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BACKGROUND: Reduced activity of the sucrase-isomaltase (SI) enzyme can cause gastrointestinal symptoms. Biochemical measurement of SI activity in small intestinal biopsies is presently considered the gold standard for the diagnosis of SI deficiency, but this invasive test is not suitable as a routine diagnostic tool. AIM: To evaluate a 13C-sucrose-breath test (13CSBT) as a diagnostic tool for SI deficiency in an adult population. METHODS: 13CSBT results were compared to sucrase activity measured in duodenal biopsies. RESULTS: Forty patients with gastrointestinal symptoms were included in the study, 4 of whom had celiac disease and the rest (n = 36) had normal histological findings. Nine patients (22.5%) had low sucrase activity measured using duodenal biopsies. No correlation was observed between enzymatic sucrase activity and the 13CSBT results. The 13CSBT-curves for the celiac patients versus patients with normal duodenal histology demonstrated that the patients with celiac disease were within the lower range of the distribution. CONCLUSION: We observed a mismatch between the 13CSBT results and the biochemically measured sucrase activity, suggesting that SI activity is not uniformly distributed throughout the small intestines. This methodological discrepancy should be acknowledged when diagnosing SI deficiency.
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Testes Respiratórios , Erros Inatos do Metabolismo dos Carboidratos , Doença Celíaca , Duodeno , Complexo Sacarase-Isomaltase , Sacarose , Humanos , Testes Respiratórios/métodos , Adulto , Complexo Sacarase-Isomaltase/deficiência , Complexo Sacarase-Isomaltase/metabolismo , Masculino , Feminino , Duodeno/enzimologia , Duodeno/patologia , Pessoa de Meia-Idade , Erros Inatos do Metabolismo dos Carboidratos/diagnóstico , Erros Inatos do Metabolismo dos Carboidratos/enzimologia , Sacarose/metabolismo , Doença Celíaca/diagnóstico , Doença Celíaca/enzimologia , Isótopos de Carbono , Idoso , Biópsia , Adulto Jovem , Ensaios Enzimáticos/métodos , AdolescenteRESUMO
PURPOSE OF REVIEW: Disaccharidase deficiency in adults causes carbohydrate malabsorption, resulting in symptoms which significantly overlap with irritable bowel syndrome (IBS). This article discusses the diagnosis and treatment of disaccharidase deficiency within the context of recent literature. RECENT FINDINGS: Disaccharidase deficiency in adults is more common than previously thought, which includes lactase, sucrase, maltase and isomaltase enzymes. Deficiency in disaccharidases, which are produced by the intestinal brush border, will interfere with the breakdown and absorption of carbohydrates and may result in abdominal pain, gas, bloating and diarrhea. Patients deficient in all 4 disaccharidases are known as having "pan-disaccharidase" deficiency, which has a distinct phenotype with more reported weight loss than patients deficient in one enzyme. IBS patients who do not respond to low FODMAP dietary restriction may have undiagnosed disaccharidase deficiency and may benefit from testing. Diagnostic testing methods are limited to duodenal biopsies, which is the gold standard, and breath testing. Dietary restriction and enzyme replacement therapy have been shown to be effective treatments in these patients. Disaccharidase deficiency is an underdiagnosed condition in adults with chronic GI symptoms. Patients who do not respond to traditional treatment strategies for DBGI may benefit from testing for disaccharidase deficiency. Further studies delineating the distinctions between disaccharidase deficient patients and those with other motility disorders are needed.
