Age-related NADH oxidase (arNOX)-catalyzed oxidative damage to skin proteins
Abstract
Age-related NADH oxidase (arNOX), a cell surface-located hydroquinone oxidase capable of superoxide generation, appears at age 30 and increases with age thereafter. The ectodomain of arNOX is shed from the cell surface into body fluids including sera and saliva where its activity was measured spectrophotometrically using a reduction of ferricytochrome c as a measure of superoxide generation. The autofluorescence of advanced glycation end products correlates with epidermal arNOX activity as well. To demonstrate protein cross-linking, a fluorescence-labeled analog of tyrosine, tyramine, that would react with proteins carrying arNOX-generated tyrosyl radicals was used. The assay demonstrated the potential for arNOX-induced oxidative damage (dityrosine formation) to human collagen and elastin and to other surface proteins of intact human embryo fibroblasts and frozen sections from epidermal punch biopsies. The findings support a role for arNOX as a major source of oxidative damage leading to cross-linking of skin proteins.
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Intrinsic aging includes ROS production via normal oxidative metabolism within cells that is inevitable, but contributes modestly to skin aging compared to extrinsic aging.
“For example, in intrinsic aging, there is ROS production via normal oxidative metabolism within cells that is inevitable, but contributes in a modest way to skin aging compared to extrinsic aging [2,18,19].”
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- Authors
- Meadows, C., Morré, D. J., Morré, D. M., Draelos, Z. D., & Kern, D.
- Affiliations
- Purdue University West Lafayette (US)
- Nu Skin (United States) (US)
- Corresponding author
- Morré, D. James
- ORCID
- Draelos, Zoe D.
- Venue
- Archives of Dermatological Research
- Published
- 2014-06-07
- Volume
- 306
- Issue
- 7
- Pages
- 645-652
- ISSN
- 0003-9187 (ISSN-L)
- 0340-3696
- 1432-069X
- OpenAlex
- W2039383508
- Cited by
- 11
- References
- 29
- Citations by year
- 2020: 1 · 2019: 1 · 2018: 2 · 2017: 1 · 2016: 3 · 2015: 3
- FWCI
- 1.61
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Archives of Dermatological Research (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Purdue University
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Advanced Glycation End Products research
- Health Sciences › Medicine › Dermatology › Skin Protection and Aging
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Keywords
- oxidative damage, skin proteins, protein cross-linking, dityrosine formation, tyrosyl radical, superoxide production, advanced glycation end products, collagen, elastin, human embryo fibroblasts, aging, skin aging
- MeSH terms
- Adult, Age Factors, Aging, Biopsy, Needle, Collagen, Elastin, Female, Humans, Male, Melanins, Middle Aged, NADH, NADPH Oxidoreductases, Oxidation-Reduction, Saliva, Skin, Superoxides, Tissue Preservation, Glycation End Products, Advanced, Protein Structure, Tertiary, Oxidative Stress, Serum, Cytochromes c, Young Adult
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