Abstract：
: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.
journal_name
Biochimiejournal_title
Biochimieauthors
Mora Huertas AC,Schmelzer CEH,Luise C,Sippl W,Pietzsch M,Hoehenwarter W,Heinz Adoi
10.1016/j.biochi.2017.11.018subject
Has Abstractpub_date
2018-03-01 00:00:00pages
73-78eissn
0300-9084issn
1638-6183pii
S0300-9084(17)30315-2journal_volume
146pub_type
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