Unique molecular networks: Formation and role of elastin cross-links
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Unique molecular networks : Formation and role of elastin cross-links. / Schmelzer, Christian E H; Hedtke, Tobias; Heinz, Andrea.
In: IUBMB Life, Vol. 55, No. 3, 2020, p. 842-854.Research output: Contribution to journal › Review › Research › peer-review
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TY - JOUR
T1 - Unique molecular networks
T2 - Formation and role of elastin cross-links
AU - Schmelzer, Christian E H
AU - Hedtke, Tobias
AU - Heinz, Andrea
N1 - © 2019 The Authors. IUBMB Life published by Wiley Periodicals, Inc. on behalf of International Union of Biochemistry and Molecular Biology.
PY - 2020
Y1 - 2020
N2 - Elastic fibers are essential assemblies of vertebrates and confer elasticity and resilience to various organs including blood vessels, lungs, skin, and ligaments. Mature fibers, which comprise a dense and insoluble elastin core and a microfibrillar mantle, are extremely resistant toward intrinsic and extrinsic influences and maintain elastic function over the human lifespan in healthy conditions. The oxidative deamination of peptidyl lysine to peptidyl allysine in elastin's precursor tropoelastin is a crucial posttranslational step in their formation. The modification is catalyzed by members of the family of lysyl oxidases and the starting point for subsequent manifold condensation reactions that eventually lead to the highly cross-linked elastomer. This review summarizes the current understanding of the formation of cross-links within and between the monomer molecules, the molecular sites, and cross-link types involved and the pathological consequences of abnormalities in the cross-linking process.
AB - Elastic fibers are essential assemblies of vertebrates and confer elasticity and resilience to various organs including blood vessels, lungs, skin, and ligaments. Mature fibers, which comprise a dense and insoluble elastin core and a microfibrillar mantle, are extremely resistant toward intrinsic and extrinsic influences and maintain elastic function over the human lifespan in healthy conditions. The oxidative deamination of peptidyl lysine to peptidyl allysine in elastin's precursor tropoelastin is a crucial posttranslational step in their formation. The modification is catalyzed by members of the family of lysyl oxidases and the starting point for subsequent manifold condensation reactions that eventually lead to the highly cross-linked elastomer. This review summarizes the current understanding of the formation of cross-links within and between the monomer molecules, the molecular sites, and cross-link types involved and the pathological consequences of abnormalities in the cross-linking process.
U2 - 10.1002/iub.2213
DO - 10.1002/iub.2213
M3 - Review
C2 - 31834666
VL - 55
SP - 842
EP - 854
JO - IUBMB Life
JF - IUBMB Life
SN - 1521-6543
IS - 3
ER -
ID: 232270415