Bioavailability of caseinophosphopeptide-bound iron

Aît-Oukhatar, Nabil; Pérès, Jean Michel; Bouhallab, Saı̈d; Neuville, Dominique; Bureau, F.; Bouvard, G.; Arhan, Pierre; Bouglé, Dominique

doi:10.1067/mlc.2002.128146

Cited by 63 publications

(35 citation statements)

References 23 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…It is known that milk -casein and products of its hydrolysis are more than just nutrients. Some of the peptides derived from milk casein are capable of affecting biological functions of the organism (Morita et al, 2004;Kilara and Panyam, 2003;Florisa et al, 2003;Clare et al, 2003;Bouhallab et al, 2002;Ait-Oukhatar et al, 2002). These effects can be antimicrobial and probiotic, i.e.…”

Section: Discussionmentioning

confidence: 97%

Casein-hydrolyzing activity of sIgA antibodies from human milk

2005

View full text Add to dashboard Cite

During pregnancy and immediately after delivery (i.e. at the beginning of lactation), the female organism is frequently characterized by an immune status similar to that of patients with autoimmune diseases. In addition, lactation is associated with an appearance of catalytically active antibodies or abzymes (Abzs) with DNAse, RNase, ATPase, amylolitic, protein kinase and lipid kinase activities in breast milk. However, until now there were no examples of human milk Abzs with a proteolytic activity. We present the first evidence that electrophoretically and immunologically homogeneous human milk sIgAs possess a beta-casein-hydrolyzing activity different from known proteases. Abzs specifically hydrolyze both human and bovine beta-caseins but not many other proteins tested. Using different methods including in situ analysis of proteolytic activity in a gel after SDS-PAGE it was shown that the observed proteolytic activity is an intrinsic property of human milk polyclonal sIgAs. Specific inhibitors of acidic and thiol proteases demonstrated a weak effect on proteolytic activity of Abzs, while a specific inhibitor of serine proteases (AEBSF) significantly inhibited the proteolytic activity of the abzymes. The K(M) value for human casein as a substrate was estimated (7.3 microM). Our findings suggest that the immune system of clinically healthy mothers can generate IgAs with a beta-casein-specific serine protease-like activity.

show abstract

Section: Discussionmentioning

confidence: 97%

Casein-hydrolyzing activity of sIgA antibodies from human milk

2005

View full text Add to dashboard Cite

show abstract

“…␤ -CPP(1-25) binds Fe tightly by its cluster of 4 phosphoseryl residues, which keeps it soluble and protects it from further digestion [11] , so it is easily taken up by the mucosa and corrects iron deficiency [5,6] .…”

Section: Discussionmentioning

confidence: 99%

“…In addition, experimental [5] and human [6] studies have previously show that ␤ -CPP(1-25) enhances iron absorption.…”

Section: Introductionmentioning

confidence: 99%

Caseinophosphopeptide-Bound Iron: Protective Effect against Gut Peroxidation

Kibangou¹,

Bouhallab

Bureau

et al. 2008

Ann Nutr Metab

View full text Add to dashboard Cite

Background: Peptides derived from cow’s milk proteins have in vitro protective effects on iron-induced peroxidation that could be used to prevent the side effects of iron fortification. The aim of the study was to confirm these properties in an in vivo model of gut peroxidation. Methods: Iron bound to the 1–25 phosphopeptide of β-casein [Fe-β-CPP(1–25)] was compared to an encapsulated ferric pyrophosphate (Fe-P) in the Caco-2 model. Ferrous sulfate (FeSO₄) was used as control (100 µmol/l iron, n = 6 per group). The concentration of malondialdehyde (MDA), a stable byproduct of lipid peroxidation, was used as the marker of peroxidation. Results: The lowest MDA levels were observed in cells grown with Fe-β-CPP(1–25) and the highest with Fe-P. Iron absorption of Fe-β-CPP(1–25) was higher than in the 2 other forms, due to its high cellular uptake and high basolateral transfer, while iron absorption of Fe-P showed high uptake and high cell retention. Conclusions: The enhancing effect of β-CPP(1–25) on iron absorption was associated with a protective effect against enterocyte peroxidation, perhaps due to its low storage by enterocytes. These observations support a role for specific milk components in food fortification to prevent iron deficiency.

show abstract

“…1) and can fix 4 to 5 iron atoms with a high affinity [2,9]. At first, the studies in rats have allowed to show the efficiency of β(1-25) on the absorption and bioavailability of iron [10], an efficiency that was confirmed in a first clinical study [11]. Then, the mechanism of absorption of iron associated with the phosphopeptide as well as the effect of the presence of other minerals (zinc) were studied using the perfusion of a ligated rat duodenal loop segment [12][13][14].…”

Section: Phosphopeptides and Bioavailability Of Mineralsmentioning

confidence: 90%

“…These results obtained in the rat were confirmed in a preliminary clinical study, comparing Fe/β(1-25) and iron sulphate. The quantity of iron stocked in the organs seven days after the ingestion of a unique dosage is higher in the group having received the Fe/β(1-25) complex [11].…”

Section: Bioavailability Of Iron Complexed To the β(1-25) Phosphopeptidementioning

confidence: 96%

Biopeptides of milk: caseinophosphopeptides and mineral bioavailability

Bouhallab

Bouglé

2004

Reprod. Nutr. Dev.

View full text Add to dashboard Cite

-The biological and physiological activities of milk proteins are partially attributed to several peptides encrypted in the protein molecules. These peptides can be liberated by enzymatic digestion in vitro and in vivo. Among the biologically active molecules, phosphorylated peptides (caseinophosphopeptides, CPP) are known to exert an effect on calcium metabolism but also on other minerals. While the existing discrepancy on the potential role of CPP on calcium availability has not been clarified, the results of our previous studies showed that a purified phosphopeptide (β(1-25)) exhibits a positive effect on iron bioavailability in vivo. Here we report the main results on the efficiency of β(1-25) in the absorption and availability of iron as well as on the mechanism involved. milk / bioactive peptide / phosphopeptide / iron bioavailability

show abstract

Bioavailability of caseinophosphopeptide-bound iron

Cited by 63 publications

References 23 publications

Casein-hydrolyzing activity of sIgA antibodies from human milk

Casein-hydrolyzing activity of sIgA antibodies from human milk

Caseinophosphopeptide-Bound Iron: Protective Effect against Gut Peroxidation

Biopeptides of milk: caseinophosphopeptides and mineral bioavailability

Contact Info

Product

Resources

About