Molecular-level insights into aging processes of skin elastin

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Molecular-level insights into aging processes of skin elastin. / Mora Huertas, Angela C; Schmelzer, Christian E H; Hoehenwarter, Wolfgang; Heyroth, Frank; Heinz, Andrea.

In: Biochimie, Vol. 128-129, 30.08.2016, p. 163-73.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Mora Huertas, AC, Schmelzer, CEH, Hoehenwarter, W, Heyroth, F & Heinz, A 2016, 'Molecular-level insights into aging processes of skin elastin', Biochimie, vol. 128-129, pp. 163-73. https://doi.org/10.1016/j.biochi.2016.08.010

APA

Mora Huertas, A. C., Schmelzer, C. E. H., Hoehenwarter, W., Heyroth, F., & Heinz, A. (2016). Molecular-level insights into aging processes of skin elastin. Biochimie, 128-129, 163-73. https://doi.org/10.1016/j.biochi.2016.08.010

Vancouver

Mora Huertas AC, Schmelzer CEH, Hoehenwarter W, Heyroth F, Heinz A. Molecular-level insights into aging processes of skin elastin. Biochimie. 2016 Aug 30;128-129:163-73. https://doi.org/10.1016/j.biochi.2016.08.010

Author

Mora Huertas, Angela C ; Schmelzer, Christian E H ; Hoehenwarter, Wolfgang ; Heyroth, Frank ; Heinz, Andrea. / Molecular-level insights into aging processes of skin elastin. In: Biochimie. 2016 ; Vol. 128-129. pp. 163-73.

Bibtex

@article{3cae81040b0341e5a2503d15b736d0ba,

title = "Molecular-level insights into aging processes of skin elastin",

abstract = "Skin aging is characterized by different features including wrinkling, atrophy of the dermis and loss of elasticity associated with damage to the extracellular matrix protein elastin. The aim of this study was to investigate the aging process of skin elastin at the molecular level by evaluating the influence of intrinsic (chronological aging) and extrinsic factors (sun exposure) on the morphology and susceptibility of elastin towards enzymatic degradation. Elastin was isolated from biopsies derived from sun-protected or sun-exposed skin of differently aged individuals. The morphology of the elastin fibers was characterized by scanning electron microscopy. Mass spectrometric analysis and label-free quantification allowed identifying differences in the cleavage patterns of the elastin samples after enzymatic digestion. Principal component analysis and hierarchical cluster analysis were used to visualize differences between the samples and to determine the contribution of extrinsic and intrinsic aging to the proteolytic susceptibility of elastin. Moreover, the release of potentially bioactive peptides was studied. Skin aging is associated with the decomposition of elastin fibers, which is more pronounced in sun-exposed tissue. Marker peptides were identified, which showed an age-related increase or decrease in their abundances and provide insights into the progression of the aging process of elastin fibers. Strong age-related cleavage occurs in hydrophobic tropoelastin domains 18, 20, 24 and 26. Photoaging makes the N-terminal and central parts of the tropoelastin molecules more susceptible towards enzymatic cleavage and, hence, accelerates the age-related degradation of elastin.",

keywords = "Adolescent, Adult, Aged, Aged, 80 and over, Aging, Amino Acid Sequence, Child, Elastin, Female, Foreskin, Humans, Male, Microscopy, Electron, Scanning, Middle Aged, Pancreatic Elastase, Peptides, Principal Component Analysis, Skin, Skin Aging, Sunlight, Tropoelastin, Young Adult, Journal Article",

author = "{Mora Huertas}, {Angela C} and Schmelzer, {Christian E H} and Wolfgang Hoehenwarter and Frank Heyroth and Andrea Heinz",

