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

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.

• Authors: Lucienne Juillerat-Jeanneret, Marie-Claude Robert, Marcel A Juillerat
• Journal: Journal of agricultural and food chemistry (J Agric Food Chem) Vol. 59 Issue 1 Pg. 370-7 (Jan 12 2011) ISSN: 1520-5118 [Electronic] United States
• PMID: 21126072 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Angiotensin-Converting Enzyme Inhibitors
• Caseins
• Peptides
• Peptidyl-Dipeptidase A

Topics

• Amino Acid Sequence
• Angiotensin-Converting Enzyme Inhibitors (chemistry, metabolism, pharmacology)
• Animals
• Caseins (chemistry, metabolism)
• Cattle
• Cell Line, Tumor
• Colonic Neoplasms (enzymology, microbiology)
• Down-Regulation
• Humans
• Lactobacillus (metabolism)
• Milk (microbiology)
• Molecular Sequence Data
• Peptides (chemistry, metabolism, pharmacology)
• Peptidyl-Dipeptidase A (metabolism)