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

Details

Serval ID
serval:BIB_9F0D74B40AA6
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
Peptides from Lactobacillus hydrolysates of bovine milk caseins inhibit prolyl-peptidases of human colon cells.
Journal
Journal of Agricultural and Food Chemistry
Author(s)
Juillerat-Jeanneret L., Robert M.C., Juillerat M.A.
ISSN
1520-5118 (Electronic)
ISSN-L
0021-8561
Publication state
Published
Issued date
2011
Volume
59
Number
1
Pages
370-377
Language
english
Notes
Publication types: Journal Article ; Research Support, Non-U.S. Gov't
Abstract
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.
Keywords
Casein peptides, human colon cells, dipeptidyl proly-amino-peptidases, prolyl-oligo-peptidases, matrix metalloproteinases
Pubmed
Web of science
Create date
05/01/2011 11:23
Last modification date
20/08/2019 15:05
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