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OBJECTIVE Skin extracellular matrix (ECM) is a dense and well-organized structure produced by fibroblasts. This ECM transduces environmental mechano-signals to cell nucleus through the integrin-actin complex, this triggering ECM protein syntheses. The aim of this study was to discover a novel peptide, structurally related to dermal matrikines, that promotes syntheses of ECM components. METHODS & RESULTS Screening tests with 120 peptides were carried out by using normal dermal human fibroblasts (HF). As a result, one candidate of interest was isolated, the N-Prolyl Palmitoyl-Tripeptide-56 Acetate (PP56), which increases collagen and fibronectin productions at gene and/or protein levels. Using liquid chromatography-tandem mass spectrometry (LC-MS/MS), a recent and innovative analytical technology, in addition to more traditional techniques, it was showed that two metabolic pathways were significantly modulated: one for collagen production and one for actin. Moreover, this peptide upregulated the transcription of Forkhead Box O (FOXO) and sestrin messenger RNAs (mRNA), leading to production of proteins involved into longevity and more recently in collagen production. RESULTS Results indicated that this peptide is a potential candidate to improve ECM density and organization in a new way. INTRODUCTION A cc ep te d A rt ic le TITLE: A New Matrikine-Derived Peptide Up-Regulates Longevity-Genes for Improving Extracellular Matrix Architecture and Connections of Dermal Cell with its Matrix. Presented at the 24th Conference of IFSCC, 23 – 25 October 2017, Seoul, Korea LEROUX R. PhD, RINGENBACH C. MSc, MARCHAND T. MSc, PESCHARD O. PhD, and MONDON P. PhD* SEDERMA, 29 rue du Chemin Vert; 78612 Le Perray-en-Yvelines cedex; France This article has been accepted for publication and undergone full peer review but has not been through the copyediting, typesetting, pagination and proofreading process, which may lead to differences between this version and the Version of Record. Please cite this article as doi: 10.1111/ICS.12584 This article is protected by copyright. All rights reserved This article is protected by copyright. All rights reserved Tissue homeostasis is controlled by interactions between cells and extracellular matrices [1]. The cells produce their surrounding extracellular matrix (ECM), which connects them together, providing information for spatial location, driving signals of attachment, multiplication, favoring syntheses and transducing mechanical environmental signals. The strong interactions between the cells and matrix are illustrated by works showing that young cells included in an aged and damaged matrix had decreased syntheses, whereas cells from an old person had their matrix syntheses reintroduced when they were included in a young matrix [2]. Thus, the quality of the matrix changes the behavior of the cells. Dermal ECM is a complex 3D-network involving several molecules interacting together such as collagen-I, -III, -IV, -VI and fibronectin. Production of mature fibrillary collagen-I is a complex mechanism with several steps which are under the control of a cohort of enzymes involved in collagen production and maturation (Peptidylproline cis-trans Isomerase: PPI, Prolyl-4-hydroxylase: P4H, Lysyl Hydroxylase: PLOD1, Collagen Galactosyl Hydroxylysyl Transferase: COLGALT and Galactosylhydroxylysyl-glucosyl Transferase: GGT) or in its deposition (N-proteinase: ADAMTS and Type I Procollagen C-proteinase Enhancer protein: PCOLCE) [3-8]. Production of several collagens is well known to be modified with age and photo-exposures; consequently, this weakens the quality of dermal ECM [9-13]. In addition, the impairment of the non-fibrillary collagen-VI induces a thinner dermis due to loosening property as an ECM organizer, a reduced production of collagen and proteoglycans and deposition of fibronectin [14, 15]. So, improving the quality of the ECM and the production of its proteins are of interest to fight against skin aging and damage. A cc ep te d A rt ic le
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