Intestinal Transport of the Lactokinin Ala‐Leu‐Pro‐Met‐His‐Ile‐Arg through a Caco‐2 Bbe Monolayer

Intestinal Transport of the Lactokinin Ala‐Leu‐Pro‐Met‐His‐Ile‐Arg through a Caco‐2... ACE inhibitory peptides are biologically active peptides that play a role in blood pressure regulation. When derived from food proteins during food processing or gastrointestinal digestion, these peptides could function as efficient agents in treating and preventing hypertension. However, in order to exert an antihypertensive effect by inhibition of the ACE enzyme, they have to reach the bloodstream intact. The aim of this research was to assess if the known ACE inhibitory peptide Ala‐Leu‐Pro‐Met‐His‐Ile‐Arg, derived from a tryptic digest of β‐lactoglobulin, could be absorbed through a Caco‐2 Bbe cell monolayer in an Ussing chamber and reach the serosal side undegraded. Samples of the mucosal compartment showed high ACE inhibitory activity. No or only little ACE inhibitory activity was detected in the serosal compartment. However, when the serosal sample was concentrated three‐fold, a substantial ACE inhibitory activity was registered. Concomitantly, HPLC and MS clearly showed the presence of Ala‐Leu‐Pro‐Met‐His‐Ile‐Arg in the mucosal compartment, whereas in the serosal compartment only MS was able to detect the heptapeptide. In conclusion, under the observed experimental conditions, the ACE inhibitory peptide Ala‐Leu‐Pro‐Met‐His‐Ile‐Arg was transported intact through the Caco‐2 Bbe monolayer, but in concentrations too low to exert an ACE inhibitory activity. Copyright © 2002 European Peptide Society and John Wiley & Sons, Ltd. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Journal of Peptide Science Wiley

Intestinal Transport of the Lactokinin Ala‐Leu‐Pro‐Met‐His‐Ile‐Arg through a Caco‐2 Bbe Monolayer

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Publisher
Wiley
Copyright
Copyright © 2002 Wiley Subscription Services
ISSN
1075-2617
eISSN
1099-1387
D.O.I.
10.1002/psc.371
Publisher site
See Article on Publisher Site

Abstract

ACE inhibitory peptides are biologically active peptides that play a role in blood pressure regulation. When derived from food proteins during food processing or gastrointestinal digestion, these peptides could function as efficient agents in treating and preventing hypertension. However, in order to exert an antihypertensive effect by inhibition of the ACE enzyme, they have to reach the bloodstream intact. The aim of this research was to assess if the known ACE inhibitory peptide Ala‐Leu‐Pro‐Met‐His‐Ile‐Arg, derived from a tryptic digest of β‐lactoglobulin, could be absorbed through a Caco‐2 Bbe cell monolayer in an Ussing chamber and reach the serosal side undegraded. Samples of the mucosal compartment showed high ACE inhibitory activity. No or only little ACE inhibitory activity was detected in the serosal compartment. However, when the serosal sample was concentrated three‐fold, a substantial ACE inhibitory activity was registered. Concomitantly, HPLC and MS clearly showed the presence of Ala‐Leu‐Pro‐Met‐His‐Ile‐Arg in the mucosal compartment, whereas in the serosal compartment only MS was able to detect the heptapeptide. In conclusion, under the observed experimental conditions, the ACE inhibitory peptide Ala‐Leu‐Pro‐Met‐His‐Ile‐Arg was transported intact through the Caco‐2 Bbe monolayer, but in concentrations too low to exert an ACE inhibitory activity. Copyright © 2002 European Peptide Society and John Wiley & Sons, Ltd.

Journal

Journal of Peptide ScienceWiley

Published: Jan 1, 2002

Keywords: ; ; ; ; ; ;

References

  • Antihypertensive peptides derived from food proteins
    Yamamoto, N
  • Tissue Utilization and Clinical Targeting
    Grimble, GK; Backwell, FRC
  • Characterization of the enterocyte‐like brush‐border cytoskeleton of the C2bbe clones of the human intestinal‐cell line, Caco‐2
    Peterson, MD; Mooseker, MS

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