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Síndrome do Intestino Irritável , Síndromes de Malabsorção , Humanos , Síndromes de Malabsorção/diagnóstico , Síndromes de Malabsorção/etiologia , Síndromes de Malabsorção/terapia , Dissacaridases/metabolismo , Sacarase/metabolismo , DiarreiaRESUMO
AIM: To compare the effect of a diet low in fermentable oligo-, di-, monosaccharides and polyols (fermentable oligosaccharides, disaccharides, monosaccharides and polyols - FODMAP) and rebamipide on carbohydrate tolerance and disaccharidases activity in patients with maldigestive enteropathy (ENMP). MATERIALS AND METHODS: The study included 61 patients with ENMP with reduced small intestine carbohydrases. Their glucoamylase activity was 100 ng glucose/mg tissue × min (quartile 53, 72), maltase - 504 (quartile 258, 708), sucrase - 43 (quartile 25, 58), lactase - 8 (quartile 4, 20). Group 1 included 19 people on a low FODMAP diet. The 2nd group included 42 patients who were on a normal diet and received rebamipide 300 mg/day. Patients were monitored weekly for 8 weeks. RESULTS: In 16 patients of the 1st group, abdominal pain and stool disorders decreased, in 15 patients, swelling and rumbling in the abdomen stopped. Glucoamylase activity increased to 196 (quartile 133, 446, Ñ<0.024) ng glucose/mg tissue × min, maltase activity increased to 889 (quartile 554, 1555, p<0.145), sucrase activity increased to 67 (quartile 43, 175, p<0.039), lactase activity increased to 13 (quartile 9, 21, p<0.02). After the diet was discontinued, intestinal symptoms in patients of group 1 resumed. In 27 patients of the 2nd group after 4 weeks dyspeptic manifestations decreased, in 34 patients the tolerability of products containing FODMAP improved. Continuation of treatment up to 8 weeks contributed to a further improvement in well-being. Glucoamylase activity increased after 4 and 8 weeks to 189 (quartile 107, 357, p<0.013) and 203 (quartile 160, 536, p<0.005), respectively; maltase - up to 812 (quartile 487, 915, p<0.005) and 966 (quartile 621, 2195, Ñ<0.0012); sucrases - up to 60 (quartile 34, 105, p<0.013) and 75 (quartile 52, 245, Ñ=0.003); lactase - up to 12 (quartile 8, 12, p<0.132) and 15 ng glucose/mg tissue × min (quartile 10, 20, Ñ<0.092). CONCLUSION: The clinical symptoms of fermentable carbohydrate intolerance and increased membrane enzyme activity are reduced by a low FODMAP diet in patients with ENMT, but clinical symptoms of food intolerance reappear when switching to a normal diet. Treatment with rebamipide improves food tolerance and consistently increases the activity of TSOTS enzymes after 4 and 8 weeks.
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Enteropatias , Síndrome do Intestino Irritável , Humanos , Dissacaridases , alfa-Glucosidases , Glucana 1,4-alfa-Glucosidase , Dieta , Sacarase , Monossacarídeos/uso terapêutico , Glucose , Lactase , DigestãoRESUMO
The Gram-negative periodontal pathogen Tannerella forsythia is inherently auxotrophic for N-acetylmuramic acid (MurNAc), which is an essential carbohydrate constituent of the peptidoglycan (PGN) of the bacterial cell wall. Thus, to build up its cell wall, T. forsythia strictly depends on the salvage of exogenous MurNAc or sources of MurNAc, such as polymeric or fragmentary PGN, derived from cohabiting bacteria within the oral microbiome. In our effort to elucidate how T. forsythia satisfies its demand for MurNAc, we recognized that the organism possesses three putative orthologs of the exo-ß-N-acetylmuramidase BsNamZ from Bacillus subtilis, which cleaves nonreducing end, terminal MurNAc entities from the artificial substrate pNP-MurNAc and the naturally-occurring disaccharide substrate MurNAc-N-acetylglucosamine (MurNAc-GlcNAc). TfNamZ1 and TfNamZ2 were successfully purified as soluble, pure recombinant His6-fusions and characterized as exo-lytic ß-N-acetylmuramidases with distinct substrate specificities. The activity of TfNamZ1 was considerably lower compared to TfNamZ2 and BsNamZ, in the cleavage of MurNAc-GlcNAc. When peptide-free PGN glycans were used as substrates, we revealed striking differences in the specificity and mode of action of these enzymes, as analyzed by mass spectrometry. TfNamZ1, but not TfNamZ2 or BsNamZ, released GlcNAc-MurNAc disaccharides from these glycans. In addition, glucosamine (GlcN)-MurNAc disaccharides were generated when partially N-deacetylated PGN glycans from B. subtilis 168 were applied. This characterizes TfNamZ1 as a unique disaccharide-forming exo-lytic ß-N-acetylmuramidase (exo-disaccharidase), and, TfNamZ2 and BsNamZ as sole MurNAc monosaccharide-lytic exo-ß-N-acetylmuramidases. IMPORTANCE Two exo-N-acetylmuramidases from T. forsythia belonging to glycosidase family GH171 (www.cazy.org) were shown to differ in their activities, thus revealing a functional diversity within this family: NamZ1 releases disaccharides (GlcNAc-MurNAc/GlcN-MurNAc) from the nonreducing ends of PGN glycans, whereas NamZ2 releases terminal MurNAc monosaccharides. This work provides a better understanding of how T. forsythia may acquire the essential growth factor MurNAc by the salvage of PGN from cohabiting bacteria in the oral microbiome, which may pave avenues for the development of anti-periodontal drugs. On a broad scale, our study indicates that the utilization of PGN as a nutrient source, involving exo-lytic N-acetylmuramidases with different modes of action, appears to be a general feature of bacteria, particularly among the phylum Bacteroidetes.
