Cargando…

Hesperetin treatment attenuates glycation of lens proteins and advanced‑glycation end products generation

Advanced glycation end products (AGEs) in lens proteins increase with aging, thus inducing cataracts and/or presbyopia. Hesperetin (Hst), which is an abundant plant flavanone largely derived from citrus species, and its derivatives attenuate cataracts and presbyopia in vivo and in vitro; however, no...

Descripción completa

Detalles Bibliográficos
Autores principales: Doki, Yuri, Nakazawa, Yosuke, Morishita, Naoki, Endo, Shin, Nagai, Noriaki, Yamamoto, Naoki, Tamura, Hiroomi, Funakoshi-Tago, Megumi
Formato: Online Artículo Texto
Lenguaje:English
Publicado: D.A. Spandidos 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10086570/
https://www.ncbi.nlm.nih.gov/pubmed/36999595
http://dx.doi.org/10.3892/mmr.2023.12990
_version_ 1785022182765625344
author Doki, Yuri
Nakazawa, Yosuke
Morishita, Naoki
Endo, Shin
Nagai, Noriaki
Yamamoto, Naoki
Tamura, Hiroomi
Funakoshi-Tago, Megumi
author_facet Doki, Yuri
Nakazawa, Yosuke
Morishita, Naoki
Endo, Shin
Nagai, Noriaki
Yamamoto, Naoki
Tamura, Hiroomi
Funakoshi-Tago, Megumi
author_sort Doki, Yuri
collection PubMed
description Advanced glycation end products (AGEs) in lens proteins increase with aging, thus inducing cataracts and/or presbyopia. Hesperetin (Hst), which is an abundant plant flavanone largely derived from citrus species, and its derivatives attenuate cataracts and presbyopia in vivo and in vitro; however, no reports have described its effects on AGE formation in lens proteins. The present study demonstrated that AGEs in lens proteins increase with age in mice. Additionally, it showed that Hst can prevent AGEs and N(ε)-carboxymethyl-lysine generation and modification of lens proteins using in vitro in human lens epithelial cell lines and ex vivo in mouse lens organ cultures. Furthermore, treatment with Hst prevented lens hardening and decreased chaperone activity in lens proteins. These results suggested that Hst and its derivatives are good candidates for the prevention of presbyopia and cataracts.
format Online
Article
Text
id pubmed-10086570
institution National Center for Biotechnology Information
language English
publishDate 2023
publisher D.A. Spandidos
record_format MEDLINE/PubMed
spelling pubmed-100865702023-04-12 Hesperetin treatment attenuates glycation of lens proteins and advanced‑glycation end products generation Doki, Yuri Nakazawa, Yosuke Morishita, Naoki Endo, Shin Nagai, Noriaki Yamamoto, Naoki Tamura, Hiroomi Funakoshi-Tago, Megumi Mol Med Rep Articles Advanced glycation end products (AGEs) in lens proteins increase with aging, thus inducing cataracts and/or presbyopia. Hesperetin (Hst), which is an abundant plant flavanone largely derived from citrus species, and its derivatives attenuate cataracts and presbyopia in vivo and in vitro; however, no reports have described its effects on AGE formation in lens proteins. The present study demonstrated that AGEs in lens proteins increase with age in mice. Additionally, it showed that Hst can prevent AGEs and N(ε)-carboxymethyl-lysine generation and modification of lens proteins using in vitro in human lens epithelial cell lines and ex vivo in mouse lens organ cultures. Furthermore, treatment with Hst prevented lens hardening and decreased chaperone activity in lens proteins. These results suggested that Hst and its derivatives are good candidates for the prevention of presbyopia and cataracts. D.A. Spandidos 2023-03-30 /pmc/articles/PMC10086570/ /pubmed/36999595 http://dx.doi.org/10.3892/mmr.2023.12990 Text en Copyright: © Doki et al. https://creativecommons.org/licenses/by-nc-nd/4.0/This is an open access article distributed under the terms of the Creative Commons Attribution-NonCommercial-NoDerivs License (https://creativecommons.org/licenses/by-nc-nd/4.0/) , which permits use and distribution in any medium, provided the original work is properly cited, the use is non-commercial and no modifications or adaptations are made.
spellingShingle Articles
Doki, Yuri
Nakazawa, Yosuke
Morishita, Naoki
Endo, Shin
Nagai, Noriaki
Yamamoto, Naoki
Tamura, Hiroomi
Funakoshi-Tago, Megumi
Hesperetin treatment attenuates glycation of lens proteins and advanced‑glycation end products generation
title Hesperetin treatment attenuates glycation of lens proteins and advanced‑glycation end products generation
title_full Hesperetin treatment attenuates glycation of lens proteins and advanced‑glycation end products generation
title_fullStr Hesperetin treatment attenuates glycation of lens proteins and advanced‑glycation end products generation
title_full_unstemmed Hesperetin treatment attenuates glycation of lens proteins and advanced‑glycation end products generation
title_short Hesperetin treatment attenuates glycation of lens proteins and advanced‑glycation end products generation
title_sort hesperetin treatment attenuates glycation of lens proteins and advanced‑glycation end products generation
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10086570/
https://www.ncbi.nlm.nih.gov/pubmed/36999595
http://dx.doi.org/10.3892/mmr.2023.12990
work_keys_str_mv AT dokiyuri hesperetintreatmentattenuatesglycationoflensproteinsandadvancedglycationendproductsgeneration
AT nakazawayosuke hesperetintreatmentattenuatesglycationoflensproteinsandadvancedglycationendproductsgeneration
AT morishitanaoki hesperetintreatmentattenuatesglycationoflensproteinsandadvancedglycationendproductsgeneration
AT endoshin hesperetintreatmentattenuatesglycationoflensproteinsandadvancedglycationendproductsgeneration
AT nagainoriaki hesperetintreatmentattenuatesglycationoflensproteinsandadvancedglycationendproductsgeneration
AT yamamotonaoki hesperetintreatmentattenuatesglycationoflensproteinsandadvancedglycationendproductsgeneration
AT tamurahiroomi hesperetintreatmentattenuatesglycationoflensproteinsandadvancedglycationendproductsgeneration
AT funakoshitagomegumi hesperetintreatmentattenuatesglycationoflensproteinsandadvancedglycationendproductsgeneration