Degradation of tropoelastin and skin elastin by neprilysin.

Autor: Mora Huertas AC; Institute of Pharmacy, Faculty of Natural Sciences I, Martin Luther University Halle-Wittenberg, Halle (Saale), Germany., Schmelzer CEH; Institute of Pharmacy, Faculty of Natural Sciences I, Martin Luther University Halle-Wittenberg, Halle (Saale), Germany; Fraunhofer Institute for Microstructure of Materials and Systems IMWS, Halle (Saale), Germany., Luise C; Institute of Pharmacy, Faculty of Natural Sciences I, Martin Luther University Halle-Wittenberg, Halle (Saale), Germany., Sippl W; Institute of Pharmacy, Faculty of Natural Sciences I, Martin Luther University Halle-Wittenberg, Halle (Saale), Germany., Pietzsch M; Institute of Pharmacy, Faculty of Natural Sciences I, Martin Luther University Halle-Wittenberg, Halle (Saale), Germany., Hoehenwarter W; Proteome Analytics, Leibniz Institute of Plant Biochemistry, Halle (Saale), Germany., Heinz A; Institute of Pharmacy, Faculty of Natural Sciences I, Martin Luther University Halle-Wittenberg, Halle (Saale), Germany; Department of Pharmacy, University of Copenhagen, Copenhagen, Denmark. Electronic address: andrea.heinz@sund.ku.dk.
Jazyk: angličtina
Zdroj: Biochimie [Biochimie] 2018 Mar; Vol. 146, pp. 73-78. Date of Electronic Publication: 2017 Nov 29.
DOI: 10.1016/j.biochi.2017.11.018
Abstrakt: Neprilysin is also known as skin fibroblast-derived elastase, and its up-regulation during aging is associated with impairments of the elastic fiber network, loss of skin elasticity and wrinkle formation. However, information on its elastase activity is still limited. The aim of this study was to investigate the degradation of fibrillar skin elastin by neprilysin and the influence of the donor's age on the degradation process using mass spectrometry and bioinformatics approaches. The results showed that cleavage by neprilysin is dependent on previous damage of elastin. While neprilysin does not cleave young and intact skin elastin well, it degrades elastin fibers from older donors, which may further promote aging processes. With regards to the cleavage behavior of neprilysin, a strong preference for Gly at P1 was found, while Gly, Ala and Val were well accepted at P1' upon cleavage of tropoelastin and skin elastin. The results of the study indicate that the progressive release of bioactive elastin peptides by neprilysin upon skin aging may enhance local tissue damage and accelerate extracellular matrix aging processes.
(Copyright © 2017 Elsevier B.V. and Société Française de Biochimie et Biologie Moléculaire (SFBBM). All rights reserved.)
Databáze: MEDLINE
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