Small intestinal disaccharidase activities in experimental Iron and protein deficiency

Sriratanaban, Amnach; Thayer, Walter R.

doi:10.1093/ajcn/24.4.411

Cited by 23 publications

(17 citation statements)

References 25 publications

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“…Lactase activity was markedly reduced in the anemic group both with respect to total activity and specific activity (Figure 1), in agreement with previous studies (17,18). These investigators, however, also detected a significant reduction in sucrase and maltase, which was not demonstrated in the present study.…”

Section: Discussionsupporting

confidence: 93%

“…Sriratanabam and Thayer (17) and Lanzkowsky et al (18) obtained similar results with rats. The first study (17) also detected disaccharidase activities similar to control values in groups of animals with protein malnutrition, and no altered disaccharidase levels in a fourth group in which protein deficiency was associated with irondeficiency anemia. Reduced disaccharidase activity was also observed in anemic children in another study (19), although the results were inconclusive.…”

Section: Introductionmentioning

confidence: 70%

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

Fernandes¹,

Galvão²,

Bortolozzi³

et al. 1997

Braz J Med Biol Res

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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 irondeficiency anemia on disaccharidases 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 an 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-rich 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 group 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 significantly different in groups 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 this fact was not related to changes in cell population and proliferation in the intestinal mucosa.

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Section: Discussionsupporting

confidence: 93%

Section: Introductionmentioning

confidence: 70%

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

Fernandes¹,

Galvão²,

Bortolozzi³

et al. 1997

Braz J Med Biol Res

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“…In agreement with previous studies, it was observed that iron-deficient Wistar rats have significantly lower sucrase and lactase activities compared with their control littermates (2,4,5,9,16,20,31,38). This decreased activity cannot be attributable to changes in kinetic properties of the enzymes as evidenced by no significant differences in K m values, inferring that it is primarily due to reduced quantities of the enzyme present in the mucosa.…”

Section: Discussionsupporting

confidence: 90%

“…In addition, it has been reported that protein-deficient diets increase disaccharidase activity, irrespective of iron status (31). As such, it seems that marginal macronutrient depletion plays little part in determining disaccharidase activity compared with the effects of iron deficiency, and thus pair-fed control experiments were not pursued.…”

Section: Discussionmentioning

confidence: 99%

“…The enzymatic activity of each individual disaccharidase is influenced primarily by the dietary level of their corresponding substrate (2, 12), and, under normal conditions, this level of activity is controlled by the abundance of the mRNA encoding the proteins (12, 34). However, it has been shown on many occasions that dietary iron deficiency can cause a significant decrease in disaccharidase activity (2,4,5,9,16,20,31,38) and that this decrease is reversible by iron supplementation (9,20,38).…”

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confidence: 99%

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Decreased sucrase and lactase activity in iron deficiency is accompanied by reduced gene expression and upregulation of the transcriptional repressor PDX-1

West¹,

Oates²

2005

American Journal of Physiology-Gastrointestinal and Liver Physi

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West, Adrian R., and Phillip S. Oates. Decreased sucrase and lactase activity in iron deficiency is accompanied by reduced gene expression and upregulation of the transcriptional repressor PDX-1. Am J Physiol Gastrointest Liver Physiol 289: G1108 -G1114, 2005. First published August 4, 2005; doi:10.1152/ajpgi.00195.2005.-Disaccharidases are important digestive enzymes whose activities can be reduced by iron deficiency. We hypothesise that this is due to reduced gene expression, either by impairment to enterocyte differentiation or by iron-sensitive mechanisms that regulate mRNA levels in enterocytes. Iron-deficient Wistar rats were generated by dietary means. The enzyme activities and kinetics of sucrase and lactase were tested as well as the activity of intestinal alkaline phosphatase (IAP)-II because it is unrelated to carbohydrate digestion. mRNA levels of ␤-actin, sucrase, lactase, and the associated transcription factors pancreatic duodenal homeobox (PDX)-1, caudal-related homeobox (CDX)-2, GATA-binding protein (GATA)-4, and hepatocyte nuclear factor (HNF)-1 were measured by real-time PCR. Spatial patterns of protein and gene expression were assessed by immunofluorescence and in situ hybridization, respectively. It was found that iron-deficient rats had significantly lower sucrase (19.5% lower) and lactase (56.8% lower) but not IAP-II activity than control rats. Kinetic properties of both enzymes remained unchanged from controls, suggesting a decrease in the quantity of enzyme present. Sucrase and lactase mRNA levels were reduced by 44.5% and 67.9%, respectively, by iron deficiency, suggesting that enzyme activity is controlled primarily by gene expression. Iron deficiency did not affect the pattern of protein and gene expression along the crypt to villus axis. Expression of PDX-1, a repressor of sucrase and lactase promoters, was 4.5-fold higher in iron deficiency, whereas CDX-2, GATA-4, and HNF-1 levels were not significantly different. These data suggest that decreases in sucrase and lactase activities result from a reduction in gene expression, following from increased levels of the transcriptional repressor PDX-1.anemia; transcription; nutrition; pancreatic duodenal homeobox CARBOHYDRATES are a vitally important dietary component, and disaccharidases are an essential subset of digestive enzymes required for the terminal step of carbohydrate digestion (13). The enzymatic activity of each individual disaccharidase is influenced primarily by the dietary level of their corresponding substrate (2, 12), and, under normal conditions, this level of activity is controlled by the abundance of the mRNA encoding the proteins (12, 34). However, it has been shown on many occasions that dietary iron deficiency can cause a significant decrease in disaccharidase activity (2,4,5,9,16,20,31,38) and that this decrease is reversible by iron supplementation (9,20,38).It is unlikely that iron is directly required for disaccharidase activity (16) or that iron deficiency alters the kinetic properties of sucrase (5). In additio...

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Impact on Iron Status of Introducing Cow's Milk in the Second Six Months of Life

Penrod,

Anderson,

Acosta

1990

J. pediatr. gastroenterol. nutr.

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SummaryTo determine the impact on iron status of introducing cow's milk (CM) into the diet during the second 6 months of life, nutrient intake was assessed and iron status measured in 100 infants. Nutrient intake for 40 of the 45 infants, age 8 to 13 months, fed CM as the primary beverage for at least 3 months prior to the study and for 45 of 55 infants the same age fed a milk‐based infant formula (FF) as the primary beverage for at least 3 months were assessed. All infants in the study were healthy, and the majority were taking no medications or supplements other than vitamins or fluoride for 3 weeks prior to the assessment. Blood drawn by peripheral venipuncture was analyzed by Coulter Counter for complete blood count; plasma albumin, iron, ferritin, transferrin saturation, and total iron‐binding capacity were measured in all infants. CM‐fed infants had significantly lower mean iron and vitamin C intakes, plasma albumin, transferrin saturation, and ferritin than did FF infants. The frequency of low plasma iron, low transferrin saturation, and low plasma ferritin was significantly greater in CM‐fed than in FF infants. The percentage of subjects with three or more abnormal iron indices was more than twice as great in CM‐fed infants (58%) as in FF infants (23%). Feeding infants iron‐fortified formula to 12 months of age appears to deter iron deficiency.

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Small intestinal disaccharidase activities in experimental Iron and protein deficiency

Cited by 23 publications

References 25 publications

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

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

Decreased sucrase and lactase activity in iron deficiency is accompanied by reduced gene expression and upregulation of the transcriptional repressor PDX-1

Impact on Iron Status of Introducing Cow's Milk in the Second Six Months of Life

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