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

Yuri Doki, Yosuke Nakazawa, Naoki Morishita, Shin Endo, Noriaki Nagai, Naoki Yamamoto, Hiroomi Tamura, Megumi Funakoshi-Tago

Research output: Contribution to journalArticlepeer-review

6 Citations (Scopus)

Abstract

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.

Original languageEnglish
Article number103
JournalMolecular Medicine Reports
Volume27
Issue number5
DOIs
Publication statusPublished - 2023 May

Keywords

  • Lens protein
  • advanced glycation end product
  • hesperetin
  • natural flavonoid
  • presbyopia

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Medicine
  • Molecular Biology
  • Genetics
  • Oncology
  • Cancer Research

Fingerprint

Dive into the research topics of 'Hesperetin treatment attenuates glycation of lens proteins and advanced-glycation end products generation'. Together they form a unique fingerprint.

Cite this