Age-related NADH oxidase (arNOX)-catalyzed oxidative damage to skin proteins

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 spectr...

Full description

Saved in:
Bibliographic Details
Published in:Archives of Dermatological Research 2014-09, Vol.306 (7), p.645-652
Main Authors: Meadows, Christiaan, Morré, D. James, Morré, Dorothy M., Draelos, Zoe D., Kern, Dale
Format: Article
Language:English
Subjects:
Adult
Age Factors
Aging
Biopsy, Needle
Collagen - metabolism
Cytochromes c - chemistry
Dermatology
Elastin - metabolism
Female
Glycation End Products, Advanced - metabolism
Humans
Male
Medicine
Medicine & Public Health
Melanins
Middle Aged
NADH, NADPH Oxidoreductases - metabolism
Original Paper
Oxidation-Reduction
Oxidative Stress
Protein Structure, Tertiary
Saliva - enzymology
Serum - enzymology
Skin - enzymology
Skin - pathology
Superoxides - metabolism
Tissue Preservation
Young Adult
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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.
ISSN:0340-3696
1432-069X
DOI:10.1007/s00403-014-1472-8