, the small intestinal disaccharidase (maltase, lactase and sucrase) activity and its daily profile were studied in streptozotocin-induced diabetic rats under physiological conditions. In diabetic rats, a similar pattern of diurnal variation of disaccharidase activity to control rats was observed, while the relationships between daily change of disaccharidase activity and that of food consumption suggested that there was a different mechanism of diurnal variation in diabetic rats. On the other hand, a significant increase of mean 24-h lactase and sucrase activities was noted in diabetic rats, while that of maltase was not significant. Using the in vitro incubation method, a significant correlation between glucose concentration and lactase or sucrase activity but not maltase activity was observed. However, insulin showed no effect on disaccharidase activity. Thus we clarified the presence of a diurnal variation of disaccharidase activity and an increase in its activity in diabetic rats. This change was suggested to be derived from high plasma glucose level.
Disaccharidase
Sucrase
Maltase
Lactase
Diurnal temperature variation
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Lycopene is known as carotenoid with antioxidant properties associated with gap‐junction formation, prevents apoptosis, atherosclerosis and cancer. This study was undertaken to determine lycopene action to nutrition processes, particularly to ontogenetic kinetic parameters of main disaccharidases of chicken jejunal brush border (BB). Lycopene consumption provide V max increasing of sucrase and maltase of chicken jejunal BB from 2nd to 4 th week and less significant decreasing of V max to 6 th week of age. Maximal values of sucrase and maltase V max during ontogenesis were stated in 2–3‐weks of chicken in control (127.3 and 12.7 nmol/mg protein per sec) and experimental (154.3 and 17.2 nmol/mg protein per sec) groups respectively. Minimal values of sucrase and maltase V max were stated in 6‐weeks of chicken in control (56.4 and 11.3 nmol/mg protein per sec) and experimental (60.1 and 13.2 nmol/mg protein per sec) groups, respectively. Also it is shown significant K m decreasing from 2nd to 6 th week of chicken in control and experimental groups for maltase and sucrase, respectively. Maltase and sucrase K i of control chicken decreased from 75 to 57 mM and from 94 to 59 mM respectively. Maltase and sucrase K i of experimental chicken decreased from 88 to 57 mM and from 93 to 66 mM respectively. Based on the received data it is concluded that lycopene affects nutrition processes in ontogenetic fashion in chicken jejunal brush border (BB).
Maltase
Disaccharidase
Sucrase
Brush border
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Disaccharidases activities in 20-day-old chick embryonic intestine were induced by the addition of sucrose, maltose, fructose and glucose to the culture medium. However, maltitol, which cannot be digested by intestinal enzymes, showed no effect on the induction of disaccharidase activity. Kinetic study of the enzymes demonstrated that the maximum velocity (Vmax) and the Michaelis constant (Km) of sucrose induced disaccharidases activities of the explants showed changes similar to those observed in the chick of same developmental stage in vivo. Namely, Vmax values of sucrase and maltase were increased. Km values of sucrase did not change, but that of maltase showed a significant decrease during development.
Disaccharidase
Sucrase
Maltase
Alpha-glucosidase
Organ culture
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Disaccharidase
Sucrase
Maltase
Alpha-glucosidase
Lactase
Husk
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Background & objectives: Malnutrition plays an important role in the intestinal absorption of nutrients. However, reports are not consistent whether intestinal enzymes are decreased in the presence of malnutrition. It is also not clear whether simultaneous presence of malnutrition and infection adds to the problem of malabsorption of nutrients. The aim of the present study was to determine intestinal functions in terms of concentrations of disaccharidase enzymes during diarrhoea and protein energy malnutrition. Methods: Concentrations of three disaccharidase enzymes, namely maltase, sucrase and lactase were measured in nine energy-restricted and five control rabbits during diarrhoea induced by rabbit diarrhoeagenic Escherichia coli (RDEC-1). Malnutrition was achieved in the rabbit model by feeding the animals for 30 days with half the amount of food fed to well-nourished control rabbits. Both the energy-restricted and the control groups were challenged by RDEC-1. Diarrhoea occurred on day 1-7 after administration of the strain. After onset of diarrhoea, both groups of rabbits were sacrificed and their intestinal mucosa was examined to determine the concentration of lactase, maltase and sucrase. Results: The energy-restricted animals and controls did not differ significantly for concentrations (units/mg proteins) of lactase (0.65 ± 0.28 vs 0.56 ± 0.17 ), maltase (6.20 ± 2.70 vs 6.47 ± 1.90) and sucrase (5.42 ± 2.30 vs 5.13 ± 1.40) measured during acute infectious diarrhoea. Interpretation & conclusion: The results suggested that the enzymatic functions of the intestinal brush border were not statistically different during diarrhoea among malnourished rabbits compared with their well-nourished counterparts.
