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Namjun Cho - One of the best experts on this subject based on the ideXlab platform.
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new research highlights impact of chronic ingestion of white kidney beans phaseolus vulgaris l var beldia on small intestinal Disaccharidase activity in wistar rats
Toxicology reports, 2018Co-Authors: Nader Nciri, Namjun ChoAbstract:Abstract The chronic ingestion of raw or undercooked kidney beans (Phaseolus vulgaris L.) is involved in the pathogenesis of multiple organ dysfunction; the underlying mechanisms are still poorly understood. The objective of this study was to assess the gavage effects of a raw Beldia bean variety on the brush border Disaccharidase activities in the jejunal mucosa of Wistar rats. Twenty young adult male rats were randomly assigned into 2 groups of 10 rats each: Control, rats were gavaged with 300 mg of a rodent pellet flour suspension (RPFS); Experimental, rats were orogastrically fed a dose of 300 mg Beldia bean flour suspension (BBFS). Prior to determining the Disaccharidase activity by Dahlqvist method, the blood and stool specimens were collected on day 10. The sera and feces were screened for the presence of lectins by serologic and hemagglutination assays. The results showed that the brush border maltase and sucrase activities were significantly diminished but lactase activity did not undergo any change in BBFS-gavaged animals as compared with control. Preliminary immunobiochemical assays revealed the absence of lectins in the systemic circulation and feces of rats, but further work is required to prove this. Overall, the dietary administration of BBFS caused depression of the activity of the small intestinal enzymes maltase and sucrase.
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New research highlights: Impact of chronic ingestion of white kidney beans (Phaseolus vulgaris L. var. Beldia) on small-intestinal Disaccharidase activity in Wistar rats
'Elsevier BV', 2018Co-Authors: Nader Nciri, Namjun ChoAbstract:The chronic ingestion of raw or undercooked kidney beans (Phaseolus vulgaris L.) is involved in the pathogenesis of multiple organ dysfunction; the underlying mechanisms are still poorly understood. The objective of this study was to assess the gavage effects of a raw Beldia bean variety on the brush border Disaccharidase activities in the jejunal mucosa of Wistar rats. Twenty young adult male rats were randomly assigned into 2 groups of 10 rats each: Control, rats were gavaged with 300 mg of a rodent pellet flour suspension (RPFS); Experimental, rats were orogastrically fed a dose of 300 mg Beldia bean flour suspension (BBFS). Prior to determining the Disaccharidase activity by Dahlqvist method, the blood and stool specimens were collected on day 10. The sera and feces were screened for the presence of lectins by serologic and hemagglutination assays. The results showed that the brush border maltase and sucrase activities were significantly diminished but lactase activity did not undergo any change in BBFS-gavaged animals as compared with control. Preliminary immunobiochemical assays revealed the absence of lectins in the systemic circulation and feces of rats, but further work is required to prove this. Overall, the dietary administration of BBFS caused depression of the activity of the small intestinal enzymes maltase and sucrase. Keywords: Disaccharidase activity, Hemagglutination assay, Jejunum, Phytohemagglutinin (PHA), Serologic assay, White kidney bean (Phaseolus vulgaris L.
Hassan Y. Naim - One of the best experts on this subject based on the ideXlab platform.
