Adhesion of bacteria to mucosal surfaces?an area of increasing importance in diarrhoeal disease

Candy, D. C. A.

doi:10.1007/bf00442395

Cited by 4 publications

(1 citation statement)

References 38 publications

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“…Despite this widespre ad exposure, however , their co ntribution to human health problem s currently rem ains unkn own. Of int erest in this regard is the suggestion by some investigator s (30 ,31) that lectin-type interactions may be important in the etiology of tropical sprue (33) , celiac disea se (34), and chronic infantile diarrhea (35). Th ough it is still too early to evaluate the validity of these hypotheses, our results and those of others indicate that further investigation in thi s area is warranted .…”

Section: Discussionmentioning

confidence: 66%

Effect of Lectins on the Activity of Brush Border Membrane‐Bound Enzymes of Rat Small Intestine

Erickson,

Kim,

Sleisenger

et al. 1985

J. pediatr. gastroenterol. nutr.

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Highly purified microvillus membrane vesicles isolated from rat small intestine were enriched in sucrase, maltase, and aminopeptidase activities. Approximately 90–95% of each enzyme was released from the membrane fraction by treatment with detergent (Triton X‐100) and sonication. Using untreated and solubilized preparations, the effect of lectin binding on the activity of each of the three enzymes was measured. It was observed that wheat germ agglutinin (WGA) and phytohemagglutinin (PHA) dramatically enhanced the activity of membrane‐bound maltase but had much less effect on the detergent solubilized enzyme. Under the same conditions aminopeptidase activity was inhibited by WGA and PHA while sucrase activity was not affected. These alterations in enzyme activity occurred at lectin concentrations that also precipitated each solubilized enzyme from solution. Inhibitory sugars prevented the alterations in enzyme activity suggesting that the effect is due to the binding of lectin to specific carbohydrate structures. Enhancement of membrane‐bound maltase activity by WGA and PHA was shown to be temperature dependent indicating that the lipid environment of the microvillus membrane may play a role in mediating the lectin effect. A kinetic analysis of the changes in maltase activity induced by these two lectins was due solely to an increase in Vmax. Two other lectins used in this study (concanavalin A and Ricinus communis agglutinin) did not readily precipitate the enzymes in question or alter their activity. These results show that binding of lectins to brush border membranes can induce variable changes in the activity of several membrane associated hydrolases, and suggest that similar changes may occur in vivo in the presence of dietary lectin. The consequences of such alterations on the ability of the intestinal mucosa to hydrolyze and absorb various dietary constituents is at present unknown.

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Section: Discussionmentioning

confidence: 66%

Effect of Lectins on the Activity of Brush Border Membrane‐Bound Enzymes of Rat Small Intestine

Erickson,

Kim,

Sleisenger

et al. 1985

J. pediatr. gastroenterol. nutr.

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Lee

1985

Advances in Microbial Ecology

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Phytohemagglutinin-induced diarrheal disease

et al. 1984

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A purified plant lectin, phytohemagglutinin (PHA), or crude red kidney bean (RKB) from which it was derived, when incorporated as 1% of dietary protein into a purified casein protein diet caused weanling rats to fail to grow or lose weight in comparison to control animals pair fed an isonitrogenous, isocaloric diet. Feeding PHA was observed to cause diarrhea: fecal wet and dry weights were increased within 2 days after starting the diet. Increased fecal weight was caused by increased dry weight as well as by an increased fecal water content. On reversion to a normal casein diet, rapid amelioration of the antinutritional effects of PHA occurred with resumption of normal growth rate. Specific binding of PHA to the microvillus region of the small intestinal epithelium was demonstrated using rabbit anti-PHA and fluorescein-labeled goat anti-rabbit immunoglobin. PHA binding was observed after chronic intake in the diet or when applied to normal tissue in vitro. Loss of PHA binding to the intestine was observed to occur within 48 hr on reversion to a control casein diet. No significant morphological damage to the microvilli or the mucosal villus architecture was observed to accompany PHA adherence under these experimental conditions. Antinutritional and antiabsorptive effects of dietary PHA were associated with diarrhea. PHA adhered to the microvillus membrane of the small intestinal villus surface during the diarrheal state.(ABSTRACT TRUNCATED AT 250 WORDS)

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Adhesion of bacteria to mucosal surfaces?an area of increasing importance in diarrhoeal disease

Cited by 4 publications

References 38 publications

Effect of Lectins on the Activity of Brush Border Membrane‐Bound Enzymes of Rat Small Intestine

Effect of Lectins on the Activity of Brush Border Membrane‐Bound Enzymes of Rat Small Intestine

Neglected Niches

Phytohemagglutinin-induced diarrheal disease

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