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Effect of elastin peptides on the production of matrix metalloproteinase 2 by human skin fibroblasts in culture

Abstract : Soluble elastin-derived peptides from alkaline or elastase hydrolysis of insoluble elastin, as well as tropoelastin, increase matrix metalloproteinase-2 (MMP-2) production by human skin fibroblasts in culture as determined by gelatin zymography and ELISA. Such an effect is time and concentration dependent; it can be reproduced by synthetic elastin: VGVAPG, PGAIPG, and laminin: LGTIPG, hexapeptides and inhibited by lactose and is therefore elastin receptor-mediated. The steady state levels of MMP-2 mRNAs are invariant following elastin-fibroblasts interaction. Inhibition of phospholipase C (D-609), ADP-ribosylation factor (brefeldin), protein kinase C (RO-318220) and phospholipase D (1-propanol) totally abolished the elastin-mediated increase of MMP-2 production. It suggested that the post-transcriptional mechanism controlling the elastin-mediated overproduction of MMP-2 involved a cascade leading to phospholipase D activation.
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https://hal.univ-reims.fr/hal-02328921
Contributor : Laurent Debelle Connect in order to contact the contributor
Submitted on : Wednesday, October 23, 2019 - 1:30:11 PM
Last modification on : Monday, January 24, 2022 - 4:50:03 PM

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  • HAL Id : hal-02328921, version 1
  • PUBMED : 11723829

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E. Huet, B. Brassart, J. Wallach, L. Debelle, B Haye, et al.. Effect of elastin peptides on the production of matrix metalloproteinase 2 by human skin fibroblasts in culture. Journal- Societe de Biologie, Paris : Société de biologie, 2001, 195 (2), pp.165-72. ⟨hal-02328921⟩

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