Journal
BIOCHIMIE
Volume 146, Issue -, Pages 73-78Publisher
ELSEVIER FRANCE-EDITIONS SCIENTIFIQUES MEDICALES ELSEVIER
DOI: 10.1016/j.biochi.2017.11.018
Keywords
Skin fibroblast-derived elastase; Mass spectrometry; Skin aging; Matrikines
Categories
Funding
- German Research Foundation (DFG) [HE 6190/1-2]
- LEO Foundation Center for Cutaneous Drug Delivery
- Departamento Administrativo de Ciencia, Tecnologia e Innovacion - Colciencias (Colombia)
- Universidad Nacional de Colombia (Bogota D.C., Colombia)
- Fraunhofer Internal Programs [Attract 069-608203]
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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. (c) 2017 Elsevier B.V. and Societe Francaise de Biochimie et Biologie Moleculaire (SFBBM). All rights reserved.
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