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Characterization of Mucosal Disaccharidases from Human Intestine
MDPI AG, 2017Co-Authors: Mahdi Amiri, Hassan Y. NaimAbstract:In this study, we used a brush border membrane (BBM) preparation from human small intestine to analyze the proportion and the activity of major intestinal Disaccharidases, including sucrase-isomaltase (SI), maltase-glucoamylase (MGAM) and lactase-phlorizin hydrolase (LPH). SI, MGAM and LPH respectively constituted 8.2%, 2.7% and 1.4% of total BBM protein. The activity of SI and LPH decreased threefold after purification from the brush border membrane, which highlights the effect of membrane microdomains on the functional capacity of these enzymes. All of the Disaccharidases showed optimal activity at pH 6, over 50% residual activity between pH 5 to pH 7, and increasing activity with rising temperatures up to 45 °C, along with a stable functional structure. Therefore the enzymes can withstand mild intraluminal pH alterations with adequate function, and are able to increase their activity with elevated core body temperature. Our data provide a functional measure for characterization of intestinal Disaccharidases under different physiological and pathological conditions
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The multiple roles of sucrase-isomaltase in the intestinal physiology
Molecular and Cellular Pediatrics, 2016Co-Authors: Birthe Gericke, Mahdi Amiri, Hassan Y. NaimAbstract:Osmotic diarrhea and abdominal pain in humans are oftentimes associated with carbohydrate malabsorption in the small intestine due to loss of function of microvillar Disaccharidases. Disaccharidases are crucial for the digestion and the subsequent absorption of carbohydrates. This review focuses on sucrase-isomaltase as the most abundant intestinal Disaccharidase and the primary or induced pathological conditions that affect its physiological function. Congenital defects are primary factors which directly influence the transport and function of sucrase-isomaltase in a healthy epithelium. Based on the mutation type and the pattern of inheritance, a mutation in the sucrase - isomaltase gene may exert a variety of symptoms ranging from mild to severe. However, structure and function of wild type sucrase-isomaltase can be also affected by secondary factors which influence its structure and function either specifically via certain inhibitors and therapeutic agents or generally as a part of intestinal pathogenesis, for example in the inflammatory responses. Diagnosis of sucrase-isomaltase deficiency and discriminating it from other gastrointestinal intolerances can be latent in the patients because of common symptoms observed in all of these cases. Here, we summarize the disorders that implicate the digestive function of sucrase-isomaltase as well as the diagnostic and therapeutic strategies utilized to restore normal intestinal function.
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The multiple roles of sucrase-isomaltase in the intestinal physiology
Molecular and cellular pediatrics, 2016Co-Authors: Birthe Gericke, Amiri, Hassan Y. NaimAbstract:Osmotic diarrhea and abdominal pain in humans are oftentimes associated with carbohydrate malabsorption in the small intestine due to loss of function of microvillar Disaccharidases. Disaccharidases are crucial for the digestion and the subsequent absorption of carbohydrates. This review focuses on sucrase-isomaltase as the most abundant intestinal Disaccharidase and the primary or induced pathological conditions that affect its physiological function. Congenital defects are primary factors which directly influence the transport and function of sucrase-isomaltase in a healthy epithelium. Based on the mutation type and the pattern of inheritance, a mutation in the sucrase-isomaltase gene may exert a variety of symptoms ranging from mild to severe. However, structure and function of wild type sucrase-isomaltase can be also affected by secondary factors which influence its structure and function either specifically via certain inhibitors and therapeutic agents or generally as a part of intestinal pathogenesis, for example in the inflammatory responses. Diagnosis of sucrase-isomaltase deficiency and discriminating it from other gastrointestinal intolerances can be latent in the patients because of common symptoms observed in all of these cases.
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Long term differential consequences of miglustat therapy on intestinal Disaccharidases
Journal of Inherited Metabolic Disease, 2014Co-Authors: Mahdi Amiri, Hassan Y. NaimAbstract:Miglustat is an oral medication for treatment of lysosomal storage diseases such as Gaucher disease type I and Niemann Pick disease type C. In many cases application of Miglustat is associated with symptoms similar to those observed in intestinal carbohydrate malabsorption. Previously, we have demonstrated that intestinal Disaccharidases are inhibited immediately by Miglustat in the intestinal lumen. Nevertheless, the multiple functions of Miglustat hypothesize long term effects of Miglustat on intracellular mechanisms, including glycosylation, maturation and trafficking of the intestinal Disaccharidases. Our data show that a major long term effect of Miglustat is its interference with N-glycosylation of the proteins in the ER leading to a delay in the trafficking of sucrase-isomaltase. Also association with lipid rafts and plausibly apical targeting of this protein is partly affected in the presence of Miglustat. More drastic is the effect of Miglustat on lactase-phlorizin hydrolase which is partially blocked intracellularly. The de novo synthesized SI and LPH in the presence of Miglustat show reduced functional efficiencies according to altered posttranslational processing of these proteins. However, at physiological concentrations of Miglustat (≤50 μM) a major part of the activity of these Disaccharidases is found to be still preserved, which puts the charge of the observed carbohydrate maldigestion mostly on the direct inhibition of Disaccharidases in the intestinal lumen by Miglustat as the immediate side effect.
