Peptides from Lactobacillus hydrolysates of bovine milk caseins inhibit prolyl-peptidases of human colon cells.

Détails

ID Serval
serval:BIB_9F0D74B40AA6
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
Peptides from Lactobacillus hydrolysates of bovine milk caseins inhibit prolyl-peptidases of human colon cells.
Périodique
Journal of Agricultural and Food Chemistry
Auteur(s)
Juillerat-Jeanneret L., Robert M.C., Juillerat M.A.
ISSN
1520-5118 (Electronic)
ISSN-L
0021-8561
Statut éditorial
Publié
Date de publication
2011
Volume
59
Numéro
1
Pages
370-377
Langue
anglais
Notes
Publication types: Journal Article ; Research Support, Non-U.S. Gov't
Résumé
Prolyl-rich peptides derived from hydrolysates of bovine caseins have been previously shown to inhibit angiotensin converting enzyme (ACE) activity, suggesting that they may also be able to inhibit the enzymatic activities of prolyl-specific peptidases. This study shows that peptides derived from α(S1)-casein and β-casein inhibited the enzymatic activities of purified recombinant matrix metalloprotease (MMP)-2, MMP-7, and MMP-9. The inhibitory efficacy was sequence-dependent. These peptides also selectively inhibited the enzymatic activities of prolyl-amino-peptidases, prolyl-amino-dipeptidases, and prolyl-endopeptidases in extracts of HT-29 and SW480 human colon carcinoma cells, but not in intact cells. They were not cytotoxic or growth inhibitory for these cells. Thus, the prolyl-rich selected peptides were good and selective inhibitors of MMPs and post-proline-cleaving proteases, demonstrating their potential to control inadequate proteolytic activity in the human digestive tract, without inducing cytotoxic effects.
Mots-clé
Casein peptides, human colon cells, dipeptidyl proly-amino-peptidases, prolyl-oligo-peptidases, matrix metalloproteinases
Pubmed
Web of science
Création de la notice
05/01/2011 11:23
Dernière modification de la notice
20/08/2019 15:05
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