Degradation of tropoelastin and skin elastin by neprilysin

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Standard

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

Harvard

Mora Huertas, AC, Schmelzer, CEH, Luise, C, Sippl, W, Pietzsch, M, Hoehenwarter, W & Heinz, A 2018, 'Degradation of tropoelastin and skin elastin by neprilysin', Biochimie, bind 146, s. 73-78. https://doi.org/10.1016/j.biochi.2017.11.018

APA

Mora Huertas, A. C., Schmelzer, C. E. H., Luise, C., Sippl, W., Pietzsch, M., Hoehenwarter, W., & Heinz, A. (2018). Degradation of tropoelastin and skin elastin by neprilysin. Biochimie, 146, 73-78. https://doi.org/10.1016/j.biochi.2017.11.018

Vancouver

Mora Huertas AC, Schmelzer CEH, Luise C, Sippl W, Pietzsch M, Hoehenwarter W o.a. Degradation of tropoelastin and skin elastin by neprilysin. Biochimie. 2018;146:73-78. https://doi.org/10.1016/j.biochi.2017.11.018

Author

Mora Huertas, Angela C. ; Schmelzer, Christian E. H. ; Luise, Chiara ; Sippl, Wolfgang ; Pietzsch, Markus ; Hoehenwarter, Wolfgang ; Heinz, Andrea. / Degradation of tropoelastin and skin elastin by neprilysin. I: Biochimie. 2018 ; Bind 146. s. 73-78.

Bibtex

@article{a1c647728eca41f1b07dc296af04e7ce,
title = "Degradation of tropoelastin and skin elastin by neprilysin",
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 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.",
author = "{Mora Huertas}, {Angela C.} and Schmelzer, {Christian E. H.} and Chiara Luise and Wolfgang Sippl and Markus Pietzsch and Wolfgang Hoehenwarter and Andrea Heinz",
year = "2018",
doi = "10.1016/j.biochi.2017.11.018",
language = "English",
volume = "146",
pages = "73--78",
journal = "Biochimie",
issn = "0300-9084",
publisher = "Elsevier Masson",

}

RIS

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