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Miglustat-induced intestinal carbohydrate malabsorption is due to the inhibition of α-glucosidases, but not β-galactosidases
Journal of Inherited Metabolic Disease, 2012Co-Authors: Mahdi Amiri, Hassan Y. NaimAbstract:Miglustat is an oral medication that has approved indication for type I Gaucher disease and Niemann pick disease type C. Usually treatment with Miglustat is associated with occurrence of gastrointestinal side effects similar to carbohydrate maldigestion symptoms. Here, we studied the direct influence of Miglustat on the enzymatic function of the major Disaccharidases of the intestinal epithelium. Our findings show that an immediate effect of Miglustat is its interference with carbohydrate digestion in the intestinal lumen via reversible inhibition of Disaccharidases that cleave α-glycosidically linked carbohydrates. Higher non physiological concentrations of Miglustat can partly affect lactase activity. We further show that the inhibition of the Disaccharidases function by Miglustat is mainly competitive and does not occur via alteration of the enzyme folding.
Devendra Mehta - One of the best experts on this subject based on the ideXlab platform.
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sucrase isomaltase gene variants in patients with abnormal sucrase activity and functional gastrointestinal disorders
Journal of Pediatric Gastroenterology and Nutrition, 2021Co-Authors: Chirajyoti Deb, Stephani Campion, Veronica Derrick, Vanessa Ruiz, Bassam Abomoelak, Angelina Avdella, Baiming Zou, Karoly Horvath, Devendra MehtaAbstract:OBJECTIVES The aim of the study was to determine prevalence and characterize sucrase-isomaltase (SI) gene variants of congenital sucrase-isomaltase deficiency in non-Hispanic white pediatric and young adult patients with functional gastrointestinal disorders (FGIDs), and abnormal sucrase activity on histologically normal duodenal biopsy. METHODS Clinical symptoms and Disaccharidase activities data were collected for an abnormal (low) sucrase (≤25.8 U, n = 125) activity group, and 2 normal sucrase activity groups with moderate (≥25.8-≤55 U, n = 250) and high (>55 U, n = 250) sucrase activities. SI gene variants were detected by next-generation sequencing of DNA from formalin-fixed paraffin-embedded tissues of these patients. FGIDs symptoms based on Rome IV criteria and subsequent clinical management of abnormal sucrase activity cases with pathogenic SI gene variants were analyzed. RESULTS Thirteen SI gene variants were found to be significantly higher in abnormal sucrase cases with FGIDs symptoms (36/125, 29%; 71% did not have a pathogenic variant) compared to moderate normal (16/250, 6.4%, P < 0.001) or high normal (5/250, 2.0%, P < 0.001) sucrase groups. Clinical management data were available in 26 of abnormal sucrase cases, and only 10 (38%) were correctly diagnosed and managed by the clinicians. Concomitant lactase deficiency (24%; 23/97) and pan-Disaccharidase deficiency (25%; 13/51) were found in the abnormal sucrase group. CONCLUSIONS Heterozygous and compound heterozygous mutations in the SI gene were more prevalent in cases with abnormal sucrase activity presenting with FGIDs, and normal histopathology. This suggests heterozygous pathogenic variants of congenital sucrase-isomaltase deficiency may present as FGIDs. Concomitant lactase or pan-Disaccharidase deficiencies were common in abnormal sucrase cases with SI gene variants.
