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Bioavailability of angiotensin I converting enzyme inhibitory peptides

Vanessa Vermeirssen, John Van Camp UGent and Willy Verstraete UGent (2004) BRITISH JOURNAL OF NUTRITION. 92(3). p.357-366
abstract
Hypertension or high blood pressure is a significant health problem worldwide. Bioactive peptides that inhibit angiotensin I converting enzyme (ACE) in the cardiovascular system can contribute to the prevention and treatment of hypertension. These ACE inhibitory peptides are derived from many food proteins, especially milk proteins. An ACE inhibitory activity in vitro does not always imply an antihypertensive effect in vivo. Even if it does, it is very difficult to establish a direct relationship between in vitro and in vivo activity. This is mainly due to the bioavailability of the ACE inhibitory peptides after oral administration and the fact that peptides may influence blood pressure by mechanisms other than ACE inhibition. To exert an antihypertensive effect after oral ingestion, ACE inhibitory peptides have to reach the cardiovascular system in an active form. Therefore, they need to remain active during digestion by human proteases and be transported through the intestinal wall into the blood. The bioavailability of some ACE inhibitory peptides has been studied. It is also known that (hydroxy)proline-containing peptides are generally resistant to degradation by digestive enzymes. Peptides can be absorbed intact through the intestine by paracellular and transcellular routes, but the potency of the bioactivity after absorption is inversely correlated to chain length. In addition, some strategies are proposed to increase the bioavailability of ACE inhibitory peptides. Further research into the bioavailability of ACE inhibitory peptides will lead to the development of more effective ACE inhibitory peptides and foods.
Please use this url to cite or link to this publication:
author
organization
year
type
journalArticle (review)
publication status
published
subject
keyword
FOOD PROTEINS, ANTIHYPERTENSIVE PEPTIDE, BLOOD-PRESSURE, BIOACTIVE PEPTIDES, HIS-ILE-ARG, HUMAN INTESTINAL-CELL, SPONTANEOUSLY HYPERTENSIVE-RATS, intestinal transport, gastrointestinal digestion, bioactive peptides, hypertension, TRANSEPITHELIAL TRANSPORT, LACTOBACILLUS-CASEI, MILK-PROTEINS
journal title
BRITISH JOURNAL OF NUTRITION
Br. J. Nutr.
volume
92
issue
3
pages
357-366 pages
Web of Science type
Review
Web of Science id
000224519100003
JCR category
NUTRITION & DIETETICS
JCR impact factor
2.71 (2004)
JCR rank
10/53 (2004)
JCR quartile
1 (2004)
ISSN
0007-1145
DOI
10.1079/BJN20041189
language
English
UGent publication?
yes
classification
A1
copyright statement
I have transferred the copyright for this publication to the publisher
id
300064
handle
http://hdl.handle.net/1854/LU-300064
date created
2005-03-16 14:47:00
date last changed
2016-12-19 15:45:44
@article{300064,
  abstract     = {Hypertension or high blood pressure is a significant health problem worldwide. Bioactive peptides that inhibit angiotensin I converting enzyme (ACE) in the cardiovascular system can contribute to the prevention and treatment of hypertension. These ACE inhibitory peptides are derived from many food proteins, especially milk proteins. An ACE inhibitory activity in vitro does not always imply an antihypertensive effect in vivo. Even if it does, it is very difficult to establish a direct relationship between in vitro and in vivo activity. This is mainly due to the bioavailability of the ACE inhibitory peptides after oral administration and the fact that peptides may influence blood pressure by mechanisms other than ACE inhibition. To exert an antihypertensive effect after oral ingestion, ACE inhibitory peptides have to reach the cardiovascular system in an active form. Therefore, they need to remain active during digestion by human proteases and be transported through the intestinal wall into the blood. The bioavailability of some ACE inhibitory peptides has been studied. It is also known that (hydroxy)proline-containing peptides are generally resistant to degradation by digestive enzymes. Peptides can be absorbed intact through the intestine by paracellular and transcellular routes, but the potency of the bioactivity after absorption is inversely correlated to chain length. In addition, some strategies are proposed to increase the bioavailability of ACE inhibitory peptides. Further research into the bioavailability of ACE inhibitory peptides will lead to the development of more effective ACE inhibitory peptides and foods.},
  author       = {Vermeirssen, Vanessa and Van Camp, John and Verstraete, Willy},
  issn         = {0007-1145},
  journal      = {BRITISH JOURNAL OF NUTRITION},
  keyword      = {FOOD PROTEINS,ANTIHYPERTENSIVE PEPTIDE,BLOOD-PRESSURE,BIOACTIVE PEPTIDES,HIS-ILE-ARG,HUMAN INTESTINAL-CELL,SPONTANEOUSLY HYPERTENSIVE-RATS,intestinal transport,gastrointestinal digestion,bioactive peptides,hypertension,TRANSEPITHELIAL TRANSPORT,LACTOBACILLUS-CASEI,MILK-PROTEINS},
  language     = {eng},
  number       = {3},
  pages        = {357--366},
  title        = {Bioavailability of angiotensin I converting enzyme inhibitory peptides},
  url          = {http://dx.doi.org/10.1079/BJN20041189},
  volume       = {92},
  year         = {2004},
}

Chicago
Vermeirssen, Vanessa, John Van Camp, and Willy Verstraete. 2004. “Bioavailability of Angiotensin I Converting Enzyme Inhibitory Peptides.” British Journal of Nutrition 92 (3): 357–366.
APA
Vermeirssen, Vanessa, Van Camp, J., & Verstraete, W. (2004). Bioavailability of angiotensin I converting enzyme inhibitory peptides. BRITISH JOURNAL OF NUTRITION, 92(3), 357–366.
Vancouver
1.
Vermeirssen V, Van Camp J, Verstraete W. Bioavailability of angiotensin I converting enzyme inhibitory peptides. BRITISH JOURNAL OF NUTRITION. 2004;92(3):357–66.
MLA
Vermeirssen, Vanessa, John Van Camp, and Willy Verstraete. “Bioavailability of Angiotensin I Converting Enzyme Inhibitory Peptides.” BRITISH JOURNAL OF NUTRITION 92.3 (2004): 357–366. Print.