Degradation of tropoelastin and skin elastin by neprilysin
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Degradation of tropoelastin and skin elastin by neprilysin. / Mora Huertas, Angela C.; Schmelzer, Christian E. H.; Luise, Chiara; Sippl, Wolfgang; Pietzsch, Markus; Hoehenwarter, Wolfgang; Heinz, Andrea.
I: Biochimie, Bind 146, 2018, s. 73-78.Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
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TY - JOUR
T1 - Degradation of tropoelastin and skin elastin by neprilysin
AU - Mora Huertas, Angela C.
AU - Schmelzer, Christian E. H.
AU - Luise, Chiara
AU - Sippl, Wolfgang
AU - Pietzsch, Markus
AU - Hoehenwarter, Wolfgang
AU - Heinz, Andrea
PY - 2018
Y1 - 2018
N2 - 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 thedegradation 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 intactskin 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.
AB - 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 thedegradation 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 intactskin 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.
U2 - 10.1016/j.biochi.2017.11.018
DO - 10.1016/j.biochi.2017.11.018
M3 - Journal article
C2 - 29196110
VL - 146
SP - 73
EP - 78
JO - Biochimie
JF - Biochimie
SN - 0300-9084
ER -
ID: 186423412