Peptides surviving the simulated gastrointestinal digestion of milk proteins: Biological and toxicological implications

Picariello, Gianluca; Ferranti, Pasquale; Fierro, Olga; Mamone, Gianfranco; Caira, Simonetta; Luccia, Aldo Di; Monica, Stefano; Addeo, Francesco

doi:10.1016/j.jchromb.2009.11.033

Cited by 175 publications

(149 citation statements)

References 76 publications

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“…The major allergens of cow's milk (CM) are betalactoglobulin (b-LG) and alpha-S1-casein, as indicated by large population studies (3). These proteins are also highly resistant to proteolysis by gastrointestinal enzymes, resulting in large peptides at the site of mucosal immune system with implications for immune reactivity and cow's milk allergy (CMA) emergence (4).…”

mentioning

confidence: 99%

Peripheral Blood Immune Response Elicited by Beta-Lactoglobulin in Childhood Cow's Milk Allergy

et al. 2011

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Several studies analyzing the immune responses in patients with cow's milk allergy (CMA) have used T-cell lines or T-cell clones that require prolonged in vitro cell culturing and may result in a switched cell phenotype and function. We investigated immune responses to beta-lactoglobulin (b-LG) in peripheral blood mononuclear cells after a short in vitro antigen stimulation in children with acute CMA (both IgE-mediated and non-IgE-mediated forms) and in those who outgrew an IgE-mediated CMA. Healthy controls were also investigated. Peripheral blood mononuclear cells were assayed for IL-13, IFN-␥, IL-4, and IL-10. Although b-LG induced a cytokine production and/or cell proliferation almost in all children, included healthy controls, differences were observed among the four groups. Children with IgE-mediated CMA had a marked Th2-response, with high IL-13 production and proliferation, but low IFN-␥; by contrast, children with non-IgE-mediated CMA produced no, or very low, IL-13 and cell proliferation. Children, who outgrew CMA, showed a shift to a Th1-response, with reduced IL-13 and increased IFN-␥. IL-10-responses were high in all groups, with the highest level in healthy children; by contrast, IL-4 was undetectable in all children. This study highlights the use of shortly stimulated peripheral blood cells to investigate the food-induced immune responses. (Pediatr Res 70: 549-554, 2011)

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Peripheral Blood Immune Response Elicited by Beta-Lactoglobulin in Childhood Cow's Milk Allergy

et al. 2011

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“…Ten out of 19 CPP contained SerP available for binding minerals, and four of these peptides, s1-CN (f57-90)5P, s1-CN (f56-90)5P, s1-CN (f55-76)5P, -CN (f1-52)5P, were reported for the first time in the CN digests [42]. Only -CN (f1-25)4P, 3P and 2P survived the simulated gastrointestinal digest of CN [43].…”

Section: Bioactive Peptides Released In Vitro By the Hydrolysis Of MImentioning

confidence: 99%

Bioactive Casein Phosphopeptides in Dairy Products as Nutraceuticals for Functional Foods

Pinto¹,

Caira²,

Cuollo³

et al. 2012

Milk Protein

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“…To this end, a simulated digestion of bovine milk proteins in vitro that includes the sequential use of pepsin, pancreatic proteases, and extracts of human intestinal brush border membranes, has allowed the identification of produced peptides by MS. The presence of characteristic β-Lg resistant peptides could implicate β-Lg in the case of a cow's milk allergy [132]. The identification by MS of peptides arising from simulated digestion is complicated by a lack of enzyme specificity.…”

Section: Standardization Of Allergen Preparationsmentioning

confidence: 99%

Allergenicity of Milk Proteins

Caira¹,

Pizzano²,

Picariello³

et al. 2012

Milk Protein

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Peptides surviving the simulated gastrointestinal digestion of milk proteins: Biological and toxicological implications

Cited by 175 publications

References 76 publications

Peripheral Blood Immune Response Elicited by Beta-Lactoglobulin in Childhood Cow's Milk Allergy

Peripheral Blood Immune Response Elicited by Beta-Lactoglobulin in Childhood Cow's Milk Allergy

Bioactive Casein Phosphopeptides in Dairy Products as Nutraceuticals for Functional Foods

Allergenicity of Milk Proteins

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