Maternal protein restriction affects gene expression and enzyme activity of intestinal disaccharidases in adult rat offspring

This study investigated the consequences of intrauterine protein restriction on the gastrointestinal tract and particularly on the gene expression and activity of intestinal disaccharidases in the adult offspring. Wistar rat dams were fed isocaloric diets containing 6% protein (restricted, n = 8) or 17% protein (control, n = 8) throughout gestation. Male offspring (n = 5-8 in each group) were evaluated at 3 or 16 weeks of age. Maternal protein restriction during pregnancy produced offspring with growth restriction from birth (5.7 ± 0.1 vs 6.3 ± 0.1 g; mean ± SE) to weaning (42.4 ± 1.3 vs 49.1 ± 1.6 g), although at 16 weeks of age their body weight was similar to control (421.7 ± 8.9 and 428.5 ± 8.5 g). Maternal protein restriction also increased lactase activity in the proximal (0.23 ± 0.02 vs 0.15 ± 0.02), medial (0.30 ± 0.06 vs 0.14 ± 0.01) and distal (0.43 ± 0.07 vs 0.07 ± 0.02 U·g-1·min-1) small intestine, and mRNA lactase abundance in the proximal intestine (7.96 ± 1.11 vs 2.38 ± 0.47 relative units) of 3-week-old offspring rats. In addition, maternal protein restriction increased sucrase activity (1.20 ± 0.02 vs 0.91 ± 0.02 U·g-1·min-1) and sucrase mRNA abundance (4.48 ± 0.51 vs 1.95 ± 0.17 relative units) in the duodenum of 16-week-old rats. In conclusion, the present study shows for the first time that intrauterine protein restriction affects gene expression of intestinal enzymes in offspring.

Comparison of duodenal and jejunal disaccharidase levels in patients with non ulcer dyspepsia.

AIMS: This study was conducted to compare the duodenal and jejunal disaccharidase levels in the same individual with duodenal ulcer or non ulcer dyspepsia. METHODS: Thirty seven patients (duodenal ulcer--11, non-ulcer dyspepsia--26) were included in the study. Endoscopic biopsy samples were obtained from jejunum and duodenum using pediatric colonofibroscope. RESULTS: Levels of jejunal disaccharidases were significantly higher than the duodenal disaccharidases. CONCLUSIONS: An estimate of jejunal disaccharidases can be had by multiplication of duodenal disaccharidased by a factor 1.48 for lactase, 1.50 for sucrase and 1.56 for maltase.

Relation of the disaccharidases in the small intestine of the rat to the degree of experimentally induced iron-deficiency anemia

Hypolactasia associated with severe iron-deficiency anemia has been reported in several studies. The objective of the present study was to determine whether hypolactasia is associated with the degree and duration of iron-deficiency anemia. Newly weaned male Wistar rats were divided into a control group receiving a diet supplemented with iron (C) and an experimental group (E) receiving a diet not supplemented with iron (iron-deficiency diet). The animals were studied on the 3rd, 5th, 7th, 14th, 21st, 28th and 35th days of the experiment, when overall and iron nutritional status and disaccharidase activity in the small intestine were determined by the Dahlqvist method. A reduction in weight occurred in the anemic animals starting on the 5th day of the study. Anemia was present in the experimental animals, with a progressive worsening up to the 14th day (hemoglobin: C = 13.27 and E = 5.37) and stabilizing thereafter. Saccharase and maltase activities did not differ significantly between groups, whereas lactase showed a significant reduction in total (TA) and specific activity (SA) in the anemic animals starting on the 21st day of the study. Median lactase TA for the C and E groups was 2.27 and 1.25 U on the 21st day, 2.87 and 1.88 U on the 28th day, and 4.20 and 1.59 U on the 35th day, respectively. Median lactase SA was 0.31 and 0.20 U/g wet weight on the 21st day, 0.39 and 0.24 U/g wet weight on the 28th day, and 0.42 and 0.23 U/g wet weight on the 35th day, respectively. These findings suggest a relationship between the enzymatic alterations observed and both the degree and duration of the anemic process. Analysis of other studies on intestinal disaccharidases in anemia suggests that the mechanism of these changes may be functional, i.e., that the enterocytes may suffer a reduction in their ability to synthesize these enzymes.

