ArticleThe Journal of biological chemistry2018
Elastin is heterogeneously cross-linked.
Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 72 citations in OpenAlex.
- The role of ECM mechanics in cancer mechanotransduction through unraveling the molecular machinery of integrins, FAK, and YAP signaling.Cellular & molecular biology letters · 2026Review
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- Beyond the Critical Threshold: Elastic Fiber Remodeling and Fracture in the Pathogenesis of Pulmonary Emphysema.International journal of molecular sciences · 2025Review
- Structure and Function of the Extracellular Matrix in Normal and Pathological Conditions: Looking at the Bicuspid Aortic Valve.International journal of molecular sciences · 2025Review
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- Extracellular matrix dysregulation in aging, calcification, and cancer diseases: insights into cellular senescence, inflammation, and novel therapeutic strategies.International journal of biological sciences · 2025Review
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- Vascular Extracellular Matrix in Atherosclerosis.International journal of molecular sciences · 2024Review
- Elastin recoil is driven by the hydrophobic effect.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Extracellular matrix protein composition dynamically changes during murine forelimb development.iScience · 2024Article
- Lysyl Oxidases as Targets for Cancer Therapy and Diagnostic Imaging.ChemMedChem · 2023Review
- Mechanical Behavior of Octopus Egg Tethers Composed of Topologically Constrained, Tandemly Repeated EGF Domains.Biomacromolecules · 2023Article
- Calcification of Various Bioprosthetic Materials in Rats: Is It Really Different?International journal of molecular sciences · 2023Article
- Mechanical Properties and Functions of Elastin: An Overview.Biomolecules · 2023Review
- Performance of xenogeneic pulmonary visceral pleura as bioprosthetic heart valve cusps in swine.Frontiers in cardiovascular medicine · 2023Article
- Exploring Biomolecular Self-Assembly with Far-Infrared Radiation.Biomolecules · 2022Review
- Dynamics in natural and designed elastins and their relation to elastic fiber structure and recoil.Biophysical journal · 2021Article
- Fuzzy binding model of molecular interactions between tropoelastin and integrin alphaVbeta3.Biophysical journal · 2021Article
- Pentagalloyl glucose (PGG) partially prevents arterial mechanical changes due to elastin degradation.Experimental mechanics · 2021Article
- Tropoelastin and Elastin Assembly.Frontiers in bioengineering and biotechnology · 2021Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Elastin is an essential vertebrate protein responsible for the elasticity of force-bearing tissues such as those of the lungs, blood vessels, and skin. One of the key features required for the exceptional properties of this durable biopolymer is the extensive covalent cross-linking between domains of its monomer molecule tropoelastin. To date, elastin's exact molecular assembly and mechanical properties are poorly understood. Here, using bovine elastin, we investigated the different types of cross-links in mature elastin to gain insight into its structure. We purified and proteolytically cleaved elastin from a single tissue sample into soluble cross-linked and noncross-linked peptides that we studied by high-resolution MS. This analysis enabled the elucidation of cross-links and other elastin modifications. We found that the lysine residues within the tropoelastin sequence were simultaneously unmodified and involved in various types of cross-links with different other domains. The Lys-Pro domains were almost exclusively linked via lysinonorleucine, whereas Lys-Ala domains were found to be cross-linked via lysinonorleucine, allysine aldol, and desmosine. Unexpectedly, we identified a high number of intramolecular cross-links between lysine residues in close proximity. In summary, we show on the molecular level that elastin formation involves random cross-linking of tropoelastin monomers resulting in an unordered network, an unexpected finding compared with previous assumptions of an overall beaded structure.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.