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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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Effect of TNF-α and GM6001 on type I collagen turnover assessed by the biochemical markers of degradation ICTP (A), neosynthesis CICP (B) and type I collagen formation (C and D). (A and B) Media from five explants per donor were pooled and then analyzed. CICP levels after ultrafiltration of day-4 samples are indicated by lower bars (B). Mean ± SEM. **p < 0.01, ***p < 0.005 versus control at respective time point. (C and D) Western blot analysis for the α1 chain of type I collagen and β-actin of pooled concentrated (Amicon® Ultra; Millipore) CNTZ tissue extracts (C and D) and conditioned media (C) from 30 individual 8-mm skin explants (5 explants from each of the 6 donors). (C) Loading of tissue extracts was normalized to the β-actin content determined separately (D) and media were adjusted to the corresponding volume to biopsy weight ratio. Lane 1, native skin; 2, control; 3, GM6001 (10 μM); 4, TNF-α. (D) Equal volume (12.5 μl) of the tissue extracts was applied to each well.
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fig0015: Effect of TNF-α and GM6001 on type I collagen turnover assessed by the biochemical markers of degradation ICTP (A), neosynthesis CICP (B) and type I collagen formation (C and D). (A and B) Media from five explants per donor were pooled and then analyzed. CICP levels after ultrafiltration of day-4 samples are indicated by lower bars (B). Mean ± SEM. **p < 0.01, ***p < 0.005 versus control at respective time point. (C and D) Western blot analysis for the α1 chain of type I collagen and β-actin of pooled concentrated (Amicon® Ultra; Millipore) CNTZ tissue extracts (C and D) and conditioned media (C) from 30 individual 8-mm skin explants (5 explants from each of the 6 donors). (C) Loading of tissue extracts was normalized to the β-actin content determined separately (D) and media were adjusted to the corresponding volume to biopsy weight ratio. Lane 1, native skin; 2, control; 3, GM6001 (10 μM); 4, TNF-α. (D) Equal volume (12.5 μl) of the tissue extracts was applied to each well.

Mentions: ICTP levels correlated strongly with those of hydroxyproline in control-treated skin explants (rs = 0.82, p < 0.005, n = 12). TNF-α treatment increased (p < 0.01) the ICTP levels compared with control while ICTP levels were reduced (p < 0.005) with 10 μM GM6001 on day 8 (Fig. 2A).


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)

Effect of TNF-α and GM6001 on type I collagen turnover assessed by the biochemical markers of degradation ICTP (A), neosynthesis CICP (B) and type I collagen formation (C and D). (A and B) Media from five explants per donor were pooled and then analyzed. CICP levels after ultrafiltration of day-4 samples are indicated by lower bars (B). Mean ± SEM. **p < 0.01, ***p < 0.005 versus control at respective time point. (C and D) Western blot analysis for the α1 chain of type I collagen and β-actin of pooled concentrated (Amicon® Ultra; Millipore) CNTZ tissue extracts (C and D) and conditioned media (C) from 30 individual 8-mm skin explants (5 explants from each of the 6 donors). (C) Loading of tissue extracts was normalized to the β-actin content determined separately (D) and media were adjusted to the corresponding volume to biopsy weight ratio. Lane 1, native skin; 2, control; 3, GM6001 (10 μM); 4, TNF-α. (D) Equal volume (12.5 μl) of the tissue extracts was applied to each well.
© Copyright Policy - CC BY-NC-ND
Related In: Results  -  Collection

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Show All Figures
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fig0015: Effect of TNF-α and GM6001 on type I collagen turnover assessed by the biochemical markers of degradation ICTP (A), neosynthesis CICP (B) and type I collagen formation (C and D). (A and B) Media from five explants per donor were pooled and then analyzed. CICP levels after ultrafiltration of day-4 samples are indicated by lower bars (B). Mean ± SEM. **p < 0.01, ***p < 0.005 versus control at respective time point. (C and D) Western blot analysis for the α1 chain of type I collagen and β-actin of pooled concentrated (Amicon® Ultra; Millipore) CNTZ tissue extracts (C and D) and conditioned media (C) from 30 individual 8-mm skin explants (5 explants from each of the 6 donors). (C) Loading of tissue extracts was normalized to the β-actin content determined separately (D) and media were adjusted to the corresponding volume to biopsy weight ratio. Lane 1, native skin; 2, control; 3, GM6001 (10 μM); 4, TNF-α. (D) Equal volume (12.5 μl) of the tissue extracts was applied to each well.
Mentions: ICTP levels correlated strongly with those of hydroxyproline in control-treated skin explants (rs = 0.82, p < 0.005, n = 12). TNF-α treatment increased (p < 0.01) the ICTP levels compared with control while ICTP levels were reduced (p < 0.005) with 10 μM GM6001 on day 8 (Fig. 2A).

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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Related in: MedlinePlus