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8‐Prenylnaringenin tissue distribution and pharmacokinetics in mice and its binding to human serum albumin and cellular uptake in human embryonic kidney cells

8‐Prenylnaringenin (8‐PN), a hop flavonoid, is a promising food substance with health benefits. Compared with nonprenylated naringenin, 8‐PN exhibits stronger estrogenic activity and prevents muscle atrophy. Moreover, 8‐PN prevents hot flushes and bone loss. Considering that prenylation reportedly i...

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Autores principales: Tanaka, Yoshiaki, Okuyama, Hitomi, Nishikawa, Miyu, Ikushiro, Shin‐ichi, Ikeda, Mayumi, Ishima, Yu, Ukawa, Yuichi, Oe, Kenichi, Terao, Junji, Mukai, Rie
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9007292/
https://www.ncbi.nlm.nih.gov/pubmed/35432956
http://dx.doi.org/10.1002/fsn3.2733
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author Tanaka, Yoshiaki
Okuyama, Hitomi
Nishikawa, Miyu
Ikushiro, Shin‐ichi
Ikeda, Mayumi
Ishima, Yu
Ukawa, Yuichi
Oe, Kenichi
Terao, Junji
Mukai, Rie
author_facet Tanaka, Yoshiaki
Okuyama, Hitomi
Nishikawa, Miyu
Ikushiro, Shin‐ichi
Ikeda, Mayumi
Ishima, Yu
Ukawa, Yuichi
Oe, Kenichi
Terao, Junji
Mukai, Rie
author_sort Tanaka, Yoshiaki
collection PubMed
description 8‐Prenylnaringenin (8‐PN), a hop flavonoid, is a promising food substance with health benefits. Compared with nonprenylated naringenin, 8‐PN exhibits stronger estrogenic activity and prevents muscle atrophy. Moreover, 8‐PN prevents hot flushes and bone loss. Considering that prenylation reportedly improves the bioavailability of flavonoids, we compared the parameters related to the bioavailability [pharmacokinetics and tissue distribution in C57/BL6 mice, binding affinity to human serum albumin (HSA), and cellular uptake in HEK293 cells] of 8‐PN and its mother (non‐prenylated) compound naringenin. C57/BL6 mice were fed an 8‐PN or naringenin mixed diet for 22 days. The amount of 8‐PN (nmol/g tissue) in the kidneys (16.8 ± 9.20), liver (14.8 ± 2.58), muscles (3.33 ± 0.60), lungs (2.07 ± 0.68), pancreas (1.80 ± 0.38), heart (1.71 ± 0.27), spleen (1.36 ± 0.29), and brain (0.31 ± 0.09) was higher than that of naringenin. A pharmacokinetic study in mice demonstrated that the C (max) of 8‐PN (50 mg/kg body weight) was lower than that of naringenin; however, the plasma concentration of 8‐PN 8 h after ingestion was higher than that of naringenin. The binding affinity of 8‐PN to HSA and cellular uptake in HEK293 cells were higher than those of naringenin. 8‐PN bioavailability features assessed in mouse or human model experiments were obviously different from those of naringenin.
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spelling pubmed-90072922022-04-15 8‐Prenylnaringenin tissue distribution and pharmacokinetics in mice and its binding to human serum albumin and cellular uptake in human embryonic kidney cells Tanaka, Yoshiaki Okuyama, Hitomi Nishikawa, Miyu Ikushiro, Shin‐ichi Ikeda, Mayumi Ishima, Yu Ukawa, Yuichi Oe, Kenichi Terao, Junji Mukai, Rie Food Sci Nutr Original Articles 8‐Prenylnaringenin (8‐PN), a hop flavonoid, is a promising food substance with health benefits. Compared with nonprenylated naringenin, 8‐PN exhibits stronger estrogenic activity and prevents muscle atrophy. Moreover, 8‐PN prevents hot flushes and bone loss. Considering that prenylation reportedly improves the bioavailability of flavonoids, we compared the parameters related to the bioavailability [pharmacokinetics and tissue distribution in C57/BL6 mice, binding affinity to human serum albumin (HSA), and cellular uptake in HEK293 cells] of 8‐PN and its mother (non‐prenylated) compound naringenin. C57/BL6 mice were fed an 8‐PN or naringenin mixed diet for 22 days. The amount of 8‐PN (nmol/g tissue) in the kidneys (16.8 ± 9.20), liver (14.8 ± 2.58), muscles (3.33 ± 0.60), lungs (2.07 ± 0.68), pancreas (1.80 ± 0.38), heart (1.71 ± 0.27), spleen (1.36 ± 0.29), and brain (0.31 ± 0.09) was higher than that of naringenin. A pharmacokinetic study in mice demonstrated that the C (max) of 8‐PN (50 mg/kg body weight) was lower than that of naringenin; however, the plasma concentration of 8‐PN 8 h after ingestion was higher than that of naringenin. The binding affinity of 8‐PN to HSA and cellular uptake in HEK293 cells were higher than those of naringenin. 8‐PN bioavailability features assessed in mouse or human model experiments were obviously different from those of naringenin. John Wiley and Sons Inc. 2022-01-22 /pmc/articles/PMC9007292/ /pubmed/35432956 http://dx.doi.org/10.1002/fsn3.2733 Text en © 2022 The Authors. Food Science & Nutrition published by Wiley Periodicals LLC. https://creativecommons.org/licenses/by/4.0/This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ (https://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 Articles
Tanaka, Yoshiaki
Okuyama, Hitomi
Nishikawa, Miyu
Ikushiro, Shin‐ichi
Ikeda, Mayumi
Ishima, Yu
Ukawa, Yuichi
Oe, Kenichi
Terao, Junji
Mukai, Rie
8‐Prenylnaringenin tissue distribution and pharmacokinetics in mice and its binding to human serum albumin and cellular uptake in human embryonic kidney cells
title 8‐Prenylnaringenin tissue distribution and pharmacokinetics in mice and its binding to human serum albumin and cellular uptake in human embryonic kidney cells
title_full 8‐Prenylnaringenin tissue distribution and pharmacokinetics in mice and its binding to human serum albumin and cellular uptake in human embryonic kidney cells
title_fullStr 8‐Prenylnaringenin tissue distribution and pharmacokinetics in mice and its binding to human serum albumin and cellular uptake in human embryonic kidney cells
title_full_unstemmed 8‐Prenylnaringenin tissue distribution and pharmacokinetics in mice and its binding to human serum albumin and cellular uptake in human embryonic kidney cells
title_short 8‐Prenylnaringenin tissue distribution and pharmacokinetics in mice and its binding to human serum albumin and cellular uptake in human embryonic kidney cells
title_sort 8‐prenylnaringenin tissue distribution and pharmacokinetics in mice and its binding to human serum albumin and cellular uptake in human embryonic kidney cells
topic Original Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9007292/
https://www.ncbi.nlm.nih.gov/pubmed/35432956
http://dx.doi.org/10.1002/fsn3.2733
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