Casein Phosphopeptides Influence Calcium Uptake by Cultured Human Intestinal HT-29 Tumor Cells

Ferraretto, Anita; Signorile, Alessandra; Gravaghi, Claudia; Fiorilli, Amelia; Tettamanti, Guido

doi:10.1093/jn/131.6.1655

Cited by 91 publications

(87 citation statements)

References 36 publications

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“…Some studies (19,20) have investigated the formation of peptides in Parmigiano Reggiano and Grana Padano cheese and/or their digested products in vitro; however, this topic needs to be studied further, with particular emphasis on biopeptide formation. As att ested by Sforza et al (20), several known bioactive peptides were found to be present in Parmigiano Reggiano cheese samples; for example, phosphopeptides derived from the N-terminal part of β-casein, known for their mineral binding capacity and vehiculation activity (21), are present in Parmigiano Reggiano cheese aged for more than 16 months.…”

Section: Bioactive Peptides: General Descriptionmentioning

confidence: 81%

Cheese as Functional Food: The Example of Parmigiano Reggiano and Grana Padano

Summer

Formaggioni

Franceschi

et al. 2017

Food Technol. Biotechnol.

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SummaryItalian hard cooked types of cheese, like Parmigiano Reggiano and Grana Padano, are characterised by positive nutritional qualities. In fact, they contain substances that have particular biological activities, and therefore they can be fully considered, according to the defi nition given by the European Unit, as 'functional' foods. This short review concisely describes these components and the benefi cial eff ects related to their activities. The description of the biologically active components has been organised in the following paragraphs: protein and peptides, fat and lipids, carbohydrates and prebiotics, probiotic bacteria, vitamins, mineral salts, and components of dairy products active in disease prevention. In particular, several known bioactive peptides were found in Parmigiano Reggiano cheese samples: for example, phosphopeptides, which are known for their mineral-binding capacity and vehiculation activity, peptides with immunomodulatory activity, and angiotensin-converting enzyme-inhibitory peptides with anti-hypertensive eff ects. Among lipids, the role of conjugated linoleic acid and other fatt y acids present in these cheese types was taken into consideration. The presence of oligosaccharides with prebiotic properties and probiotic bacteria was also described. Finally, particular emphasis was given to highly available calcium and its impact on bone health.

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Section: Bioactive Peptides: General Descriptionmentioning

confidence: 81%

Cheese as Functional Food: The Example of Parmigiano Reggiano and Grana Padano

Summer

Formaggioni

Franceschi

et al. 2017

Food Technol. Biotechnol.

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“…Thus, the dietary protein might increase calcium solubility by stimulating gastric acid production (DelValle and Yamada, 1990;Schulte-Frohlinde et al, 1993). Furthermore, some products of protein digestion, such as casein, seem to enhance calcium intestinal absorption through direct interactions with calcium (Ferraretto et al, 2001;Erba et al, 2002).…”

Section: Modulations Of Intestinal Dietary Calcium Absorptionmentioning

confidence: 99%

Protein intake, calcium balance and health consequences

et al. 2011

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High-protein (HP) diets exert a hypercalciuric effect at constant levels of calcium intake, even though the effect may depend on the nature of the dietary protein. Lower urinary pH is also consistently observed for subjects consuming HP diets. The combination of these two effects was suspected to be associated with a dietary environment favorable for demineralization of the skeleton. However, increased calcium excretion due to HP diet does not seem to be linked to impaired calcium balance. In contrast, some data indicate that HP intakes induce an increase of intestinal calcium absorption. Moreover, no clinical data support the hypothesis of a detrimental effect of HP diet on bone health, except in a context of inadequate calcium supply. In addition, HP intake promotes bone growth and retards bone loss and low-protein diet is associated with higher risk of hip fractures. The increase of acid and calcium excretion due to HP diet is also accused of constituting a favorable environment for kidney stones and renal diseases. However, in healthy subjects, no damaging effect of HP diets on kidney has been found in either observational or interventional studies and it seems that HP diets might be deleterious only in patients with preexisting metabolic renal dysfunction. Thus, HP diet does not seem to lead to calcium bone loss, and the role of protein seems to be complex and probably dependent on other dietary factors and the presence of other nutrients in the diet.

