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Blood Pressure-Lowering Peptides from Neo-Fermented Buckwheat Sprouts: A New Approach to Estimating ACE-Inhibitory Activity
Neo-fermented buckwheat sprouts (neo-FBS) contain angiotensin-converting enzyme (ACE) inhibitors and vasodilators with blood pressure-lowering (BPL) properties in spontaneously hypertensive rats (SHRs). In this study, we investigated antihypertensive mechanisms of six BPL peptides isolated from neo-...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2014
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4164440/ https://www.ncbi.nlm.nih.gov/pubmed/25222748 http://dx.doi.org/10.1371/journal.pone.0105802 |
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author | Koyama, Masahiro Hattori, Seiji Amano, Yoshihiko Watanabe, Masanori Nakamura, Kozo |
author_facet | Koyama, Masahiro Hattori, Seiji Amano, Yoshihiko Watanabe, Masanori Nakamura, Kozo |
author_sort | Koyama, Masahiro |
collection | PubMed |
description | Neo-fermented buckwheat sprouts (neo-FBS) contain angiotensin-converting enzyme (ACE) inhibitors and vasodilators with blood pressure-lowering (BPL) properties in spontaneously hypertensive rats (SHRs). In this study, we investigated antihypertensive mechanisms of six BPL peptides isolated from neo-FBS (FBPs) by a vasorelaxation assay and conventional in vitro, in vivo, and a new ex vivo ACE inhibitory assays. Some FBPs demonstrated moderate endothelium-dependent vasorelaxation in SHR thoracic aorta and all FBPs mildly inhibited ACE in vitro. Orally administered FBPs strongly inhibited ACE in SHR tissues. To investigate detailed ACE-inhibitory mechanism of FBPs in living body tissues, we performed the ex vivo assay by using endothelium-denuded thoracic aorta rings isolated from SHRs, which demonstrated that FBPs at low concentration effectively inhibited ACE in thoracic aorta tissue and suppressed angiotensin II-mediated vasoconstriction directly associated with BPL. These results indicate that the main BPL mechanism of FBP was ACE inhibition in living body tissues, suggesting that high FBP's bioavailability including absorption, tissue affinity, and tissue accumulation was responsible for the superior ACE inhibition in vivo. We propose that our ex vivo assay is an efficient and reliable method for evaluating ACE-inhibitory mechanism responsible for BPL activity in vivo. |
format | Online Article Text |
id | pubmed-4164440 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-41644402014-09-19 Blood Pressure-Lowering Peptides from Neo-Fermented Buckwheat Sprouts: A New Approach to Estimating ACE-Inhibitory Activity Koyama, Masahiro Hattori, Seiji Amano, Yoshihiko Watanabe, Masanori Nakamura, Kozo PLoS One Research Article Neo-fermented buckwheat sprouts (neo-FBS) contain angiotensin-converting enzyme (ACE) inhibitors and vasodilators with blood pressure-lowering (BPL) properties in spontaneously hypertensive rats (SHRs). In this study, we investigated antihypertensive mechanisms of six BPL peptides isolated from neo-FBS (FBPs) by a vasorelaxation assay and conventional in vitro, in vivo, and a new ex vivo ACE inhibitory assays. Some FBPs demonstrated moderate endothelium-dependent vasorelaxation in SHR thoracic aorta and all FBPs mildly inhibited ACE in vitro. Orally administered FBPs strongly inhibited ACE in SHR tissues. To investigate detailed ACE-inhibitory mechanism of FBPs in living body tissues, we performed the ex vivo assay by using endothelium-denuded thoracic aorta rings isolated from SHRs, which demonstrated that FBPs at low concentration effectively inhibited ACE in thoracic aorta tissue and suppressed angiotensin II-mediated vasoconstriction directly associated with BPL. These results indicate that the main BPL mechanism of FBP was ACE inhibition in living body tissues, suggesting that high FBP's bioavailability including absorption, tissue affinity, and tissue accumulation was responsible for the superior ACE inhibition in vivo. We propose that our ex vivo assay is an efficient and reliable method for evaluating ACE-inhibitory mechanism responsible for BPL activity in vivo. Public Library of Science 2014-09-15 /pmc/articles/PMC4164440/ /pubmed/25222748 http://dx.doi.org/10.1371/journal.pone.0105802 Text en © 2014 Koyama et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited. |
spellingShingle | Research Article Koyama, Masahiro Hattori, Seiji Amano, Yoshihiko Watanabe, Masanori Nakamura, Kozo Blood Pressure-Lowering Peptides from Neo-Fermented Buckwheat Sprouts: A New Approach to Estimating ACE-Inhibitory Activity |
title | Blood Pressure-Lowering Peptides from Neo-Fermented Buckwheat Sprouts: A New Approach to Estimating ACE-Inhibitory Activity |
title_full | Blood Pressure-Lowering Peptides from Neo-Fermented Buckwheat Sprouts: A New Approach to Estimating ACE-Inhibitory Activity |
title_fullStr | Blood Pressure-Lowering Peptides from Neo-Fermented Buckwheat Sprouts: A New Approach to Estimating ACE-Inhibitory Activity |
title_full_unstemmed | Blood Pressure-Lowering Peptides from Neo-Fermented Buckwheat Sprouts: A New Approach to Estimating ACE-Inhibitory Activity |
title_short | Blood Pressure-Lowering Peptides from Neo-Fermented Buckwheat Sprouts: A New Approach to Estimating ACE-Inhibitory Activity |
title_sort | blood pressure-lowering peptides from neo-fermented buckwheat sprouts: a new approach to estimating ace-inhibitory activity |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4164440/ https://www.ncbi.nlm.nih.gov/pubmed/25222748 http://dx.doi.org/10.1371/journal.pone.0105802 |
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