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Tumor necrosis factor-α-accelerated degradation of type I collagen in human skin is associated with elevated matrix metalloproteinase (MMP)-1 and MMP-3 ex vivo.

Ågren MS, Schnabel R, Christensen LH, Mirastschijski U - Eur. J. Cell Biol. (2014)

Bottom Line: Levels of the collagenases MMP-8 and MMP-13 were insignificant and neither MMP-2 nor MMP-14 were associated with increased collagen degradation.Type I collagen formation was down-regulated in cultured compared with native skin explants but was not reduced further by TNF-α.TNF-α had no significant effect on epidermal apoptosis.

View Article: PubMed Central - PubMed

Affiliation: Copenhagen Wound Healing Center, Bispebjerg Hospital, University of Copenhagen, Copenhagen, Denmark; Digestive Disease Center, Bispebjerg Hospital, University of Copenhagen, Copenhagen, Denmark; Department of Clinical Medicine, Faculty of Health and Medical Sciences, University of Copenhagen, Copenhagen, Denmark. Electronic address: saag0005@regionh.dk.

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MMP and TIMP contents of native skin and cultured skin explants treated without (control) or with TNF-α (10 ng/ml) were measured in pooled tissue extracts by the Quantibody® array and expressed in total amount (ng) per explant. Each pool comprised extracts made from 30 individual 8-mm skin explants (5 explants from each of the 6 donors per group). (For interpretation of the references to color in this figure legend, the reader is referred to the web version of this article.)
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fig0035: MMP and TIMP contents of native skin and cultured skin explants treated without (control) or with TNF-α (10 ng/ml) were measured in pooled tissue extracts by the Quantibody® array and expressed in total amount (ng) per explant. Each pool comprised extracts made from 30 individual 8-mm skin explants (5 explants from each of the 6 donors per group). (For interpretation of the references to color in this figure legend, the reader is referred to the web version of this article.)

Mentions: Collectively, MMPs were responsible for the degradation of endogenous and exogenous type I skin collagen. Our initial approach for identifying the operative MMPs was to analyze pooled tissue extracts using a quantitative MMP/TIMP multiarray (Fig. 6). Clearly, MMP-1 was the dominant MMP in cultured skin explants. MMP-3 was barely detectable in quiescent skin but increased after 8 days of culture. MMP-2 content of native skin was ∼30 ng and increased further in culture. The amount of MMP-8 in native skin was ∼0.1 ng but was reduced after culture. The MMP-9 content was likewise lowered after incubation. Although MMP-10 was detectable in native and incubated skin the levels were insignificant (<0.05 ng/explant). Tissue MMP-13 was nondetectable. The TIMP-1 content of the explants increased after culture whereas TIMP-2 decreased. TIMP-4 was nondetectable in the tissue. From this screening we conclude that MMP-1, MMP-3, MMP-2 and TIMP-1 were the most prominent MMPs/TIMPs in our system and were analyzed on individual samples.


Tumor necrosis factor-α-accelerated degradation of type I collagen in human skin is associated with elevated matrix metalloproteinase (MMP)-1 and MMP-3 ex vivo.

Ågren MS, Schnabel R, Christensen LH, Mirastschijski U - Eur. J. Cell Biol. (2014)

MMP and TIMP contents of native skin and cultured skin explants treated without (control) or with TNF-α (10 ng/ml) were measured in pooled tissue extracts by the Quantibody® array and expressed in total amount (ng) per explant. Each pool comprised extracts made from 30 individual 8-mm skin explants (5 explants from each of the 6 donors per group). (For interpretation of the references to color in this figure legend, the reader is referred to the web version of this article.)
© Copyright Policy - CC BY-NC-ND
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4300401&req=5

fig0035: MMP and TIMP contents of native skin and cultured skin explants treated without (control) or with TNF-α (10 ng/ml) were measured in pooled tissue extracts by the Quantibody® array and expressed in total amount (ng) per explant. Each pool comprised extracts made from 30 individual 8-mm skin explants (5 explants from each of the 6 donors per group). (For interpretation of the references to color in this figure legend, the reader is referred to the web version of this article.)
Mentions: Collectively, MMPs were responsible for the degradation of endogenous and exogenous type I skin collagen. Our initial approach for identifying the operative MMPs was to analyze pooled tissue extracts using a quantitative MMP/TIMP multiarray (Fig. 6). Clearly, MMP-1 was the dominant MMP in cultured skin explants. MMP-3 was barely detectable in quiescent skin but increased after 8 days of culture. MMP-2 content of native skin was ∼30 ng and increased further in culture. The amount of MMP-8 in native skin was ∼0.1 ng but was reduced after culture. The MMP-9 content was likewise lowered after incubation. Although MMP-10 was detectable in native and incubated skin the levels were insignificant (<0.05 ng/explant). Tissue MMP-13 was nondetectable. The TIMP-1 content of the explants increased after culture whereas TIMP-2 decreased. TIMP-4 was nondetectable in the tissue. From this screening we conclude that MMP-1, MMP-3, MMP-2 and TIMP-1 were the most prominent MMPs/TIMPs in our system and were analyzed on individual samples.

Bottom Line: Levels of the collagenases MMP-8 and MMP-13 were insignificant and neither MMP-2 nor MMP-14 were associated with increased collagen degradation.Type I collagen formation was down-regulated in cultured compared with native skin explants but was not reduced further by TNF-α.TNF-α had no significant effect on epidermal apoptosis.

View Article: PubMed Central - PubMed

Affiliation: Copenhagen Wound Healing Center, Bispebjerg Hospital, University of Copenhagen, Copenhagen, Denmark; Digestive Disease Center, Bispebjerg Hospital, University of Copenhagen, Copenhagen, Denmark; Department of Clinical Medicine, Faculty of Health and Medical Sciences, University of Copenhagen, Copenhagen, Denmark. Electronic address: saag0005@regionh.dk.

Show MeSH
Related in: MedlinePlus