Disaccharidase levels in normal epithelium of the small intestine of rats with iron-deficiency anemia

Iron-deficiency anemia is the nutritional deficiency most frequently occurring throughout the world, which manifests as a complex systemic disease involving all cells, affecting enzyme activities and modifying protein synthesis. In view of these considerations, the objective of the present study was to determine the effects of iron-deficiency anemia on disaccharidase and on the epithelial morphokinetics of the jejunal mucosa. Newly weaned male Wistar rats were divided into 4 groups of 10 animals each: C6w received a standard ration containing 36 mg elemental iron per Kg ration for 6 weeks; E6w received and iron-poor ration (5-8 mg/kg ration) for 6 weeks; C10w received an iron-rich ration (36 mg/kg ration) for 10 weeks; E10w received an iron-poor ration for 6 weeks and then an iron-rick ration (36 mg/kg) for an additional 4 weeks. Jejunal fragments were used to measure disaccharidase content and to study cell proliferation. The following results were obtained: 1) a significant reduction (P<0.001) of animal weight, hemoglobin (Hb), serum iron and total iron-binding capacity (TIBC) in groups E6w as compared to C6w; reversal of the alterations in Hb, serum iron and TIBC with iron repletion (E10w = C10w); animal weights continued to be significanly different in group E10w and C10w. 2) Sucrase and maltase levels were unchanged; total and specific lactase levels were significantly lower in group E6w and this reduction was reversed by iron repletion (E10w = C10w). 3) The cell proliferation parameters did not differ between groups. On the basis of these results, we conclude that lactase production was influenced by iron deficiency and that fact was not related to changes in cell population and proliferation in the intestinal mucosa.

Esvaziamento gástrico de sacarose e maltose e os níveis das respectivas dissacaridases na mucosa do intestino delgado de ratos adultos / Gastric emptying of sucrose and maltose and the activities of respective disaccharidases in the intestinal mucosa of adult rats

O esvaziamento gástrico (EG) de soluçöes de sacarose e de maltose em diferentes concentraçöes, marcadas com fenol vermelho (6mg por cento), foi determinado em 144 ratos Wistar machos. Foi avaliada a retençäo gástrica (RG), após 15 minutos da infusäo orogástrica, de soluçöes de sacarose e de maltose nas concentraçöes de 2,5 por cento, 5 por cento e 10 por cento, empregado inicialmente 1 ml e noutra observaçäo 2 ml/100 g de peso do animal. Para cada volume e concentraçäo foram utilizados 12 animais. Foram determinadas as atividades das dissacridases, lactase, sacarase e maltase no intestino delgado de outros oito ratos Wistar machos, submetidos às mesmas condiçöes do estudo. Os resultados mostrarom uma relaçäo da atividade da maltose com a da atividade da maltose com a da sacarose de 4:1. Por outro lado, a RG das soluçöes de maltose a 5 por cento e 10 por cento foi significativamente maior que a de sacarose nas mesmas concentraçöes, independente do volume utilizado. Em concentraçäo a 2,5 por cento näo houve diferença significativa entre as RG das duas soluçöes. Para explicar os resultados, é proposto que o EG mais rápido da soluçäo de sacarose nas concentraçöes a 5 por cento e 10 por cento comparado à soluçäo de maltose nas mesmas concentraçöes, resulta de uma possível saturaçäo da sacarose, com interrupçäo na regulaçäo do EG, gerada a partir de receptores intestinais

Influencia de la ingestión de biomasa de Kluyveromyces fragilis sobre la actividad de las disacaridasas intestinales en ratas / Influence of Kluyveromyces fragilis biomasa intake on the intestinal dissacharidase activity in rats

Se evaluó la influencia de la ingestión de Kluyveromyces fragilis en dietas para ratas con 20 y 40 % de la levadura como fuente de proteinas sobre la actividad de las disacaridasas intestinales: lactasa, maltasa, sacarosa y trealasa en 4 niveles sucesivos de ubicación de la microvellosidad intestinal: luminal, membrana, enterocito y actividad total, para lo cual se utilizó una técnica de lavados y homogeneizados en fragmentos de intestinos tomados en la zona del ángulo de Treittz, en un total de 67 ratas agrupadas según la dieta recibida en a) grupo con pienso para roedores, b) grupo con caseina como fuente de proteinas, c)grupo con levadura al 40% durante un período experimental de 90 dias. Al comparar los resultados de las actividades enzimáticas entre los grupos estudiados, no se encontraron diferencias significativas para ninguna de las enzimas analizadas ni en ninguno de los niveles de localización en el enterocito