Chicken Muscle-Derived ACE2 Upregulating Peptide VVHPKESF Inhibits Angiotensin II-Stimulated Inflammation in Vascular Smooth Muscle Cells via the ACE2/Ang (1-7)/MasR Axis

Hongbing Fan; Wang Liao; Sandra T. Davidge; Jianping Wu

doi:10.1021/acs.jafc.1c07161

Chicken Muscle-Derived ACE2 Upregulating Peptide VVHPKESF Inhibits Angiotensin II-Stimulated Inflammation in Vascular Smooth Muscle Cells via the ACE2/Ang (1-7)/MasR Axis

Hongbing Fan, Wang Liao, Sandra T. Davidge, Jianping Wu

Research output: Contribution to journal › Article › peer-review

5 Scopus citations

Abstract

This study aimed to evaluate the modulatory effects of four chicken muscle-derived peptides [VRP, LKY, VRY, and VVHPKESF (V-F)] on angiotensin II (Ang II)-induced inflammation in rat vascular smooth muscle A7r5 cells. Only V-F could significantly attenuate Ang II-stimulated inflammation via the inhibition of NF-κB and p38 MAPK signaling, being dependent on the Mas receptor (MasR) not on the Ang II type 1 or type 2 receptor (AT₁R or AT₂R). V-F accelerated Ang II degradation by enhancing cellular ACE2 activity, which was due to ACE2 upregulation other than a direct ACE2 activation. These findings demonstrated that V-F ameliorated Ang II-induced inflammation in A7r5 cells via the ACE2/Ang (1-7)/MasR axis. Three peptide metabolites of V-F─VHPKESF, PKESF, and SF─were identified but were not considered major contributors to V-F's bioactivity. The regulation of peptide V-F on vascular inflammation supported its functional food or nutraceutical application in the prevention and treatment of hypertension and cardiovascular diseases.

Original language	English
Pages (from-to)	6397-6406
Number of pages	10
Journal	Journal of Agricultural and Food Chemistry
Volume	70
Issue number	21
DOIs	https://doi.org/10.1021/acs.jafc.1c07161
State	Published - Jun 1 2022

Bibliographical note

Funding Information:
This work was supported by the Natural Sciences and Engineering Research Council of Canada and Egg Farmers of Canada. The authors would also like to acknowledge the financial support received from Alberta Innovates─Technology Futures, Killam Trusts, and the American Oil Chemists’ Society (AOCS) Thomas H. Smouse Memorial Fellowship.

Publisher Copyright:
© 2022 American Chemical Society. All rights reserved.

Keywords

ACE
ACE2
bioactive peptides
chicken
inflammation
metabolism
signaling pathways
vascular smooth muscle cells

ASJC Scopus subject areas

Chemistry (all)
Agricultural and Biological Sciences (all)

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1021/acs.jafc.1c07161

Cite this

@article{6cd42d1d2d2544eda47f9a43d78a1bfd,

title = "Chicken Muscle-Derived ACE2 Upregulating Peptide VVHPKESF Inhibits Angiotensin II-Stimulated Inflammation in Vascular Smooth Muscle Cells via the ACE2/Ang (1-7)/MasR Axis",

abstract = "This study aimed to evaluate the modulatory effects of four chicken muscle-derived peptides [VRP, LKY, VRY, and VVHPKESF (V-F)] on angiotensin II (Ang II)-induced inflammation in rat vascular smooth muscle A7r5 cells. Only V-F could significantly attenuate Ang II-stimulated inflammation via the inhibition of NF-κB and p38 MAPK signaling, being dependent on the Mas receptor (MasR) not on the Ang II type 1 or type 2 receptor (AT1R or AT2R). V-F accelerated Ang II degradation by enhancing cellular ACE2 activity, which was due to ACE2 upregulation other than a direct ACE2 activation. These findings demonstrated that V-F ameliorated Ang II-induced inflammation in A7r5 cells via the ACE2/Ang (1-7)/MasR axis. Three peptide metabolites of V-F─VHPKESF, PKESF, and SF─were identified but were not considered major contributors to V-F's bioactivity. The regulation of peptide V-F on vascular inflammation supported its functional food or nutraceutical application in the prevention and treatment of hypertension and cardiovascular diseases.",

keywords = "ACE, ACE2, bioactive peptides, chicken, inflammation, metabolism, signaling pathways, vascular smooth muscle cells",