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Peptidoglicano , Tannerella forsythia , Acetilglucosamina/metabolismo , Bacillus subtilis/metabolismo , Parede Celular/metabolismo , Dissacarídeos/metabolismo , Peptidoglicano/metabolismo , Especificidade por Substrato , Tannerella forsythia/genéticaRESUMO
The article presents an analysis of the literature on food intolerance (FS) associated with the presence in the diet of fermentable oligodimosaccharides and polyols FODMAP (fermentable oligosaccharides, disaccharides, monosaccharides and polyols), histamine and food additives. The relationship between FS and insufficient activity of enzymes of the small intestine mucosa, in particular, in patients with irritable bowel syndrome, is discussed. FS often noted in them forces them to strictly adhere to the elimination diet and significantly impair the quality of life due to dissatisfaction with the results of treatment. Analysis of the literature has confirmed in many patients with irritable bowel syndrome an etiotropic relationship with poor food tolerance and dictates the need for randomized studies to further study the pathogenetic mechanisms of increasing food tolerance under the influence of cytoprotective therapy.
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Síndrome do Intestino Irritável , Humanos , Intolerância Alimentar , Qualidade de Vida , Histamina , Fermentação , Monossacarídeos , Dissacarídeos , Oligossacarídeos , Aditivos Alimentares , DuodenoRESUMO
The article describes enteropathy with impaired membrane digestion (EIMD) as a new nosological form. The main clinical manifestation of EIMD is the poor tolerance of food products, in particular carbohydrates and a decrease in the activity of membrane enzymes, in particular, carbohydrates, in the mucous membrane of the small intestine. The cause of the disease can be acute intestinal infections, viruses, drugs and other agents that damage the small intestine. The pathophysiology, clinical picture and diagnosis of EIMD are described. The basis of therapy is rebamipide, which has the ability to reduce the symptoms of carbohydrate intolerance and increase the activity of disaccharidases.
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BACKGROUND: Small intestinal starch digestion in ruminants is potentially limited by inadequate production of carbohydrases. Previous research has demonstrated that small intestinal starch digestion can be improved by postruminal supply of casein or glutamic acid. However, the mechanisms by which casein and glutamic acid increase starch digestion are not well understood. OBJECTIVES: The objective of this experiment was to evaluate the effects of duodenal infusions of starch with casein or glutamic acid on postruminal carbohydrase activities in cattle. METHODS: Twenty-two steers [mean body weight (BW) = 179 ± 4.23 kg] were surgically fitted with duodenal and ileal cannulas and limit-fed a soybean hull-based diet containing small amounts of starch. Raw cornstarch (1.61 ± 0.0869 kg/d) was infused into the duodenum alone (control), or with 118 ± 7.21 g glutamic acid/d, or 428 ± 19.4 g casein/d. Treatments were infused continuously for 58 d and then steers were killed for tissue collection. Activities of pancreatic (α-amylase) and intestinal (maltase, isomaltase, glucoamylase, sucrase) carbohydrases were determined. Data were analyzed as a randomized complete block (replicate group) design using the GLM procedure of SAS to determine effects of infusion treatment. RESULTS: Duodenal casein infusion increased (P < 0.05) pancreatic α-amylase activity by 290%. Duodenal glutamic acid infusion increased (P < 0.03) duodenal maltase activity by 233%. Duodenal casein infusion increased jejunal maltase (P = 0.02) and glucoamylase (P = 0.03) activity per gram protein by 62.9% and 97.4%, respectively. Duodenal casein infusion tended to increase (P = 0.10) isomaltase activity per gram jejunum by 38.5% in the jejunum. Sucrase activity was not detected in any segment of the small intestine. CONCLUSIONS: These results suggest that small intestinal starch digestion can be improved in cattle with increased small intestinal flow of casein through increases in postruminal carbohydrase activities.
