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Angiotensin‐1‐converting enzyme inhibition, antioxidant activity, and modulation of cerebral Na+/K+ ATPase by free phenolics of African locust bean (Parkia biglobosa)

AIMS: To investigate the antioxidant activities and effects of free phenols (FPPB) and bound phenols (BPPB) of Parkia biglobosa leaves on some enzymes of neuro‐cardiovascular relevance. METHODS AND RESULTS: HPLC‐DAD fingerprinting of FPPB and BPPB, and the antihemolytic, radical (1,1‐diphenyl‐2 picr...

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Autores principales: Komolafe, Kayode, Akinmoladun, Afolabi C., Komolafe, Titilope R., Olaleye, Mary T., Boligon, Aline A., Akindahunsi, Akintunde A., Rocha, Joao B.T.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6266567/
https://www.ncbi.nlm.nih.gov/pubmed/30623035
http://dx.doi.org/10.1002/hsr2.17
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author Komolafe, Kayode
Akinmoladun, Afolabi C.
Komolafe, Titilope R.
Olaleye, Mary T.
Boligon, Aline A.
Akindahunsi, Akintunde A.
Rocha, Joao B.T.
author_facet Komolafe, Kayode
Akinmoladun, Afolabi C.
Komolafe, Titilope R.
Olaleye, Mary T.
Boligon, Aline A.
Akindahunsi, Akintunde A.
Rocha, Joao B.T.
author_sort Komolafe, Kayode
collection PubMed
description AIMS: To investigate the antioxidant activities and effects of free phenols (FPPB) and bound phenols (BPPB) of Parkia biglobosa leaves on some enzymes of neuro‐cardiovascular relevance. METHODS AND RESULTS: HPLC‐DAD fingerprinting of FPPB and BPPB, and the antihemolytic, radical (1,1‐diphenyl‐2 picrylhydrazyl, DPPH; 2,2‐azino‐bis(3‐ethylbenzthiazoline‐6‐sulphonic acid), ABTS) scavenging and ferric reducing antioxidant properties of extracts, were assessed. In addition, the effects of the phenolics on angiotensin‐1‐converting enzyme (ACE), cerebral acetylcholinesterase/butyrylcholinesterase (AChE/BuChE), and Na(+)/K(+)ATPase were determined in vitro. FPPB was more potent than BPPB in terms of ABTS (EC(50):4.06 ± 0.3 vs 24.07 ± 2.1 μg/mL) and DPPH (EC(50):3.82 ± 0.2 vs 10.22 ± 0.1 μg/mL) radicals scavenged, respectively. The free phenolic extract was a better DPPH(.) scavenger than ascorbic acid (EC(50) = 12.58 ± 0.4 μg/mL; DPPH reference) and compared well with Trolox (EC(50):4.44 ± 0.08 μg/mL; ABTS reference). The anti‐hemolytic effect of FPPB (36%) and BPPB (53%) was highest at 15 μg/mL but lower than that recorded for ascorbic acid (67% at 10 μg/mL). Even though FPPB (IC(50) = 15.35 ± 4.0 μg/mL) and BPPB (IC(50) = 46.85 ± 3.3 μg/mL) showed considerably lower ACE‐inhibitory effect than ramipril (IC(50):0.173 ± 0.04 μg/mL), both extracts demonstrated dose‐dependent, significant (p < 0.01/p < 0.05) inhibition of the enzyme. FPPB increased cerebral Na+/K+ATPase activity but neither phenolic extract affects cerebral AChE/BuChE activities. HPLC‐DAD revealed catechin, caffeic acid, and quercetin, respectively, as the major phenolics (mg/g) in FPPB (29.85, 30.29, and 17.10) and BPPB (32.70, 30.51, and 19.25). CONCLUSION: The effects of P biglobosa on ACE and cerebral ATPase are related to its constituent phenolics. ACE inhibition could be an important mechanism underlying the documented hypotensive effect of the plant.