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“…Furthermore, CPP-calcium phosphate complexes have been shown to be anticariogenic and to remineralize early stages of enamel caries in animal and human studies (12,15,(23)(24)(25). In summary, the ability to stabilize calcium phosphate and thereby enhance mineral solubility and bioavailability (26) confers upon the CPP the potential to be biological delivery vehicles for calcium and phosphate (27).…”

mentioning

confidence: 99%

Physicochemical Characterization of Casein Phosphopeptide-Amorphous Calcium Phosphate Nanocomplexes

Cross

Huq

Palamara

et al. 2005

Journal of Biological Chemistry

236

183

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Milk caseins stabilize calcium and phosphate ions and make them available to the neonate. Tryptic digestion of the caseins yields phosphopeptides from their polar Nterminal regions that contain clusters of phosphorylated seryl residues. These phosphoseryl clusters have been hypothesized to be responsible for the interaction between the caseins and calcium phosphate that lead to the formation of casein micelles. The casein phosphopeptides stabilize calcium and phosphate ions through the formation of complexes. The calcium phosphate in these complexes is biologically available for intestinal absorption and remineralization of subsurface lesions in tooth enamel. We have studied the structure of the complexes formed by the casein phosphopeptides with calcium phosphate using a range of physicochemical techniques including x-ray powder diffraction, scanning electron microscopy, transmission electron microscopy, and equilibrium binding analyses. The amorphous nature of the calcium phosphate phase was confirmed by two independent methods: x-ray powder diffraction and selected area diffraction. In solution, the ion activity product of a basic amorphous calcium phosphate phase was the only ion product that was a function of bound phosphate independent of pH, consistent with basic amorphous calcium phosphate being the phase stabilized by the casein phosphopeptides. Detailed investigations of calcium and calcium phosphate binding using a library of synthetic homologues and analogues of the casein phosphopeptides have revealed that although the fully phosphorylated seryl-cluster motif is pivotal for the interaction with calcium and phosphate, other factors are also important. In particular, calcium binding and calcium phosphate stabilization by the peptides was influenced by peptide net charge, length, and sequence.Bovine milk contains ϳ30 mM calcium and 22 mM inorganic phosphate in solution with most of the calcium (68%) and phosphate (47%) associated with the proteins ␣ S1 -, ␣ S2 -, ␤-, and -casein in casein micelles (1, 2). The ␣ S1 -, ␣ S2 -, and ␤-caseins have a number of Ser(P) residues in a specific motif, Ser(P) 3 -Glu 2 , that is involved in the interaction with calcium phosphate (3).Many techniques have been used to investigate the ultrastructure of the casein micelles. Although the structural details are still being elucidated, the casein micelles are believed to be roughly spherical particles with a radius of ϳ100 nm, dispersed in a continuous phase of water, salt, lactose, and whey proteins (4). The calcium phosphate isolated after exhaustive hydrazine deproteination of micelles has been reported to exhibit a fine and uniform granularity under the electron microscope with the particles consisting of small subunits of 2.5-nm diameter (5, 6). The calcium phosphate, present as nanometer-sized ion clusters, and caseins are not covalently bound; hence the casein micelle is known as an association colloid (7). Nevertheless, the casein micelles are extremely stable and can withstand boiling, freeze-drying, and the add...

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Casein Phosphopeptides Influence Calcium Uptake by Cultured Human Intestinal HT-29 Tumor Cells

Cited by 91 publications

References 36 publications

Cheese as Functional Food: The Example of Parmigiano Reggiano and Grana Padano

Cheese as Functional Food: The Example of Parmigiano Reggiano and Grana Padano

Protein intake, calcium balance and health consequences

Physicochemical Characterization of Casein Phosphopeptide-Amorphous Calcium Phosphate Nanocomplexes

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