Disaccharidase
Sucrase
Maltase
Lactase
Intestinal mucosa
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Brush border enzymatic activities (maltase, lactase and sucrase) have been determined in the ileal mucosa of rats subjected to a 30% ethanol ingestion for 3 and 5 months. The data were compared with the results obtained with control rats. Mucosal protein content after 3 months of ethanol treatment was similar to that of control rats. Maltase, lactase and sucrase specific activities in ileal mucosa were significantly decreased in ethanol-fed animals as compared to control rats. After 5 months of ethanol consumption, the protein content was decreased in ethanol-fed rats. However, no differences were found between specific activities of maltase, lactase and sucrase of ethanol-fed with respect to control rats. It is suggested that prolonged exposure of rats to ethanol results in adaptive responses to the effects of shorter periods of exposure on intestinal mucosal function.
Sucrase
Disaccharidase
Maltase
Lactase
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Summary The purpose of this study was to examine the short‐term effects of 75, 100 and 150 mg of acarbose mixed in 100 g standard laboratory chow on specific intestinal disaccharidase activities and on hyperglycaemia in diabetic CBA strain mice on standard diet. The small intestine was excised and divided into three segments, from pylorus to duodenum, and two equal lengths of the jejunum and ileum of control and diabetic mice with or without added acarbose. Specific maltase and sucrase activities were determined using maltose and sucrose as substrates respectively. Increased specific activities of maltase and sucrase were detected in the intestines of CBA mice on standard laboratory diet seven days after alloxan‐induced diabetes. Feeding for 7 days with 75, 100 or 150 mg acarbose uniformly mixed in 100 g standard laboratory chow, induced a decrease in the specific maltase and sucrase activities, compared with diabetic mice on standard laboratory diet. Feeding with 75 mg acarbose mixed in 100 g standard laboratory chow caused a statistically significant decrease of maltase in the duodenum and of sucrase in duodenum and jejunum, without a antihyperglycaemic effect. Feeding with 100 or 150 mg caused statistically significant decreases in specific maltase and sucrase activities in duodenum, jejunum and ileum. An antihyperglycaemic effect was observed only in the group of diabetic mice fed with 100 mg acarbose. This indicates that the antihyperglycaemic effect of acarbose involves factors other than these, related only to its inhibitory effect on disaccharidase activities.
Acarbose
Disaccharidase
Sucrase
Maltase
Jejunum
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Disaccharidase
Sucrase
Maltase
Lactase
Alpha-glucosidase
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Citations (14)
The objective of this study was to determine and describe the age-related changes in intestinal brush border membrane enzyme activities that occur in C57Bl/6 mice. Specifically, jejunal, duodenal, and ileal dipeptidyl peptidase IV/CD26, disaccharidase (lactase, sucrase, and maltase), and alkaline phosphatase activities were determined. A significant correlation between analyzed intestinal brush border membrane enzyme activities and animal age was found. Our study revealed that intestinal dipeptidyl peptidase IV/CD26, lactase, sucrase, maltase, and alkaline phosphatase activities decline significantly with age (p < .05). Nevertheless, the horizontal (duodenum to ileum) enzyme activity patterns are not affected by age.
Disaccharidase
Sucrase
Maltase
Lactase
Dipeptidyl peptidase
Brush border
Alpha-glucosidase
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Digestive enzymatic activities (maltase, lactase and sucrase) have been determined in the intestinal mucosa of rats subjected to a jejunoileal bypass of 45 cm. The weight and protein content of the mucosa (mg/cm) were significantly decreased in the bypassed segment and significantly increased in the unbypassed segment, as compared to control rats. Maltase, lactase and sucrase specific (U/g protein) and total activity (U/cm intestine) were significantly decreased in the bypassed jejunum, compared to sham-operated rats. In the ileum, maltase specific and total activities increased in bypassed animals while the lactase and sucrase activities remained unchanged.
Disaccharidase
Sucrase
Lactase
Maltase
Jejunum
Jejunoileal bypass
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