Influence of Dietary Protein Level and Origin on the Flow of Mucin Along the Small Intestine of the Preruminant Calf

Montagné, Lucile; Toullec, R.; Formal, Michèle; Lallès, Jean Paul

doi:10.3168/jds.s0022-0302(00)75181-2

Cited by 40 publications

(51 citation statements)

References 21 publications

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“…Using a specific enzyme-linked immunosorbent assay (ELISA), investigators in our laboratory measured the flow of mucin along the small intestine of preruminant calves that were fed a protein-free diet. 13,14 The basal flow of mucin protein at the duodenum, jejunum, and ileum was 1.1, 1.8, and 4.0 g/kg DMI, respectively (i.e., 2.1, 3.4, and 7.5 g mucin/kg DMI). The latter value at the ileum was twice the value obtained in pigs (3.9 g/kg DMI).…”

Section: Roles In Relation With Gut Healthmentioning

confidence: 99%

“…1 Nevertheless, in these calves, the contribution of mucin amino acids to the total flow of amino acids was quite high for lysine (40%), and to a lesser extent for glutamic acid (29%), and threonine, serine, and aspartic acid (25% each). 14 We also measured the flow of mucin protein at the duodenum, which originate from the upper GIT and the stomach. This would represent 25% of the ileal loss of mucin protein, 14 which concurs with the value in pigs provided by Lien et al 11…”

Section: Roles In Relation With Gut Healthmentioning

confidence: 99%

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Effect of Diet on Mucin Kinetics and Composition: Nutrition and Health Implications

Montagne¹,

Piel²,

Lallès³

2004

Nut. Rev.

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The mucus gel covering the gut epithelium is in dynamic balance between synthesis and secretion of mucin from goblet cells and proteolytic and physical erosion that releases mucin into the lumen. In the lumen, mucin is partially protected from proteolysis by carbohydrate chains, and it contributes to endogenous protein reaching the ileum. Dietary components modulate the contribution of mucin to endogenous protein components and their qualitative composition. In addition, mucin plays a key role in gastrointestinal protection in association with the microflora. In this review, we will attempt to evaluate the consequences of dietary manipulation of mucin on gut health.

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Section: Roles In Relation With Gut Healthmentioning

confidence: 99%

Section: Roles In Relation With Gut Healthmentioning

confidence: 99%

Effect of Diet on Mucin Kinetics and Composition: Nutrition and Health Implications

Montagne¹,

Piel²,

Lallès³

2004

Nut. Rev.

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“…Phytate was probably present in both soya preparations (57) and may have triggered these increases in alkaline phosphatase activity. Therefore, it is noteworthy that Montagne et al (61) found that both soya preparations substantially increased the flow of mucin protein in the duodenum, jejunum and ileum in pre-ruminant calves by approximately 70 -90%. Moreover, Montagne et al (62) determined the effect of these partial substitutions on the apparent digestibility of cystine, lysine and threonine at the jejunal and ileal levels.…”

Section: Ternary Protein -Phytate Complexesmentioning

confidence: 99%

Protein–phytate interactions in pig and poultry nutrition: a reappraisal

et al. 2012

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Protein–phytate interactions are fundamental to the detrimental impact of phytate on protein/amino acid availability. The inclusion of exogenous phytase in pig and poultry diets degrades phytate to more innocuous esters and attenuates these negative influences. The objective of the present review is to reappraise the underlying mechanisms of these interactions and reassess their implications in pig and poultry nutrition. Protein digestion appears to be impeded by phytate in the following manner. Binary protein–phytate complexes are formed at pH levels less than the isoelectric point of proteins and complexed proteins are refractory to pepsin digestion. Once the protein isoelectric points are exceeded binary complexes dissociate; however, the isoelectric point of proteins in cereal grains may be sufficiently high to permit these complexes to persist in the small intestine. Ternary protein–phytate complexes are formed at pH levels above the isoelectric point of proteins where a cationic bridge links the protein and phytate moieties. The molecular weights of protein and polypeptides in small-intestinal digesta may be sufficient to allow phytate to bind nutritionally important amounts of protein in ternary complexes. Thus binary and ternary complexes may impede protein digestion and amino acid absorption in the small intestine. Alternatively, phytate may interact with protein indirectly.Myo-inositol hexaphosphate possesses six phosphate anionic moieties (HPO42–) that have strong kosmotropic effects and can stabilise proteins by interacting with the surrounding water medium. Phytate increases mucin secretions into the gut, which increases endogenous amino acid flows as the protein component of mucin remains largely undigested. Phytate promotes the transition of Na+into the small-intestinal lumen and this suggests that phytate may interfere with glucose and amino acid absorption by compromising Na+-dependent transport systems and the activity of the Na pump (Na+-K+-ATPase). Starch digestion may be depressed by phytate interacting with proteins that are closely associated with starch in the endosperm of cereal grains. While elucidation is required, the impacts of dietary phytate and exogenous phytase on the site, rate and synchrony of glucose and amino acid intestinal uptakes may be of importance to efficient protein deposition. Somewhat paradoxically, the responses to phytase in the majority of amino acid digestibility assays in pigs and poultry are equivocal. A brief consideration of the probable reasons for these inconclusive outcomes is included in this reappraisal.

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“…11,12 The control diet was based on skim milk powder. The other three diets contained a mixture of skim milk powder and plant products.…”

Section: Materials and Methods Dietsmentioning

confidence: 99%

Enzymes of the small intestine of the calf: effect of dietary protein source on the activities of some enzymes in the small intestinal mucosa and digesta

Montagné¹,

Salgado²,

Toullec³

et al. 2002

J Sci Food Agric

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The objective of this study was to examine the effect of dietary protein source on the morphology and enzyme activities in the small intestinal mucosa and digesta of preruminant calves. The control diet contained skim milk powder. Plant proteins from soy concentrate (unhydrolysed or partially hydrolysed) and potato concentrate were incorporated into experimental diets. Duodenal, jejunal and ileal mucosal biopsies and digesta were collected from calves fitted with simple cannulae and continuously infused with milk replacers into the abomasum. Biopsies were used for morphology measurements. The activity of dipeptidylpeptidase IV, aminopeptidases, lactase and alkaline phosphatase was estimated in biopsies and digesta. Incorporating plant protein had a limited effect on the intestinal mucosa. A partial villus atrophy and crypt hyperplasia were noted with the soy concentrate only. Decreases in the activity of dipeptidylpeptidase IV with the potato concentrate diet and of aminopeptidase N and lactase with the hydrolysed soy concentrate diet, were also observed in ileal biopsies. Mucosal enzymes were released in the lumen and most of them accumulated in digesta of the distal small intestine. The activity of aminopeptidase N and lactase in ileal digesta was higher in calves fed the soy and potato concentrate diets than in those fed the control diet.

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Influence of Dietary Protein Level and Origin on the Flow of Mucin Along the Small Intestine of the Preruminant Calf

Cited by 40 publications

References 21 publications

Effect of Diet on Mucin Kinetics and Composition: Nutrition and Health Implications

Effect of Diet on Mucin Kinetics and Composition: Nutrition and Health Implications

Protein–phytate interactions in pig and poultry nutrition: a reappraisal

Enzymes of the small intestine of the calf: effect of dietary protein source on the activities of some enzymes in the small intestinal mucosa and digesta

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