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Caseínas/administração & dosagem , Bovinos/fisiologia , Duodeno/efeitos dos fármacos , Ácido Glutâmico/administração & dosagem , Glicosídeo Hidrolases/metabolismo , Amido/administração & dosagem , Fenômenos Fisiológicos da Nutrição Animal , Animais , Digestão/efeitos dos fármacos , Digestão/fisiologia , Duodeno/enzimologia , Regulação Enzimológica da Expressão Gênica/efeitos dos fármacos , Glicosídeo Hidrolases/genética , Masculino , Pâncreas/efeitos dos fármacos , Pâncreas/enzimologiaRESUMO
1. The present study focused on the potential effects of antibiotics on intestinal digestion and integrity in broilers in terms of disaccharidase activity, electrophysiological properties and morphology. 2. One-day-old Arbour Acres birds were randomly allocated to one of four treatment groups for 42 days; control, colistin (20 mg/kg), tylosin (55 mg/kg) or chlortetracycline (CTC, 55 mg/kg) groups. Colistin and tylosin supplementation, but not CTC supplementation, caused an increase in body weight gain. 3. Colistin and tylosin elevated the activities of maltase and sucrase in the mucosa of the jejunum on d 42. Age caused a gradual decrease in the short-circuit current (Isc) and conductance (Gt) of the ileum, as a measure of permeability. The Isc and Gt of the ileum were higher in the colistin-supplemented broilers than in the control birds on d 42. Tylosin- and CTC-supplemented birds displayed Isc and Gt values similar to those of the control birds. 4. Colistin supplementation increased the villus area in the jejunum and thinned the muscularis mucosae in the ileum compared with the control group. Tylosin supplementation decreased the thickness of the muscularis mucosae and the depth of crypt in the jejunum. CTC thickened the muscularis mucosae in the jejunum and ileum. 5. Colistin and tylosin exhibited a beneficial effect on intestinal digestion and integrity by enhancing disaccharidase activities and improving gut morphology and permeability.
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Ração Animal , Galinhas , Suplementos Nutricionais , Tilosina , Ração Animal/análise , Animais , Colistina , Dieta , Dissacaridases , PermeabilidadeRESUMO
BACKGROUND: Infantile gangliosidoses include GM1 gangliosidosis and GM2 gangliosidosis (Tay-Sachs disease, Sandhoff disease). To date, natural history studies in infantile GM2 (iGM2) have been retrospective and conducted through surveys. Compared to iGM2, there is even less natural history information available on infantile GM1 disease (iGM1). There are no approved treatments for infantile gangliosidoses. Substrate reduction therapy using miglustat has been tried, but is limited by gastrointestinal side effects. Development of effective treatments will require identification of meaningful outcomes in the setting of rapidly progressive and fatal diseases. OBJECTIVES: This study aimed to establish a timeline of clinical changes occurring in infantile gangliosidoses, prospectively, to: 1) characterize the natural history of these diseases; 2) improve planning of clinical care; and 3) identify meaningful future treatment outcome measures. METHODS: Patients were evaluated prospectively through ongoing clinical care. RESULTS: Twenty-three patients were evaluated: 8 infantile GM1, 9 infantile Tay-Sachs disease, 6 infantile Sandhoff disease. Common patterns of clinical change included: hypotonia before 6months of age; severe motor skill impairment within first year of life; seizures; dysphagia and feeding-tube placement before 18months of age. Neurodevelopmental testing scores reached the floor of the testing scale by 20 to 28months of age. Vertebral beaking, kyphosis, and scoliosis were unique to patients with infantile GM1. Chest physiotherapy was associated with increased survival in iGM1 (p=0.0056). Miglustat combined with a low-carbohydrate ketogenic diet (the Syner-G regimen) in patients who received a feeding-tube was associated with increased survival in infantile GM1 (p=0.025). CONCLUSIONS: This is the first prospective study of the natural history of infantile gangliosidoses and the very first natural history of infantile GM1. The homogeneity of the infantile gangliosidoses phenotype as demonstrated by the clinical events timeline in this study provides promising secondary outcome measure candidates. This study indicates that overall survival is a meaningful primary outcome measure for future clinical trials due to reliable timing and early occurrence of this event. Combination therapy approaches, instead of monotherapy approaches, will likely be the best way to optimize clinical outcomes. Combination therapy approaches include palliative therapies (e.g., chest physiotherapy) along with treatments that address the underlying disease pathology (e.g. miglustat or future gene therapies).