author = "Hongbing Fan and Wang Liao and Davidge, {Sandra T.} and Jianping Wu",

note = "Funding Information: This work was supported by the Natural Sciences and Engineering Research Council of Canada and Egg Farmers of Canada. The authors would also like to acknowledge the financial support received from Alberta Innovates─Technology Futures, Killam Trusts, and the American Oil Chemists{\textquoteright} Society (AOCS) Thomas H. Smouse Memorial Fellowship. Publisher Copyright: {\textcopyright} 2022 American Chemical Society. All rights reserved.",

year = "2022",

month = jun,

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doi = "10.1021/acs.jafc.1c07161",

language = "English",

volume = "70",

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Chicken Muscle-Derived ACE2 Upregulating Peptide VVHPKESF Inhibits Angiotensin II-Stimulated Inflammation in Vascular Smooth Muscle Cells via the ACE2/Ang (1-7)/MasR Axis. / Fan, Hongbing; Liao, Wang; Davidge, Sandra T. et al.
In: Journal of Agricultural and Food Chemistry, Vol. 70, No. 21, 01.06.2022, p. 6397-6406.

Research output: Contribution to journal › Article › peer-review

TY - JOUR

T1 - Chicken Muscle-Derived ACE2 Upregulating Peptide VVHPKESF Inhibits Angiotensin II-Stimulated Inflammation in Vascular Smooth Muscle Cells via the ACE2/Ang (1-7)/MasR Axis

AU - Fan, Hongbing

AU - Liao, Wang

AU - Davidge, Sandra T.

AU - Wu, Jianping

N1 - Funding Information: This work was supported by the Natural Sciences and Engineering Research Council of Canada and Egg Farmers of Canada. The authors would also like to acknowledge the financial support received from Alberta Innovates─Technology Futures, Killam Trusts, and the American Oil Chemists’ Society (AOCS) Thomas H. Smouse Memorial Fellowship. Publisher Copyright: © 2022 American Chemical Society. All rights reserved.

PY - 2022/6/1

Y1 - 2022/6/1

N2 - This study aimed to evaluate the modulatory effects of four chicken muscle-derived peptides [VRP, LKY, VRY, and VVHPKESF (V-F)] on angiotensin II (Ang II)-induced inflammation in rat vascular smooth muscle A7r5 cells. Only V-F could significantly attenuate Ang II-stimulated inflammation via the inhibition of NF-κB and p38 MAPK signaling, being dependent on the Mas receptor (MasR) not on the Ang II type 1 or type 2 receptor (AT1R or AT2R). V-F accelerated Ang II degradation by enhancing cellular ACE2 activity, which was due to ACE2 upregulation other than a direct ACE2 activation. These findings demonstrated that V-F ameliorated Ang II-induced inflammation in A7r5 cells via the ACE2/Ang (1-7)/MasR axis. Three peptide metabolites of V-F─VHPKESF, PKESF, and SF─were identified but were not considered major contributors to V-F's bioactivity. The regulation of peptide V-F on vascular inflammation supported its functional food or nutraceutical application in the prevention and treatment of hypertension and cardiovascular diseases.

AB - This study aimed to evaluate the modulatory effects of four chicken muscle-derived peptides [VRP, LKY, VRY, and VVHPKESF (V-F)] on angiotensin II (Ang II)-induced inflammation in rat vascular smooth muscle A7r5 cells. Only V-F could significantly attenuate Ang II-stimulated inflammation via the inhibition of NF-κB and p38 MAPK signaling, being dependent on the Mas receptor (MasR) not on the Ang II type 1 or type 2 receptor (AT1R or AT2R). V-F accelerated Ang II degradation by enhancing cellular ACE2 activity, which was due to ACE2 upregulation other than a direct ACE2 activation. These findings demonstrated that V-F ameliorated Ang II-induced inflammation in A7r5 cells via the ACE2/Ang (1-7)/MasR axis. Three peptide metabolites of V-F─VHPKESF, PKESF, and SF─were identified but were not considered major contributors to V-F's bioactivity. The regulation of peptide V-F on vascular inflammation supported its functional food or nutraceutical application in the prevention and treatment of hypertension and cardiovascular diseases.

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ER -

Chicken Muscle-Derived ACE2 Upregulating Peptide VVHPKESF Inhibits Angiotensin II-Stimulated Inflammation in Vascular Smooth Muscle Cells via the ACE2/Ang (1-7)/MasR Axis

Abstract

Bibliographical note

Keywords

ASJC Scopus subject areas

UN SDGs

Access to Document

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