Peptic erosion of gastric mucus in the rat

Munster, D; Bagshaw, Philip; Wilson, J G

doi:10.1016/0300-9629(87)90159-9

Cited by 13 publications

(7 citation statements)

References 15 publications

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“…Allen et al (1990) illustrated this relationship in the context of the mucus gel in ulceration, indicating that proteolytic degradation weakens mucus gels, making these more susceptible to the physical forces of digestion. The introduction of pepsin into the stomach of rats caused a linear increase in the recovery of mucin up to a pepsin concentration of 1 mg/mL (Munster et al, 1987). There were no differences in mucin outputs as the pepsin concentration was increased from 1 to 2 mg/mL.…”

Section: Degradation Of Mucus In the Stomach And Small Intestinementioning

confidence: 86%

“…There were no differences in mucin outputs as the pepsin concentration was increased from 1 to 2 mg/mL. Addition of a 10-fold excess of bovine serum albumin to the stomach resulted in a 60% reduction in the effect of pepsin on glycoprotein recovery (Munster et al, 1987). Furthermore, peptic degradation of mucus is reduced in the presence of ethanol, a pepsin denaturant (Laszewicz et al, 1985).…”

Section: Degradation Of Mucus In the Stomach And Small Intestinementioning

confidence: 94%

“…Increased pepsin concentration is positively correlated with glycoprotein output (Allen et al, 1980;Munster et al, 1987) and the amount of degraded subunits (Allen et al, 1980;Laszewicz et al, 1985). It is, therefore, proposed that proteolytic enzymes continuously erode mucus gels throughout the gastrointestinal tract.…”

Section: Degradation Of Mucus In the Stomach And Small Intestinementioning

confidence: 99%

See 2 more Smart Citations

Dietary influences on the secretion into and degradation of mucin in the digestive tract of monogastric animals and humans

Lien¹,

Sauer²,

Jian-xin³

2001

J. Anim. Feed Sci.

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Current information on the effect of diet on the secretion of mucus and the recovery of mucin in ileal digesta is summarized. A general description of mucus structure and its degradation in the small and large intestine is provided. As the protective lining of the entire gastrointestinal tract, mucus gels are exposed to all chemical and physical forces of digestion. Most important among these is the proteolytic breakdown of mucus gels into component mucin subunits and their subsequent release into the intestinal lumen. Erosion of mucus gels is countered by synthesis and secretion from the underlying epithelium. Diets can influence this process, both indirectly by their effects on digestive processes most importantly with respect to the amount and distribution of proteolytic enzymes in the intestinal lumen, and directly by the physical forces which they exert on the gastrointestinal mucosa. Adaptive changes in goblet cell activity have been noted in response to different diets. Once in the intestinal lumen, little further degradation of mucus occurs prior to the large intestine. Once in the large intestine mucin is fermented by resident microbial populations. The recovery of undegraded mucin in ileal digesta has important implications for nutritional studies: firstly because it may represent a considerable loss of endogenous amino acids and carbohydrates and secondly because it may provide insight into the effects of diets on the digestive tract itself.

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Section: Degradation Of Mucus In the Stomach And Small Intestinementioning

confidence: 86%

Section: Degradation Of Mucus In the Stomach And Small Intestinementioning

confidence: 94%

Section: Degradation Of Mucus In the Stomach And Small Intestinementioning

confidence: 99%

See 1 more Smart Citation

Dietary influences on the secretion into and degradation of mucin in the digestive tract of monogastric animals and humans

Lien¹,

Sauer²,

Jian-xin³

2001

J. Anim. Feed Sci.

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“…Gastric installation of pepsin has been shown to increase mucin secretion in rats (Munster et al, 1987), so it is noteworthy that phytate stimulates mucin secretion in broilers, which is counteracted by phytase (Cowieson et al, 2004). Possibly, this increased mucin secretion is stimulated by additional outputs of pepsin and hydrochloric acid induced by protein-phytate complexes.…”

Section: Probable Underlying Mechanismsmentioning

confidence: 97%

Phytate-degrading enzymes in pig nutrition

2008

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“…For example, increased gastric mucin secretions in response to pepsin infusion have been demonstrated in rats (82) . Importantly, as first reported by Cowieson et al (83) , phytate increases mucin and Na excretion in broilers, which is ameliorated by phytase.…”

Section: Implications Of Binary 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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Peptic erosion of gastric mucus in the rat

Cited by 13 publications

References 15 publications

Dietary influences on the secretion into and degradation of mucin in the digestive tract of monogastric animals and humans

Dietary influences on the secretion into and degradation of mucin in the digestive tract of monogastric animals and humans

Phytate-degrading enzymes in pig nutrition

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

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