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

  • Authors:
    • Yuri Doki
    • Yosuke Nakazawa
    • Naoki Morishita
    • Shin Endo
    • Noriaki Nagai
    • Naoki Yamamoto
    • Hiroomi Tamura
    • Megumi Funakoshi‑Tago
  • View Affiliations / Copyright

    Affiliations: Department of Hygienic Chemistry, Faculty of Pharmacy, Keio University, Tokyo 105-8512, Japan, R&D Division, Hayashibara Co., Ltd., Okayama 702-8006, Japan, Department of Advanced Design for Pharmaceuticals, Faculty of Pharmacy, Kindai University, Osaka 577-8502, Japan, Regenerative Medicine Support Promotion Facility, Center for Research Promotion and Support, Fujita Health University, Toyoake, Aichi 470-1192, Japan
    Copyright: © Doki et al. This is an open access article distributed under the terms of Creative Commons Attribution License.
  • Article Number: 103
    |
    Published online on: March 30, 2023
       https://doi.org/10.3892/mmr.2023.12990
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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.
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Copy and paste a formatted citation
Spandidos Publications style
Doki Y, Nakazawa Y, Morishita N, Endo S, Nagai N, Yamamoto N, Tamura H and Funakoshi‑Tago M: Hesperetin treatment attenuates glycation of lens proteins and advanced‑glycation end products generation. Mol Med Rep 27: 103, 2023.
APA
Doki, Y., Nakazawa, Y., Morishita, N., Endo, S., Nagai, N., Yamamoto, N. ... Funakoshi‑Tago, M. (2023). Hesperetin treatment attenuates glycation of lens proteins and advanced‑glycation end products generation. Molecular Medicine Reports, 27, 103. https://doi.org/10.3892/mmr.2023.12990
MLA
Doki, Y., Nakazawa, Y., Morishita, N., Endo, S., Nagai, N., Yamamoto, N., Tamura, H., Funakoshi‑Tago, M."Hesperetin treatment attenuates glycation of lens proteins and advanced‑glycation end products generation". Molecular Medicine Reports 27.5 (2023): 103.
Chicago
Doki, Y., Nakazawa, Y., Morishita, N., Endo, S., Nagai, N., Yamamoto, N., Tamura, H., Funakoshi‑Tago, M."Hesperetin treatment attenuates glycation of lens proteins and advanced‑glycation end products generation". Molecular Medicine Reports 27, no. 5 (2023): 103. https://doi.org/10.3892/mmr.2023.12990
Copy and paste a formatted citation
x
Spandidos Publications style
Doki Y, Nakazawa Y, Morishita N, Endo S, Nagai N, Yamamoto N, Tamura H and Funakoshi‑Tago M: Hesperetin treatment attenuates glycation of lens proteins and advanced‑glycation end products generation. Mol Med Rep 27: 103, 2023.
APA
Doki, Y., Nakazawa, Y., Morishita, N., Endo, S., Nagai, N., Yamamoto, N. ... Funakoshi‑Tago, M. (2023). Hesperetin treatment attenuates glycation of lens proteins and advanced‑glycation end products generation. Molecular Medicine Reports, 27, 103. https://doi.org/10.3892/mmr.2023.12990
MLA
Doki, Y., Nakazawa, Y., Morishita, N., Endo, S., Nagai, N., Yamamoto, N., Tamura, H., Funakoshi‑Tago, M."Hesperetin treatment attenuates glycation of lens proteins and advanced‑glycation end products generation". Molecular Medicine Reports 27.5 (2023): 103.
Chicago
Doki, Y., Nakazawa, Y., Morishita, N., Endo, S., Nagai, N., Yamamoto, N., Tamura, H., Funakoshi‑Tago, M."Hesperetin treatment attenuates glycation of lens proteins and advanced‑glycation end products generation". Molecular Medicine Reports 27, no. 5 (2023): 103. https://doi.org/10.3892/mmr.2023.12990
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