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Gangliosidoses GM2/fisiopatologia , Gangliosidoses/fisiopatologia , Gangliosidoses/terapia , Gangliosidose GM1/fisiopatologia , 1-Desoxinojirimicina/efeitos adversos , 1-Desoxinojirimicina/análogos & derivados , 1-Desoxinojirimicina/uso terapêutico , Dieta Cetogênica , Dissacaridases/antagonistas & inibidores , Feminino , Gangliosidoses/complicações , Gangliosidoses GM2/terapia , Gangliosidose GM1/terapia , Inibidores de Glicosídeo Hidrolases/efeitos adversos , Inibidores de Glicosídeo Hidrolases/uso terapêutico , Humanos , Lactente , Masculino , Estudos Prospectivos , Estudos RetrospectivosRESUMO
The inhibition by 1,5-anhydro-d-glucitol (1,5-AG) was determined on disaccharidases of rats and humans. Then, the metabolism and fate of 1,5-AG was investigated in rats and humans. Although 1,5-AG inhibited about 50 % of sucrase activity in rat small intestine, the inhibition was less than half of d-sorbose. 1,5-AG strongly inhibited trehalase and lactase, whereas d-sorbose inhibited them very weakly. 1,5-AG noncompetitively inhibited sucrase. The inhibition of 1,5-AG on sucrase and maltase was similar between humans and rats. 1,5-AG in serum increased 30 min after oral administration of 1,5-AG (600 mg) in rats, and mostly 100 % of 1,5-AG was excreted into the urine 24 h after administration. 1,5-AG in serum showed a peak 30 min after ingestion of 1,5-AG (20 g) by healthy subjects, and decreased gradually over 180 min. About 60 % of 1,5-AG was excreted into the urine for 9 h following ingestion. Hydrogen was scarcely excreted in both rats and humans 24 h after administration of 1,5-AG. Furthermore, 1,5-AG significantly suppressed the blood glucose elevation, and hydrogen excretion was increased following the simultaneous ingestion of sucrose and 1,5-AG in healthy subjects. 1,5-AG also significantly suppressed the blood glucose elevation following the simultaneous ingestion of glucose and 1,5-AG; however, hydrogen excretion was negligible. The available energy of 1,5-AG, which is absorbed readily from the small intestine and excreted quickly into the urine, is 0 kJ/g (0 kcal/g). Furthermore, 1,5-AG might suppress the blood glucose elevation through the inhibition of sucrase, as well as intestinal glucose absorption.
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Glicemia/análise , Desoxiglucose/farmacologia , Insulina/sangue , Período Pós-Prandial , Adulto , Animais , Desoxiglucose/farmacocinética , Dissacaridases/antagonistas & inibidores , Inibidores Enzimáticos/farmacologia , Feminino , Glucose/administração & dosagem , Glucose/farmacocinética , Inibidores de Glicosídeo Hidrolases/farmacologia , Humanos , Hidrogênio/urina , Absorção Intestinal , Intestino Delgado/enzimologia , Masculino , Ratos , Ratos Wistar , Sacarase/antagonistas & inibidores , Sacarose/administração & dosagem , alfa-GlucosidasesRESUMO
BACKGROUND: Many previous studies have reported the role of oat ß-glucan (OBG) in the reduction of postprandial glucose, and hypothesised that OBG may form a protective layer along the intestinal wall, acting as a viscous barrier to decrease glucose transportation. This study examined whether the molecular weight (MW) and concentration of OBG affected the diffusion of glucose in vitro. The effect of OBG on glucose transportation in vitro and sodium-potassium adenosine triphosphatase (Na(+)/K(+)-ATPase) activity in the everted small intestines of normal rats was also examined. RESULTS: In vitro, higher MWs and concentrations of OBG increased the inhibitory effects on glucose diffusion and glucose adsorption. The transport of glucose by glucose transporters and Na(+)/K(+)-ATPase activity in the small intestinal mucosa of rats were significantly lower following the addition of OBG than those in the absence of OBG at the same time-points throughout glucose transportation (P < 0.05). In the OBG-treated group, the Na(+)/K(+)-ATPase activity decreased with increasing OBG MW. However, as the concentration of OBG in the solution increased, the Na(+)/K(+)-ATPase activity in the small intestine increased due to stronger gastrointestinal motility. We also found that higher MWs of OBG had a greater inhibitory effect on intestinal disaccharidase activities in vitro. CONCLUSION: Oat ß-glucan is able to adsorb glucose molecules, inhibit glucose transport, decrease the concentration of available glucose and suppress disaccharidase activities in the small intestine.
