Cited by 61Skin Protection and AgingAdvanced Glycation End Products researchDermatological and Skeletal Disorders

Nε-(Carboxymethyl)lysine Modification of Elastin Alters Its Biological Properties: Implications for the Accumulation of Abnormal Elastic Fibers in Actinic Elastosis

Open access
Yoshinaga, Eiji, Kawada, Akira, Ono, Koji, Fujimoto, Eita, Wachi, Hiroshi, Harumiya, Satoru, Nagai, Ryoji, Tajima, Shingo·2012·Journal of Investigative Dermatology

Abstract

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.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1038/jid.2011.298

Cites

46 of 46 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

  • 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]

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Cites

Flagged first, then by citations

Cited by

Sorted by citations

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
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

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review