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sucrase isomaltase gene variants in patients with abnormal sucrase activity and functional gi disorders
Journal of Pediatric Gastroenterology and Nutrition, 2020Co-Authors: Chirajyoti Deb, Stephani Campion, Veronica Derrick, Vanessa Ruiz, Bassam Abomoelak, Angelina Avdella, Baiming Zou, Karoly Horvath, Devendra MehtaAbstract:OBJECTIVES To determine prevalence and characterize sucrase-isomaltase (SI) gene variants of congenital sucrase-isomaltase deficiency (CSID) in non-Hispanic white pediatric and young adult patients with functional gastrointestinal disorders (FGIDs), and abnormal sucrase activity on histologically normal duodenal biopsy. METHODS Clinical symptoms and Disaccharidase activities data were collected for an abnormal (low) sucrase (≤25.8U, n = 125) activity group, and two normal sucrase activity groups with moderate (≥25.8U to ≤55U, n = 250) and high (>55U, n = 250) sucrase activities. Sucrase isomaltase (SI) gene variants were detected by next-generation sequencing (NGS) of DNA from formalin-fixed-paraffin-embedded (FFPE) tissues of these patients. FGIDs symptoms based on Rome IV criteria and subsequent clinical management of abnormal sucrase activity cases with pathogenic SI gene variants were analyzed. RESULTS Thirteen SI gene variants were found to be significantly higher in abnormal sucrase cases with FGIDs symptoms (36/125, 29%; 71% did not have a pathogenic variant) compared to moderate normal (16/250, 6.4%, p < 0.001) or high normal (5/250, 2.0%, p < 0.001) sucrase groups. Clinical management data were available in 26 of abnormal sucrase cases, and only 10 (38%) were correctly diagnosed and managed by the clinicians. Concomitant lactase deficiency (24%; 23/97) and pan-Disaccharidase deficiency (25%; 13/51) were found in the abnormal sucrase group. CONCLUSIONS Heterozygous and compound heterozygous mutations in the SI gene were more prevalent in cases with abnormal sucrase activity presenting with FGIDs, and normal histopathology. This suggests heterozygous pathogenic variants of CSID may present as FGIDs. Concomitant lactase or pan-Disaccharidase deficiencies were common in abnormal sucrase cases with SI gene variants.
Nader Nciri - One of the best experts on this subject based on the ideXlab platform.
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new research highlights impact of chronic ingestion of white kidney beans phaseolus vulgaris l var beldia on small intestinal Disaccharidase activity in wistar rats
Toxicology reports, 2018Co-Authors: Nader Nciri, Namjun ChoAbstract:Abstract The chronic ingestion of raw or undercooked kidney beans (Phaseolus vulgaris L.) is involved in the pathogenesis of multiple organ dysfunction; the underlying mechanisms are still poorly understood. The objective of this study was to assess the gavage effects of a raw Beldia bean variety on the brush border Disaccharidase activities in the jejunal mucosa of Wistar rats. Twenty young adult male rats were randomly assigned into 2 groups of 10 rats each: Control, rats were gavaged with 300 mg of a rodent pellet flour suspension (RPFS); Experimental, rats were orogastrically fed a dose of 300 mg Beldia bean flour suspension (BBFS). Prior to determining the Disaccharidase activity by Dahlqvist method, the blood and stool specimens were collected on day 10. The sera and feces were screened for the presence of lectins by serologic and hemagglutination assays. The results showed that the brush border maltase and sucrase activities were significantly diminished but lactase activity did not undergo any change in BBFS-gavaged animals as compared with control. Preliminary immunobiochemical assays revealed the absence of lectins in the systemic circulation and feces of rats, but further work is required to prove this. Overall, the dietary administration of BBFS caused depression of the activity of the small intestinal enzymes maltase and sucrase.
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New research highlights: Impact of chronic ingestion of white kidney beans (Phaseolus vulgaris L. var. Beldia) on small-intestinal Disaccharidase activity in Wistar rats
'Elsevier BV', 2018Co-Authors: Nader Nciri, Namjun ChoAbstract:The chronic ingestion of raw or undercooked kidney beans (Phaseolus vulgaris L.) is involved in the pathogenesis of multiple organ dysfunction; the underlying mechanisms are still poorly understood. The objective of this study was to assess the gavage effects of a raw Beldia bean variety on the brush border Disaccharidase activities in the jejunal mucosa of Wistar rats. Twenty young adult male rats were randomly assigned into 2 groups of 10 rats each: Control, rats were gavaged with 300 mg of a rodent pellet flour suspension (RPFS); Experimental, rats were orogastrically fed a dose of 300 mg Beldia bean flour suspension (BBFS). Prior to determining the Disaccharidase activity by Dahlqvist method, the blood and stool specimens were collected on day 10. The sera and feces were screened for the presence of lectins by serologic and hemagglutination assays. The results showed that the brush border maltase and sucrase activities were significantly diminished but lactase activity did not undergo any change in BBFS-gavaged animals as compared with control. Preliminary immunobiochemical assays revealed the absence of lectins in the systemic circulation and feces of rats, but further work is required to prove this. Overall, the dietary administration of BBFS caused depression of the activity of the small intestinal enzymes maltase and sucrase. Keywords: Disaccharidase activity, Hemagglutination assay, Jejunum, Phytohemagglutinin (PHA), Serologic assay, White kidney bean (Phaseolus vulgaris L.