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Avena/química , Glucose/metabolismo , Intestino Delgado/efeitos dos fármacos , beta-Glucanas/farmacologia , Adsorção , Animais , Transporte Biológico , Relação Dose-Resposta a Droga , Intestino Delgado/metabolismo , Microscopia Eletroquímica de Varredura , Ratos , ATPase Trocadora de Sódio-Potássio/metabolismo , Propriedades de Superfície , beta-Glucanas/administração & dosagem , beta-Glucanas/químicaRESUMO
Background: Natural restoratives from traditional medicinal plants are considered to be a convenient, potent, and risk-free substitute treatment for hyperglycaemia. Our objective was to explore the activity of the crude extract of Heritiera fomes on postprandial hyperglycaemia by assessing relative measurements in a laboratory animal model. Methods: The Streptozotocin induced diabetic rat (n = 88, twenty-two per group) was used for the glucose tolerance test as an initial support for the study. BaSO4 was administered orally as a marker to measure gut motility after one hour of methanolic extract (500 mg/kg body weight) administration where, only purified water (10 ml/kg) was used to treat the control group (n = 12) and a dose (500 mg/kg) of H. fomes extract was used for the test group (n = 12 in each group). After 60 min of incubation of the mixture of extract and glucose with 10% (v/v) yeast cell suspension, the absorbance was measured to determine the capacity of glucose absorption by yeast cells. Sixty Long Evans rats (n = 12 in each group) were used to assess disaccharidase enzyme activity as µmol/mg protein per hour by Lowry's protein estimation method. The carbohydrate absorption investigation was executed to evaluate the leftover sucrose content in the gastrointestinal system (n = 64). Results: After oral administration of MHFL (71.84%), MHFB (71.41%), and MHFR (72.55%), GI motility (%) increased significantly (p < 0.001) compared to the control group (59.06%). A significant increase in glucose uptake and adsorption capacity measured by different concentrations of glucose ensures the decrease of glucose bound rate and a significant drop in blood glucose concentration. The significant (p < 0.001) decrease in intestinal disaccharidase activity of MHFL (1.40), MHFB (1.36), and MHFR (1.20) in comparison to the control group (1.50) indicates that the presence of H. fomes may reduce glucose absorption in the small bowel. Significant (p < 0.001 & p < 0.05) accumulation of sucrose content in the six different parts of the GI tract suggests the absorption of sucrose was decreased. Conclusions: The findings of this study provide evidence on probable mechanisms for the anti-diabetic characteristics of H. fomes, and it is predicted that this plant will be studied further for the development of strong anti-hyperglycemic medicines.
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This study was conducted to investigate the development patterns of small intestine, intestinal morphology, disaccharidase activities, and sugar transporter gene expression in goslings during pre- and post-hatching periods. Small intestine was sampled on embryonic d 23 and 27, day of hatch, and d 1, 4, and 7 post-hatching. A total of 18 eggs with the breed of Jilin White geese were selected at each sampling timepoint for measuring relevant parameters. Three eggs were considered as a group, with 6 groups in each sampling timepoint. Rapid development of small intestine was observed around the hatching, of which jejunum and ileum had relatively higher development rates. Villus surface area from three intestinal segments started to increase on embryonic d 27, and kept relatively stable during day of hatch to d 1 post-hatching, and following increased till d 7 post-hatching. A high priority of villi enrichment was observed in duodenum and jejunum. The activity of disaccharidase increased before hatching and kept relatively high-level post-hatching, of which the activity of disaccharidase was highest in jejunum. The expression of sugar transporter gene increased prior to hatching and then decreased post-hatching, of which jejunum and duodenum were sites with high sugar transporter gene expression. Rapid development in intestinal morphology, disaccharidase activities, and sugar transporter gene expression around the hatching indicated that goslings have high potential to digest and/or assimilate carbohydrates during its early-life, which provided a preparation for further digestion of exogenous feed. This study provided a profile of development patterns for intestinal morphology, disaccharidase activities, and sugar transporter gene expression in goslings, which was beneficial to understanding the characteristics of nutrient absorption during the early-life of goslings.
