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β-Casein(94-123)-derived peptides differently modulate production of mucins in intestinal goblet cells

Published online by Cambridge University Press:  22 October 2014

Pascale Plaisancié ,
Rachel Boutrou ,
Monique Estienne ,
Gwénaële Henry ,
Julien Jardin ,
Armelle Paquet  and
Joëlle Léonil
Pascale Plaisancié*
Affiliation:
INRA USC1235, INSERM U1060, CarMeN Laboratory, University Lyon-1, INSA-Lyon, IMBL, Bât. Louis Pasteur, 20 av. Albert Einstein, 69621, F-69100 Villeurbanne, France
Rachel Boutrou
Affiliation:
INRA, UMR1253 Science et Technologie du Lait et de l'Œuf, F-35000 Rennes, France AGROCAMPUS OUEST, UMR1253 Science et Technologie du Lait et de l'Œuf, F-35000 Rennes, France
Monique Estienne
Affiliation:
INRA USC1235, INSERM U1060, CarMeN Laboratory, University Lyon-1, INSA-Lyon, IMBL, Bât. Louis Pasteur, 20 av. Albert Einstein, 69621, F-69100 Villeurbanne, France
Gwénaële Henry
Affiliation:
INRA, UMR1253 Science et Technologie du Lait et de l'Œuf, F-35000 Rennes, France AGROCAMPUS OUEST, UMR1253 Science et Technologie du Lait et de l'Œuf, F-35000 Rennes, France
Julien Jardin
Affiliation:
INRA, UMR1253 Science et Technologie du Lait et de l'Œuf, F-35000 Rennes, France AGROCAMPUS OUEST, UMR1253 Science et Technologie du Lait et de l'Œuf, F-35000 Rennes, France
Armelle Paquet
Affiliation:
INRA USC1235, INSERM U1060, CarMeN Laboratory, University Lyon-1, INSA-Lyon, IMBL, Bât. Louis Pasteur, 20 av. Albert Einstein, 69621, F-69100 Villeurbanne, France
Joëlle Léonil
Affiliation:
INRA, UMR1253 Science et Technologie du Lait et de l'Œuf, F-35000 Rennes, France AGROCAMPUS OUEST, UMR1253 Science et Technologie du Lait et de l'Œuf, F-35000 Rennes, France
*
*For correspondence; e-mail: pascale.plaisancie@inserm.fr
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Abstract

We recently reported the identification of a peptide from yoghurts with promising potential for intestinal health: the sequence (94-123) of bovine β-casein. This peptide, composed of 30 amino acid residues, maintains intestinal homoeostasis through production of the secreted mucin MUC2 and of the transmembrane-associated mucin MUC4. Our study aimed to search for the minimal sequence responsible for the biological activity of β-CN(94-123) by using several strategies based on (i) known bioactive peptides encrypted in β-CN(94-123), (ii) in silico prediction of peptides reactivity and (iii) digestion of β-CN(94-123) by enzymes of intestinal brush border membranes. The revealed sequences were tested in vitro on human intestinal mucus-producing HT29-MTX cells. We demonstrated that β-CN(108-113) (an ACE-inhibitory peptide) and β-CN(114-119) (an opioid peptide named neocasomorphin-6) up-regulated MUC4 expression whereas levels of the secreted mucins MUC2 and MUC5AC remained unchanged. The digestion of β-CN(94-123) by intestinal enzymes showed that the peptides β-CN(94-108) and β-CN(117-123) were present throughout 1·5 to 3 h of digestion, respectively. These two peptides raised MUC5AC expression while β-CN(117-123) also induced a decrease in the level of MUC2 mRNA and protein. In addition, this inhibitory effect was reproduced in airway epithelial cells. In conclusion, β-CN(94-123) is a multifunctional molecule but only the sequence of 30 amino acids has a stimulating effect on the production of MUC2, a crucial factor of intestinal protection.

Keywords

Milk bioactive peptidesβ-caseinintestinal barrierintestinal protectionmucus
Type
Research Article
Information
Journal of Dairy Research , Volume 82 , Issue 1 , February 2015 , pp. 36 - 46
Copyright
Copyright © Proprietors of Journal of Dairy Research 2014 

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