Sadako Nakamura - One of the best experts on this subject based on the ideXlab platform.
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d sorbose inhibits Disaccharidase activity and demonstrates suppressive action on postprandial blood levels of glucose and insulin in the rat
Nutrition Research, 2014Co-Authors: Yoko Muratatakenoshita, Yuko Yamazaki, Fumio Shimura, Sadako NakamuraAbstract:Abstract In an attempt to develop d-sorbose as a new sweetener that could help in preventing lifestyle-related diseases, we investigated the inhibitory effect of d-sorbose on Disaccharidase activity, using the brush border membrane vesicles of rat small intestines. The inhibitory effect was compared with that of l-sorbose and other rare sugars, and the small intestinal Disaccharidases in rats was compared with that of humans as well. In humans and the small intestines of rats, d-sorbose strongly inhibited sucrase activity and weakly inhibited maltase activity. Inhibition by d-sorbose of sucrase activity was similar to that of l-arabinose, and the K i of d-sorbose was 7.5 mM. Inhibition by d-sorbose was very strong in comparison with that of l-sorbose ( K i , 60.8 mM), whereas inhibition of d-tagatose was between that of d-sorbose and l-sorbose. The inhibitory mode of d-sorbose for sucrose and maltase was uncompetitive, and that of l-sorbose was competitive. To determine a suppressive effect on postprandial blood levels of glucose and insulin via inhibition of sucrase activity, sucrose solution with or without d-sorbose was administered to rats. Increments in the blood levels of glucose and insulin were suppressed significantly after administration of sucrose solution with d-sorbose to rats, in comparison to administration of sucrose solution without d-sorbose. In contrast, the suppressive effect of l-sorbose on postprandial blood levels of glucose and insulin was very weak. These results suggest that d-sorbose may have an inhibitory effect on Disaccharidase activity and could be used as a sweetener to suppress the postprandial elevation of blood levels of glucose and insulin. The use of d-sorbose as a sweetener may contribute to the prevention of lifestyle-related diseases, such as type 2 diabetes mellitus.
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inhibitory effects of extractives from leaves of morus alba on human and rat small intestinal Disaccharidase activity
British Journal of Nutrition, 2006Co-Authors: Tsuneyuki Oku, Mai Yamada, Mariko Nakamura, Naoki Sadamori, Sadako NakamuraAbstract:The inhibitory effect on human and rat intestinal Disaccharidase by the extractive from the leaves of Morus alba (ELM) containing 0.24 % 1-deoxynojirimycin equivalent and its inhibitory activities were investigated by the modified Dahlqvist method. In the presence of 1000-fold diluted ELM solution, the sucrase activity of four human samples was inhibited by 96 % and that of maltase and isomaltase by 95 and 99 %, respectively. The activities of trehalase and lactase were inhibited by 44 and 38 %, respectively. The human Disaccharidase activities varied from sample to sample because the samples were obtained from different resected regions after surgery. However, the ratio of the inhibitory effect for sucrase, maltase, isomaltase, trehalase and lactase was very similar among the four samples, and also that of resembled rat intestinal disaccharides. The inhibitory constant of the 1-deoxynojirimycin equivalent for sucrase, maltase and isomaltase was 2.1 x 10(-4), 2.5 x 10(-4) and 4.5 x 10(-4) mm, respectively, and these inhibitory activities were shown, using rat brush border membrane vesicles, to be competitive. These results demonstrate that digestion is inhibited when an appropriate amount of ELM is orally ingested with sucrose or polysaccharide in man. When ELM was orally administered in a sucrose solution to fasted rats, the elevation in blood glucose was significantly suppressed, depending on the concentration of ELM given. These results suggest that ELM could be used as an ingredient in health foods and in foods that help to prevent diabetes.