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Gansos , Açúcares , Animais , Galinhas , Óvulo , Intestino Delgado/anatomia & histologia , Carboidratos , DissacaridasesRESUMO
BACKGROUND: There are currently three known congenital disaccharidase deficiencies: congenital lactase deficiency (CLD), congenital sucrase-isomaltase deficiency (CSD), and congenital trehalase deficiency (CTD). No congenital deficiency has been described for maltase-glucoamylase (MGAM). METHODS: A literature search was performed in PubMed for the pathogenic variants CLD, CSD, and CTD and the articles retrieved were analyzed to estimate the prevalence of congenital disaccharidase deficiencies. RESULTS: Based on reported variants, the estimated prevalence was 1.3 per 106 births (95% CI: 1.1-1.7) for CLD, and 31.4 per 106 births (95% CI: 28.3-34.8) for CSD. Using data on previously reported variants and variants predicted to be loss-of-function in gnomAD, the overall estimated prevalence was 2.3 per 106 births (95% CI: 1.9-2.9) for CLD, 57.6 per 106 births (95% CI:52.5-63.2) for CSD, and 9.2 per 106 births (95% CI: 2.5-3.7) for CTD. CONCLUSION: The prevalence of CSD was found to be relatively high, while for other congenital disaccharidase deficiencies, the estimated prevalence was very low.
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Erros Inatos do Metabolismo dos Carboidratos , Síndromes de Malabsorção , Humanos , Dissacaridases/genética , Prevalência , Erros Inatos do Metabolismo dos Carboidratos/epidemiologia , Erros Inatos do Metabolismo dos Carboidratos/genética , Frequência do GeneRESUMO
Human giardiasis, caused by the protozoan parasite Giardia duodenalis (syn. Giardia lamblia, Giardia intestinalis, Lamblia intestinalis), is one of the most commonly-identified parasitic diseases worldwide. Chronic G. duodenalis infections cause a malabsorption syndrome that may lead to failure to thrive and/or stunted growth, especially in children in developing countries. Understanding the parasite/epithelial cell crosstalk at the mucosal surfaces of the small intestine during human giardiasis may provide novel insights into the mechanisms underlying the parasite-induced immunopathology and epithelial tissue damage, leading to malnutrition. Efforts to identify new targets for intervening in the development of intestinal immunopathology and the progression to malnutrition are critical. Translating these findings into a clinical setting will require analysis of these pathways in cells and tissues from humans and clinical trials could be devised to determine whether interfering with unwanted mucosal immune responses developed during human giardiasis provide better therapeutic benefits and clinical outcomes for G. duodenalis infections in humans.
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Giardia lamblia , Giardíase , Desnutrição , Criança , Células Epiteliais , Giardia , Humanos , Mucosa IntestinalRESUMO
Most physiological studies on oat beta (ß)-glucan referred to attenuation of blood glucose and insulin responses in both healthy and diabetic individuals. The main purpose of this work was to evaluate the effects of oat ß-glucan on glucose metabolism in streptozotocin-induced diabetic mice and the activities of intestinal disaccharidases in the diabetic mice and in vitro. Meanwhile, the potentially regulative mechanisms on intestinal disaccharidases were discussed. Normal and diabetic mice, treated with metformin, were used as the negative and positive controls, respectively. The results indicated that oat ß-glucan could regulate the glucose metabolism and inhibit the activities of intestinal disaccharidases in vivo and in vitro (p<0.01), especially when using a high-dose, which suggested that oat ß-glucan could effectively improve the internal environment of intestinal tract and would be a potential alpha (α)-glycosidase inhibitor.
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Congenital sucrase isomaltase deficiency (CSID) is an autosomal recessive disorder which leads to chronic intestinal malabsorption of nutrients from ingested starch and sucrose. Symptoms usually present after consumption of fruits, juices, grains, and starches, leading to failure to thrive and malnutrition. Diagnosis is suspected on detailed patient history and confirmed by a disaccharidase assay using small intestinal biopsies or sucrose hydrogen breath test. Treatment of CSID consists of limiting sucrose in diet and replacement therapy with sacrosidase. Due to its nonspecific symptoms, CSID may be undiagnosed in many patients for several years. We present a case of a 50-year-old woman with persistent symptoms of bloating in spite of extensive evaluation and treatment.