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spelling pubmed-62665672019-01-08 Angiotensin‐1‐converting enzyme inhibition, antioxidant activity, and modulation of cerebral Na+/K+ ATPase by free phenolics of African locust bean (Parkia biglobosa) Komolafe, Kayode Akinmoladun, Afolabi C. Komolafe, Titilope R. Olaleye, Mary T. Boligon, Aline A. Akindahunsi, Akintunde A. Rocha, Joao B.T. Health Sci Rep Original Papers AIMS: To investigate the antioxidant activities and effects of free phenols (FPPB) and bound phenols (BPPB) of Parkia biglobosa leaves on some enzymes of neuro‐cardiovascular relevance. METHODS AND RESULTS: HPLC‐DAD fingerprinting of FPPB and BPPB, and the antihemolytic, radical (1,1‐diphenyl‐2 picrylhydrazyl, DPPH; 2,2‐azino‐bis(3‐ethylbenzthiazoline‐6‐sulphonic acid), ABTS) scavenging and ferric reducing antioxidant properties of extracts, were assessed. In addition, the effects of the phenolics on angiotensin‐1‐converting enzyme (ACE), cerebral acetylcholinesterase/butyrylcholinesterase (AChE/BuChE), and Na(+)/K(+)ATPase were determined in vitro. FPPB was more potent than BPPB in terms of ABTS (EC(50):4.06 ± 0.3 vs 24.07 ± 2.1 μg/mL) and DPPH (EC(50):3.82 ± 0.2 vs 10.22 ± 0.1 μg/mL) radicals scavenged, respectively. The free phenolic extract was a better DPPH(.) scavenger than ascorbic acid (EC(50) = 12.58 ± 0.4 μg/mL; DPPH reference) and compared well with Trolox (EC(50):4.44 ± 0.08 μg/mL; ABTS reference). The anti‐hemolytic effect of FPPB (36%) and BPPB (53%) was highest at 15 μg/mL but lower than that recorded for ascorbic acid (67% at 10 μg/mL). Even though FPPB (IC(50) = 15.35 ± 4.0 μg/mL) and BPPB (IC(50) = 46.85 ± 3.3 μg/mL) showed considerably lower ACE‐inhibitory effect than ramipril (IC(50):0.173 ± 0.04 μg/mL), both extracts demonstrated dose‐dependent, significant (p < 0.01/p < 0.05) inhibition of the enzyme. FPPB increased cerebral Na+/K+ATPase activity but neither phenolic extract affects cerebral AChE/BuChE activities. HPLC‐DAD revealed catechin, caffeic acid, and quercetin, respectively, as the major phenolics (mg/g) in FPPB (29.85, 30.29, and 17.10) and BPPB (32.70, 30.51, and 19.25). CONCLUSION: The effects of P biglobosa on ACE and cerebral ATPase are related to its constituent phenolics. ACE inhibition could be an important mechanism underlying the documented hypotensive effect of the plant. John Wiley and Sons Inc. 2017-11-27 /pmc/articles/PMC6266567/ /pubmed/30623035 http://dx.doi.org/10.1002/hsr2.17 Text en © 2017 The Authors. Health Science Reports published by Wiley Periodicals, Inc. This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
spellingShingle Original Papers
Komolafe, Kayode
Akinmoladun, Afolabi C.
Komolafe, Titilope R.
Olaleye, Mary T.
Boligon, Aline A.
Akindahunsi, Akintunde A.
Rocha, Joao B.T.
Angiotensin‐1‐converting enzyme inhibition, antioxidant activity, and modulation of cerebral Na+/K+ ATPase by free phenolics of African locust bean (Parkia biglobosa)
title Angiotensin‐1‐converting enzyme inhibition, antioxidant activity, and modulation of cerebral Na+/K+ ATPase by free phenolics of African locust bean (Parkia biglobosa)
title_full Angiotensin‐1‐converting enzyme inhibition, antioxidant activity, and modulation of cerebral Na+/K+ ATPase by free phenolics of African locust bean (Parkia biglobosa)
title_fullStr Angiotensin‐1‐converting enzyme inhibition, antioxidant activity, and modulation of cerebral Na+/K+ ATPase by free phenolics of African locust bean (Parkia biglobosa)
title_full_unstemmed Angiotensin‐1‐converting enzyme inhibition, antioxidant activity, and modulation of cerebral Na+/K+ ATPase by free phenolics of African locust bean (Parkia biglobosa)
title_short Angiotensin‐1‐converting enzyme inhibition, antioxidant activity, and modulation of cerebral Na+/K+ ATPase by free phenolics of African locust bean (Parkia biglobosa)
title_sort angiotensin‐1‐converting enzyme inhibition, antioxidant activity, and modulation of cerebral na+/k+ atpase by free phenolics of african locust bean (parkia biglobosa)
topic Original Papers
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6266567/
https://www.ncbi.nlm.nih.gov/pubmed/30623035
http://dx.doi.org/10.1002/hsr2.17
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