References of "Lapière, ChM"
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See detailLe systeme vasculaire lymphatique: etats des connaissances et implications dermatologiques potentielles.
Henno, Audrey ULg; Lapiere, ChM; Nusgens, Betty ULg et al

in Annales de Dermatologie et de Vénéréologie (2008), 135(10), 704-9

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See detailSignaling through Rho GTPases in microgravity (Rho signaling) on ISS (Soyuz TMA-1) Belgian Soyuz Mission "Odissea"
Nusgens, Betty ULg; Lambert, Charles ULg; Lapière, ChM

in Microgravity Science and Technology (2007), XIX(5-6),

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See detailDecrease of Plasma Vitamin E (Alpha-Tocopherol) Levels in Patients with Abdominal Aortic Aneurysm
Sakalihasan, Natzi ULg; Pincemail, Joël ULg; Defraigne, Jean-Olivier ULg et al

in Annals of the New York Academy of Sciences (1996), 800

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See detailEvidence for a relationship between Ehlers-Danlos type VII C in humans and bovine dermatosparaxis.
Nusgens, Betty ULg; Verellen-Dumoulin, C.; Hermanns-Le, Trinh ULg et al

in Nature Genetics (1992), 1(3), 214-7

Ehlers-Danlos (ED) syndrome type VII is characterized by the accumulation of collagen precursors in connective tissues. ED VII A and B are caused by mutations in the genes of alpha 1 and alpha 2 collagen ... [more ▼]

Ehlers-Danlos (ED) syndrome type VII is characterized by the accumulation of collagen precursors in connective tissues. ED VII A and B are caused by mutations in the genes of alpha 1 and alpha 2 collagen I which result in the disruption of the cleavage site of procollagen I N-proteinase. The existence of ED VII C in humans has been hypothesized on the basis of a disorder in cattle and sheep related to the absence of the enzyme. We now present evidence for the existence of this disease in humans, characterized by skin fragility, altered polymers seen as hieroglyphic pictures with electron microscopy, accumulation of p-N-alpha 1 and p-N-alpha 2 collagen type I in the dermis and absence of processing of the p-N-I polypeptides in fibroblast cultures. [less ▲]

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See detailAltered Response of Progeria Fibroblasts to Epidermal Growth Factor
Colige, Alain ULg; Nusgens, Betty ULg; Lapiere, ChM

in Journal of Cell Science (1991), 100((Pt 3)), 649-55

The Hutchinson-Gilford syndrome (progeria) is a rare disorder in childhood characterized by premature and accelerated aging. This study reports the effect of a potent growth factor, EGF, on the ... [more ▼]

The Hutchinson-Gilford syndrome (progeria) is a rare disorder in childhood characterized by premature and accelerated aging. This study reports the effect of a potent growth factor, EGF, on the proliferative capacities and extracellular matrix macromolecules and collagenase expression of two strains of progeria skin-derived cells. At low population doubling levels (PDL less than 10), confluent cultures of progeria fibroblasts made quiescent by lowering the concentration of serum in the medium did not respond to EGF while the mitotic activity of normal PDL-matched fibroblasts was almost maximally restored upon addition of EGF. No obvious difference between normal and low PDL progeria fibroblasts was observed in the number and in the affinity of the receptors measured by [125I]EGF binding. The synthesis of collagen and non-collagen proteins was similar in normal and affected cells at low and high serum concentration and both types of cells responded to EGF by a specific inhibition of collagen synthesis. Besides a normal level of mRNA coding for type I and type III collagens, collagenase and laminin, progeria fibroblasts expressed a high level of elastin and type IV collagen mRNA. Like normal fibroblasts, progeria cells responded to EGF by a decrease in the level of mRNA for fibrillar collagens and elastin. In contrast, a complete lack of response to EGF was observed for collagenase mRNA whereas the expression of this enzyme was strikingly induced by EGF in normal PDL-matched cells. The abnormal expression of type IV collagen was not significantly modified by EGF. At PDL greater than 10, progeria cells exhibited features of senescence. A significant reduction of collagen synthesis was observed and no further inhibition by EGF was recorded. [less ▲]

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See detailResponse to Epidermal Growth Factor of Skin Fibroblasts from Donors of Varying Age Is Modulated by the Extracellular Matrix
Colige, Alain ULg; Nusgens, Betty ULg; Lapiere, ChM

in Journal of Cellular Physiology (1990), 145(3), 450-7

The present study was undertaken to investigate the effect of epidermal growth factor (EGF) on the biosynthetic activity of skin fibroblasts from donors of varying age and the modulation of their response ... [more ▼]

The present study was undertaken to investigate the effect of epidermal growth factor (EGF) on the biosynthetic activity of skin fibroblasts from donors of varying age and the modulation of their response to this growth factor by culture in a three-dimensional extracellular matrix. When cultured in monolayer on plastic or at the surface of a collagen gel, EGF specifically inhibited collagen synthesis whatever the age of the donor (from 17 to 84 years, n = 11). This inhibition was paralleled by a significant decrease in the steady-state level of procollagen type I mRNAs. When embedded in a three-dimensional floating collagen lattice, EGF stimulated the non-collagen protein (NCP) synthesis in fibroblasts from younger donors (5 out of 6) while fibroblasts from the older ones were not affected. Collagen production by fibroblasts from younger donors was not inhibited as in monolayer (some being even stimulated) while that of the older donors was inhibited as observed in monolayer. The steady-state level of procollagen type I mRNA was not modified by EGF in the three-dimensional culture. No significant difference was observed in the affinity and the number of EGF receptors of the fibroblasts on plastic or embedded in a collagen lattice between young and aged donors. Our results suggest that the environment of the cells can modulate the reactivity to EGF and reveal differences related to in vivo aging. [less ▲]

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