year = "2016",

month = aug,

day = "30",

doi = "10.1016/j.biochi.2016.08.010",

language = "English",

volume = "128-129",

pages = "163--73",

journal = "Biochimie",

issn = "0300-9084",

publisher = "Elsevier Masson",

}

RIS

TY - JOUR

T1 - Molecular-level insights into aging processes of skin elastin

AU - Mora Huertas, Angela C

AU - Schmelzer, Christian E H

AU - Hoehenwarter, Wolfgang

AU - Heyroth, Frank

AU - Heinz, Andrea

PY - 2016/8/30

Y1 - 2016/8/30

N2 - Skin aging is characterized by different features including wrinkling, atrophy of the dermis and loss of elasticity associated with damage to the extracellular matrix protein elastin. The aim of this study was to investigate the aging process of skin elastin at the molecular level by evaluating the influence of intrinsic (chronological aging) and extrinsic factors (sun exposure) on the morphology and susceptibility of elastin towards enzymatic degradation. Elastin was isolated from biopsies derived from sun-protected or sun-exposed skin of differently aged individuals. The morphology of the elastin fibers was characterized by scanning electron microscopy. Mass spectrometric analysis and label-free quantification allowed identifying differences in the cleavage patterns of the elastin samples after enzymatic digestion. Principal component analysis and hierarchical cluster analysis were used to visualize differences between the samples and to determine the contribution of extrinsic and intrinsic aging to the proteolytic susceptibility of elastin. Moreover, the release of potentially bioactive peptides was studied. Skin aging is associated with the decomposition of elastin fibers, which is more pronounced in sun-exposed tissue. Marker peptides were identified, which showed an age-related increase or decrease in their abundances and provide insights into the progression of the aging process of elastin fibers. Strong age-related cleavage occurs in hydrophobic tropoelastin domains 18, 20, 24 and 26. Photoaging makes the N-terminal and central parts of the tropoelastin molecules more susceptible towards enzymatic cleavage and, hence, accelerates the age-related degradation of elastin.

AB - Skin aging is characterized by different features including wrinkling, atrophy of the dermis and loss of elasticity associated with damage to the extracellular matrix protein elastin. The aim of this study was to investigate the aging process of skin elastin at the molecular level by evaluating the influence of intrinsic (chronological aging) and extrinsic factors (sun exposure) on the morphology and susceptibility of elastin towards enzymatic degradation. Elastin was isolated from biopsies derived from sun-protected or sun-exposed skin of differently aged individuals. The morphology of the elastin fibers was characterized by scanning electron microscopy. Mass spectrometric analysis and label-free quantification allowed identifying differences in the cleavage patterns of the elastin samples after enzymatic digestion. Principal component analysis and hierarchical cluster analysis were used to visualize differences between the samples and to determine the contribution of extrinsic and intrinsic aging to the proteolytic susceptibility of elastin. Moreover, the release of potentially bioactive peptides was studied. Skin aging is associated with the decomposition of elastin fibers, which is more pronounced in sun-exposed tissue. Marker peptides were identified, which showed an age-related increase or decrease in their abundances and provide insights into the progression of the aging process of elastin fibers. Strong age-related cleavage occurs in hydrophobic tropoelastin domains 18, 20, 24 and 26. Photoaging makes the N-terminal and central parts of the tropoelastin molecules more susceptible towards enzymatic cleavage and, hence, accelerates the age-related degradation of elastin.

KW - Adolescent

KW - Adult

KW - Aged

KW - Aged, 80 and over

KW - Aging

KW - Amino Acid Sequence

KW - Child

KW - Elastin

KW - Female

KW - Foreskin

KW - Humans

KW - Male

KW - Microscopy, Electron, Scanning

KW - Middle Aged

KW - Pancreatic Elastase

KW - Peptides

KW - Principal Component Analysis

KW - Skin

KW - Skin Aging

KW - Sunlight

KW - Tropoelastin

KW - Young Adult

KW - Journal Article

U2 - 10.1016/j.biochi.2016.08.010

DO - 10.1016/j.biochi.2016.08.010

M3 - Journal article

C2 - 27569260

VL - 128-129

SP - 163

EP - 173

JO - Biochimie

JF - Biochimie

SN - 0300-9084

ER -

ID: 186421638