ArticleProceedings of the National Academy of Sciences of the United States of America2012
Tropoelastin bridge region positions the cell-interactive C terminus and contributes to elastic fiber assembly.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed.
- Evolutionary constraints on positional sequence, collective properties and sequence style of tropoelastin dictated by fundamental requirements for formation and function of the extracellular elastic matrix.Matrix biology plus · 2025Review
- Elastin turnover in ocular diseases: A special focus on age-related macular degeneration.Experimental eye research · 2022Review
- Structural studies of elastic fibre and microfibrillar proteins.Matrix biology plus · 2021Article
- A coarse-grained mechanical model for folding and unfolding of tropoelastin with possible mutations.Acta biomaterialia · 2021Article
- Tropoelastin and Elastin Assembly.Frontiers in bioengineering and biotechnology · 2021Review
- Natural-Based Hydrogels for Tissue Engineering Applications.Molecules (Basel, Switzerland) · 2020Review
- Transglutaminase-Mediated Cross-Linking of Tropoelastin to Fibrillin Stabilises the Elastin Precursor Prior to Elastic Fibre Assembly.Journal of molecular biology · 2020Article
- Allysine modifications perturb tropoelastin structure and mobility on a local and global scale.Matrix biology plus · 2019Article
- Synthesis and Mechanochemical Activity of Peptide-Based Cu(I) Bis(Biomimetics (Basel, Switzerland) · 2019Article
- Molecular model of human tropoelastin and implications of associated mutations.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Targeted Modulation of Tropoelastin Structure and Assembly.ACS biomaterials science & engineering · 2017Article
- Design of an elastin-layered dermal regeneration template.Acta biomaterialia · 2017Article
- The Coupled Bio-Chemo-Electro-Mechanical Behavior of Glucose Exposed Arterial Elastin.Journal of physics D: Applied physics · 2017Article
- Article
- Blended Polyurethane and Tropoelastin as a Novel Class of Biologically Interactive Elastomer.Tissue engineering. Part A · 2016Article
- Subtle balance of tropoelastin molecular shape and flexibility regulates dynamics and hierarchical assembly.Science advances · 2016Article
- Silk-elastin-like protein biomaterials for the controlled delivery of therapeutics.Expert opinion on drug delivery · 2015Review
- Mechanistic insight into the elastin degradation process by the metalloprotease myroilysin from the deep-sea bacterium Myroides profundi D25.Marine drugs · 2015Article
- A negatively charged residue stabilizes the tropoelastin N-terminal region for elastic fiber assembly.The Journal of biological chemistry · 2014Article
- Tropoelastin: a versatile, bioactive assembly module.Acta biomaterialia · 2014Review
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Authors and funding
9 authors.
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No grant is acknowledged in the PubMed record.
Abstract
The tropoelastin monomer undergoes stages of association by coacervation, deposition onto microfibrils, and cross-linking to form elastic fibers. Tropoelastin consists of an elastic N-terminal coil region and a cell-interactive C-terminal foot region linked together by a highly exposed bridge region. The bridge region is conveniently positioned to modulate elastic fiber assembly through association by coacervation and its proximity to dominant cross-linking domains. Tropoelastin constructs that either modify or remove the entire bridge and downstream regions were assessed for elastogenesis. These constructs focused on a single alanine substitution (R515A) and a truncation (M155n) at the highly conserved arginine 515 site that borders the bridge. Each form displayed less efficient coacervation, impaired hydrogel formation, and decreased dermal fibroblast attachment compared to wild-type tropoelastin. The R515A mutant protein additionally showed reduced elastic fiber formation upon addition to human retinal pigmented epithelium cells and dermal fibroblasts. The small-angle X-ray scattering nanostructure of the R515A mutant protein revealed greater conformational flexibility around the bridge and C-terminal regions. This increased flexibility of the R515A mutant suggests that the tropoelastin R515 residue stabilizes the structure of the bridge region, which is critical for elastic fiber assembly.
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