Nε-(Carboxymethyl)lysine Modification of Elastin Alters Its Biological Properties: Implications for the Accumulation of Abnormal Elastic Fibers in Actinic Elastosis
Open accessAbstract
Accumulation of degenerated elastic fibers in the sun-exposed skin designated as actinic elastosis is a histological hallmark of photodamaged skin. Previous studies have indicated that the elastic fibers of actinic elastosis interact with lysozyme and are modified by N(ɛ)-(carboxymethyl)lysine (CML), one of the major advanced glycation end products (AGEs). We studied here how CML modification of elastin is involved in the pathogenesis of actinic elastosis. The CML-modified insoluble elastin became resistant to neutrophil elastase digestion, which was reversed by treatment with aminoguanidine, a potent inhibitor of AGE formation. In a temperature-dependent aggregation assay, CML-modified elastin rapidly formed self-aggregates, the size of which was larger than unmodified elastin. The elastic fiber sheets prepared from CML-modified α-elastin showed 3D wider diameter, tortuous appearance, and decreased elasticity on tensile tests. The CML-modified α-elastin, but not unmodified α-elastin, was found to bind to lysozyme in vitro, supporting the immunohistochemical findings that the antibodies for lysozyme and CML reacted simultaneously with the elastic fibers of actinic elastosis and UV-irradiated skin. The glycated elastin is likely to cause the accumulation of abnormally aggregated elastic fibers and unusual interaction with lysozyme in actinic elastosis.
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AGEs accumulate in photo-aging skin, affect protein function in the dermis, and promote skin aging.
“As the final product of nonenzymatic glycosylation reaction, AGEs accumulate in photo-aging skin, affect protein function in the dermis, and promote skin aging [48,49,50].”
From Diet and Skin Aging—From the Perspective of Food Nutrition (2020) · cites this paper as [48]
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Fighting against Skin Aging: The Way from Bench to Bedside
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- Authors
- Yoshinaga, E., Kawada, A., Ono, K., Fujimoto, E., Wachi, H., Harumiya, S., Nagai, R., & Tajima, S.
- Affiliations
- Kindai University (JP)
- National Defense Medical College Hospital (JP)
- Hoshi University (JP)
- Tokyo Medical and Dental University (JP)
- Japan Women's University (JP)
- Corresponding author
- Yoshinaga, Eiji
- Venue
- Journal of Investigative Dermatology
- Publisher
- Elsevier BV
- Published
- 2012-02
- Volume
- 132
- Issue
- 2
- Pages
- 315-323
- ISSN
- 0022-202X (ISSN-L)
- OpenAlex
- W1990380577
- Cited by
- 61
- References
- 46
- Citations by year
- 2026: 3 · 2025: 2 · 2024: 3 · 2023: 6 · 2022: 8 · 2021: 7 · 2020: 1 · 2019: 2 · 2018: 7 · 2017: 4 · 2016: 6 · 2015: 8 · 2014: 2 · 2013: 1 · 2012: 1
- FWCI
- 1.71
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Journal of Investigative Dermatology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Japan Society for the Promotion of Science (21590340)
- Topics
- Health Sciences › Medicine › Dermatology › Skin Protection and Aging
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Advanced Glycation End Products research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Dermatological and Skeletal Disorders
- Keywords
- carboxymethyllysine, advanced glycation end products, elastin, actinic elastosis, elastic fiber degeneration, lysozyme, neutrophil elastase, aminoguanidine, photodamaged skin, UV irradiation, skin elasticity
- MeSH terms
- Adult, Elastic Tissue, Elastin, Humans, Lysine, Male, Microscopy, Electron, Scanning, Muramidase, Sunlight, Ultraviolet Rays, Skin Aging, Leukocyte Elastase
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