The matricellular protein periostin contributes to proper collagen function and is downregulated during skin aging.
BACKGROUND
Periostin is a secreted 90kDa matricellular protein, which is predominantly expressed in collagen-rich tissues. Collagen is the most abundant protein in mammals and has great tensile strength. Recent investigations have shown that periostin influences collagen fibrillogenesis and biomechanical properties of murine connective tissues.


OBJECTIVE
We investigated the function of periostin concerning collagen homeostasis during intrinsic and extrinsic skin aging. For this purpose, human skin samples of young and old donors as well as samples of photoaged and sun-protected skin areas were analyzed for periostin expression. Using in vitro models, we determined the cell types responsible for periostin expression and performed functional analyses with periostin knockdown cells.


METHODS
TaqMan Real-Time PCR, UV irradiation, knockdown experiments, immunostaining, electron microscopy, collagen degradation assay, collagen crosslink analysis.


RESULTS
Periostin expression is highest in the papillary dermis and downregulated during skin aging. Fibroblasts and non-follicular skin derived precursors were identified as main source for periostin expression in human skin. Periostin knockdown in fibroblasts has no effect on collagen expression, but results in an increased fibril diameter and aberrant collagen structure. This leads to an increased susceptibility of collagen toward proteases, whereas recombinant periostin protects collagen fibrils from degradation.


CONCLUSIONS
Our data show that periostin plays an important role for proper collagen assembly and homeostasis. During skin aging periostin expression decreases and contributes to the phenotype of aged skin.
Research & Development, Beiersdorf AG, Unnastr. 48, 20245 Hamburg, Germany.
M
M
Egbert
Research & Development, Beiersdorf AG, Unnastr. 48, 20245 Hamburg, Germany; Department of Anatomy, University of Kiel, Olshausenstr. 40, 24098 Kiel, Germany.
M
M
Ruetze
Research & Development, Beiersdorf AG, Unnastr. 48, 20245 Hamburg, Germany.
M
M
Sattler
Research & Development, Beiersdorf AG, Unnastr. 48, 20245 Hamburg, Germany.
H
H
Wenck
Research & Development, Beiersdorf AG, Unnastr. 48, 20245 Hamburg, Germany.
S
S
Gallinat
Department of Anatomy, University of Kiel, Olshausenstr. 40, 24098 Kiel, Germany.
R
R
Lucius
Research & Development, Beiersdorf AG, Unnastr. 48, 20245 Hamburg, Germany. Electronic address: Julia.Weise@Beiersdorf.com.
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JM
Weise
D000328:Adult; D000367:Age Factors; D000368:Aged; D000369:Aged, 80 and over; D000375:Aging / Q000235:genetics / Q000378:metabolism*; D015815:Cell Adhesion Molecules / Q000235:genetics / Q000378:metabolism*; D002478:Cells, Cultured; D024042:Collagen Type I / Q000378:metabolism*; D015536:Down-Regulation; D005260:Female; D005347:Fibroblasts / Q000378:metabolism; D006706:Homeostasis; D006801:Humans; D008297:Male; D008875:Middle Aged; D034622:RNA Interference; D012867:Skin / Q000378:metabolism* / Q000528:radiation effects; D015595:Skin Aging; D013472:Sunlight / Q000009:adverse effects; D013997:Time Factors; D014162:Transfection; D053773:Transforming Growth Factor beta1 / Q000378:metabolism; D055815:Young Adult
D015815:Cell Adhesion Molecules; D024042:Collagen Type I; C512835:POSTN protein, human; D053773:Transforming Growth Factor beta1
AA2P; BAPN; Collagen; Ct; DHLNL; ECM; HDF; HHMD; HLNL; HP; HPLC; LOX; MMP; Matricellular protein; Periostin; SKP; SSR; Skin aging; TEM; UV; cycle threshold; dihydroxylysinonorleucine; extracellular matrix; high performance liquid chromatography; histidinohydroxymerodesmosine; human dermal fibroblasts; hydroxylysinonorleucine; hydroxylysylpyridinoline; l-ascorbic acid 2-phosphate sesquimagnesium salt hydrate; lysyloxidase; matrix metalloproteinase; qRT-PCR; quantitative real-time polymerase chain reaction; recombinant human; rh; skin derived precursor; solar simulated radiation; transmission electron microscopy; ultraviolet; β-aminopropionitrile-fumarate