Characterization of an unusual tropoelastin with truncated C-terminus in the frog

Miao, Ming; Stahl, Richard; Petersen, L.; Reintsch, Wolfgang; Davis, Elaine C.; Keeley, Fred W.

doi:10.1016/j.matbio.2009.07.003

Cited by 13 publications

(12 citation statements)

References 33 publications

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“…We have shown in previous work in vitro that peptides based on synthetic KP domains containing Lya instead of Lys are able to form of DES/IDES [22]. Although it contains almost exclusively domains of the KP type [56,57], the DES/IDES amount is comparable to that of teleosts [58]. Other evidence for an involvement of KP domains can be seen in the results of quantitative analyses of amphibian elastin.…”

Section: Discussionmentioning

confidence: 72%

A comprehensive map of human elastin cross‐linking during elastogenesis

et al. 2019

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Elastin is an essential structural protein in the extracellular matrix of vertebrates. It is the core component of elastic fibers, which enable connective tissues such as those of the skin, lungs or blood vessels to stretch and recoil. This function is provided by elastin's exceptional properties, which mainly derive from a unique covalent cross‐linking between hydrophilic lysine‐rich motifs of units of the monomeric precursor tropoelastin. To date, elastin's cross‐linking is poorly investigated. Here, we purified elastin from human tissue and cleaved it into soluble peptides using proteases with different specificities. We then analyzed elastin's molecular structure by identifying unmodified residues, post‐translational modifications and cross‐linked peptides by high‐resolution mass spectrometry and amino acid analysis. The data revealed the presence of multiple isoforms in parallel and a complex and heterogeneous molecular interconnection. We discovered that the same lysine residues in different monomers were simultaneously involved in various cross‐link types or remained unmodified. Furthermore, both types of cross‐linking domains, Lys‐Pro and Lys‐Ala domains, participate not only in bifunctional inter‐ but also in intra‐domain cross‐links. We elucidated the sequences of several desmosine‐containing peptides and the contribution of distinct domains such as 6, 14 and 25. In contrast to earlier assumptions proposing that desmosine cross‐links are formed solely between two domains, we elucidated the structure of a peptide that proves a desmosine formation with participation of three Lys‐Ala domains. In summary, these results provide new and detailed insights into the cross‐linking process, which takes place within and between human tropoelastin units in a stochastic manner.

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Section: Discussionmentioning

confidence: 72%

A comprehensive map of human elastin cross‐linking during elastogenesis

et al. 2019

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“…The alternating hydrophobic and crosslinking domain arrangement characteristic of human tropoelastin (hTE) is shown diagramatically in Figure . Similar alternating domain arrangements are present in tropoelastins of other species . Domains 21 and 23 are typical of most crosslinking domains in mammalian tropoelastins and include lysine residues present in KAAK or KAAAK motifs usually preceded by an alanine‐rich sequence (Table ).…”

Section: Resultsmentioning

confidence: 87%

Sequence and domain arrangements influence mechanical properties of elastin‐like polymeric elastomers

et al. 2013

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Elastin is the polymeric, extracellular matrix protein that provides properties of extensibility and elastic recoil to large arteries, lung parenchyma, and other tissues. Elastin assembles by crosslinking through lysine residues of its monomeric precursor, tropoelastin. Tropoelastin, as well as polypeptides based on tropoelastin sequences, undergo a process of self-assembly that aligns lysine residues for crosslinking. As a result, both the full-length monomer as well as elastin-like polypeptides (ELPs) can be made into biomaterials whose properties resemble those of native polymeric elastin. Using both full-length human tropoelastin (hTE) as well as ELPs, we and others have previously reported on the influence of sequence and domain arrangements on self-assembly properties. Here we investigate the role of domain sequence and organization on the tensile mechanical properties of crosslinked biomaterials fabricated from ELP variants. In general, substitutions in ELPs involving similiar domain types (hydrophobic or crosslinking) had little effect on mechanical properties. However, modifications altering either the structure or the characteristic sequence style of these domains had significant effects on such properties. In addition, using a series of deletion and replacement constructs for full-length hTE, we provide new insights into the role of conserved domains of tropoelastin in determining mechanical properties.

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“…This finding suggests a potential driving force for maintaining relatively short elastomeric domains associated with these proteins. In elastin, for example, individual elastomeric domains may be as short as 5 amino acids, as found between the two cross-linking domains encoded by exons 23 and 24 in tropoelastin-2 of Xenopus tropicalis [54]. However, it is noted that here we only explored a limited number of conformations, in the next section, we explore the impact of a wider range of rod architectures on aggregate morphology.…”

Section: Resultsmentioning

confidence: 99%

Modelling the Self-Assembly of Elastomeric Proteins Provides Insights into the Evolution of Their Domain Architectures

Song

Parkinson

2012

PLoS Comput Biol

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Elastomeric proteins have evolved independently multiple times through evolution. Produced as monomers, they self-assemble into polymeric structures that impart properties of stretch and recoil. They are composed of an alternating domain architecture of elastomeric domains interspersed with cross-linking elements. While the former provide the elasticity as well as help drive the assembly process, the latter serve to stabilise the polymer. Changes in the number and arrangement of the elastomeric and cross-linking regions have been shown to significantly impact their assembly and mechanical properties. However, to date, such studies are relatively limited. Here we present a theoretical study that examines the impact of domain architecture on polymer assembly and integrity. At the core of this study is a novel simulation environment that uses a model of diffusion limited aggregation to simulate the self-assembly of rod-like particles with alternating domain architectures. Applying the model to different domain architectures, we generate a variety of aggregates which are subsequently analysed by graph-theoretic metrics to predict their structural integrity. Our results show that the relative length and number of elastomeric and cross-linking domains can significantly impact the morphology and structural integrity of the resultant polymeric structure. For example, the most highly connected polymers were those constructed from asymmetric rods consisting of relatively large cross-linking elements interspersed with smaller elastomeric domains. In addition to providing insights into the evolution of elastomeric proteins, simulations such as those presented here may prove valuable for the tuneable design of new molecules that may be exploited as useful biomaterials.

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Characterization of an unusual tropoelastin with truncated C-terminus in the frog

Cited by 13 publications

References 33 publications

A comprehensive map of human elastin cross‐linking during elastogenesis

A comprehensive map of human elastin cross‐linking during elastogenesis

Sequence and domain arrangements influence mechanical properties of elastin‐like polymeric elastomers

Modelling the Self-Assembly of Elastomeric Proteins Provides Insights into the Evolution of Their Domain Architectures

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