Age-related changes in dermal collagen physical properties in human skin

Collagen is the major structural protein in the skin. Fragmentation and disorganization of the collagen fibrils are the hallmarks of the aged human skin dermis. These age-related alterations of collagen fibrils impair skin structural integrity and make the tissue microenvironment more prone to skin...

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Published in:PloS one 2023-12, Vol.18 (12), p.e0292791-e0292791
Main Authors: He, Tianyuan, Fisher, Gary J, Kim, Ava J, Quan, Taihao
Format: Article
Language:English
Subjects:
Advanced glycosylation end products
Age
Aging
Atomic force microscopy
Biopsy
Care and treatment
Collagen
Collagen - metabolism
Dermis
Dermis - metabolism
Epidermis - metabolism
Extracellular Matrix - metabolism
Fibrils
Hardness
Health aspects
Humans
Interstitial collagenase
Matrix metalloproteinase
Matrix metalloproteinases
Mechanical properties
Medical research
Medicine, Experimental
Metalloproteinase
Microenvironments
Microscopy
Nanoindentation
Peptides
Physical properties
Physiological aspects
Skin
Skin - metabolism
Skin diseases
Structural integrity
Surface roughness
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Fisher, Gary J
Kim, Ava J
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description Collagen is the major structural protein in the skin. Fragmentation and disorganization of the collagen fibrils are the hallmarks of the aged human skin dermis. These age-related alterations of collagen fibrils impair skin structural integrity and make the tissue microenvironment more prone to skin disorders. As the biological function of collagen lies predominantly in its physical properties, we applied atomic force microscopy (AFM) and nanoindentation to evaluate the physical properties (surface roughness, stiffness, and hardness) of dermal collagen in young (25±5 years, N = 6) and aged (75±6 years, N = 6) healthy sun-protected hip skin. We observed that in the aged dermis, the surface of collagen fibrils was rougher, and fiber bundles were stiffer and harder, compared to young dermal collagen. Mechanistically, the age-related elevation of matrix metalloproteinase-1 (MMP-1) and advanced glycation end products (AGEs) are responsible for rougher and stiffer/harder dermal collagen, respectively. Analyzing the physical properties of dermal collagen as a function of age revealed that alterations of the physical properties of collagen fibrils changed with age (22-89 years, N = 18). We also observed that the reticular dermis is rougher and mechanically stiffer and harder compared to the papillary dermis in human skin. These data extend the current understanding of collagen beyond biological entities to include biophysical properties.
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subjects Advanced glycosylation end products
Age
Aging
Atomic force microscopy
Biopsy
Care and treatment
Collagen
Collagen - metabolism
Dermis
Dermis - metabolism
Epidermis - metabolism
Extracellular Matrix - metabolism
Fibrils
Hardness
Health aspects
Humans
Interstitial collagenase
Matrix metalloproteinase
Matrix metalloproteinases
Mechanical properties
Medical research
Medicine, Experimental
Metalloproteinase
Microenvironments
Microscopy
Nanoindentation
Peptides
Physical properties
Physiological aspects
Skin
Skin - metabolism
Skin diseases
Structural integrity
Surface roughness
title Age-related changes in dermal collagen physical properties in human skin
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