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BACKGROUND: Functional bowel disorder (FBD) may be caused by a decrease in disaccharidase activity. Thus, the timely diagnosis of disaccharidase deficiency could lead to a better prognosis in patients with this condition. AIM: To determine the potential value of intestinal disaccharidases glucoamylase, maltase, sucrase, and lactase in understanding the etiology and pathogenesis of FBD. METHODS: A total of 82 FBD patients were examined. According to the Rome IV criteria (2016), 23 patients had diarrhea-predominant irritable bowel syndrome (IBS), 33 had functional diarrhea, 10 had constipation-predominant IBS, 4 had functional constipation, and 12 had mixed IBS. The Dahlqvist method was used to measure disaccharidase activity in the brush-border membrane of mature enterocytes of the small intestine, in duodenal biopsies obtained during esophagogastroduodenoscopy. RESULTS: Lactase deficiency was detected in 86.5% of patients, maltase deficiency in 48.7%, sucrase deficiency in 50%, and glucoamylase deficiency in 84.1%. The activities of all enzymes were reduced in 31.7% of patients, and carbohydrase deficiency was detected in 63.5% of patients. The low activity of enzymes involved in membrane digestion in the small intestine was found in 95.2% of patients. CONCLUSION: In 78 of the 82 patients with FBD, gastrointestinal symptoms were associated with disaccharidase deficiency.
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Background/Aims: Disaccharidase assay is used for assessing carbohydrate intolerance in children, but its usefulness in adults is not known. The aim of this study is to assess the prevalence of disaccharidase deficiency in patients with unexplained gastrointestinal symptoms. Methods: A retrospective review of adults with chronic (> 1 year) abdominal symptoms and negative imaging and endoscopy/colonoscopy and who completed bowel symptom questionnaire and duodenal biopsy for lactase, maltase, sucrase, and palatinase was performed. A subset also underwent 25 g lactose breath test (LBT). Results: One hundred twenty patients (females = 83) were evaluated, of whom 48 also underwent LBT. Fifty-six (46.7%) patients had enzyme deficiency; 44 (36.7%) had single (either lactase or maltase), 1 had 3 enzyme deficiencies, 11 (9.2 %) had all 4 disaccharidase enzyme (pan-disaccharidase) deficiency, and 64 (53.0%) had normal enzyme levels. Baseline prevalence and severity of 11 gastrointestinal symptoms were similar between normal and single enzyme deficiency groups. The sensitivity and specificity of LBT was 78.3% and 72.0%, respectively and overall agreement with lactase deficiency was 75.0%. Conclusions: Isolated disaccharidase deficiency occurs in adults, usually lactase and rarely maltase, and pan-disaccharidase deficiency is rare. Baseline symptoms or its severity did not predict enzyme deficiency.
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Zearalenone (ZEA) is a secondary metabolite with estrogenic effects produced by Fusarium fungi and mainly occurs as a contaminant of grains such as corn and wheat. ZEA, to which weaned gilts are extremely sensitive, is the main Fusarium toxin detected in corn-soybean meal diets. Our aim was to examine the effects of ZEA on the growth performance, intestinal disaccharidase activity, and anti-stress capacity of weaned gilts. Twenty 42-day-old healthy Duroc × Landrace × Large White weaned gilts (12.84 ± 0.26 kg) were randomly divided into control and treatment (diet containing 1.04 mg/kg ZEA) groups. The experiment included a 7-day pre-trial period followed by a 35-day test period, all gilts were euthanized and small intestinal samples were collected and subjected to immunohistochemical and western blot analyses. The results revealed that inclusion of 1.04 mg/kg ZEA in the diet significantly reduced the activities of lactase, sucrase, and maltase in the duodenum, jejunum, and ileum of gilts. Similarly, the activities of superoxide dismutase and glutathione peroxidase in the duodenum, jejunum, and ileum, and activities of catalase in the jejunum and ileum were reduced (p < 0.05). Conversely, the content of malondialdehyde in the duodenum, jejunum, and ileum, and the integrated optical density (IOD), IOD in single villi, and the mRNA and protein expression of heat shock protein 70 (Hsp70) were significantly increased (p < 0.05). The results of immunohistochemical analyses revealed that the positive reaction of Hsp70 in the duodenum, jejunum, and ileum of weaned gilts was enhanced in the ZEA treatment, compared with the control. The findings of this study indicate the inclusion of ZEA (1.04 mg/kg) in the diet of gilts reduced the activity of disaccharidase enzymes and induced oxidative stress in the small intestine, thereby indicating that ZEA would have the effect of reducing nutrient absorption in these animals.