For example, the tetrafunctional cross-link, on which the model is based, is derived from porcine elastin (Brown-Augsburger et al., 1995). Biochemistry of tropoelastin. 21:063001. doi: 10.1088/0965-0393/21/6/063001, Tarakanova, A., Huang, W., Weiss, A. S., Kaplan, D. L., and Buehler, M. J. PLoS One 7:e46130. A., Gray, W. R., and Franzblau, C. (1973). Closer to the base of the molecule, the flexible hinge region between domains 21 and 23 presented with a scissors-like bending, which is now believed to contribute to elasticity and multimeric assembly through enhanced conformational space sampling (Tarakanova et al., 2019b). J. doi: 10.7554/eLife.26526. Combinations of these two amino acids result in domains that undergo rapid conformational sampling (Rauscher and Pomes, 2017), which, if perturbed toward a conformation that gravitate toward stability, will assemble into highly ordered amyloid-like fibrils that are not elastomeric (Rauscher et al., 2006; Roberts et al., 2015). FEBS Lett. Matrix Biol. For many years it was difficult to study tropoelastin at an atomic scale, but the application of computational methods, such as full-atomistic molecular dynamics and elastic network models, in combination with powerful low-resolution structural studies, have expanded the field and delivered an enhanced understanding of the mechanisms that contribute to self-assembly. A novel cell adhesion region in tropoelastin mediates attachment to integrin alphaVbeta5. Integrins canonically bind proteins containing Arg-Glu-Asp motifs, but this sequence is not found in tropoelastin (Lee et al., 2014). doi: 10.1096/fj.201801860RR, Schrader, C. U., Heinz, A., Majovsky, P., Karaman Mayack, B., Brinckmann, J., Sippl, W., et al. doi: 10.1038/246461a0, Haust, M. D., More, R. H., Bencosme, S. A., and Balis, J. U. 29, 152159. Front. Poly (Val-Gly-Gly-Leu-Gly). Localizing alpha-helices in human tropoelastin: assembly of the elastin puzzle. doi: 10.1074/jbc.M501390200, Chung, M. I., Miao, M., Stahl, R. J., Chan, E., Parkinson, J., and Keeley, F. W. (2006). Elastin-like polypeptides as models of intrinsically disordered proteins. 16,17 We have previously shown that monomeric TE is utilized as a substrate by dermal fibroblasts in the formation of elastin fibroblasts in vitro, where Alternative splicing of human elastin mRNA indicated by sequence analysis of cloned genomic and complementary DNA. Synthesis and properties of crosslinked recombinant pro-resilin. Structure 14, 16671676. Biochim. The flexibility of the mid-region of the molecule was proposed to drive the overall elasticity of the resultant fibers. AW gratefully acknowledges NHMRC funding (Ref: 1195827). doi: 10.1002/mabi.201800250, Tiedemann, K., Batge, B., Muller, P. K., and Reinhardt, D. P. (2001). doi: 10.1080/07391102.1992.10508661, Tamburro, A. M., Pepe, A., and Bochicchio, B. Dissection of human tropoelastin: solution structure, dynamics and self-assembly of the exon 5 peptide. Elastagen's revolutionary recombinant human tropoelastin, is identical to that present in human tissue and has many clinical applications, including effective breakthrough treatments for acne. Most organisms contain one copy of ELN, other than teleosts and amphibians which notably possess two distinct types of ELN genes (He et al., 2007; Miao et al., 2007, 2009). 7:32. doi: 10.3389/fphar.2016.00032, Schmelzer, C. E. H., Heinz, A., Troilo, H., Lockhart-Cairns, M. P., Jowitt, T. A., Marchand, M. F., et al. Even after being able to produce recombinant tropoelastin at scales suited to characterization studies, traditional techniques have not yet produced an experimentally verified atomistic structure (Martin et al., 1995; Tarakanova and Buehler, 2013). Proc. In addition to the RKRK sequence, domain 36 contains tropoelastins sole two cysteines and only disulfide bond. Natl. Its estimated half-life of 70 years (Shapiro et al., 1991) is due to its extensive cross-linking and high hydrophobicity, which render it resistant to degradation (Vrhovski and Weiss, 1998; Schrader et al., 2018; Hedtke et al., 2019). 293, 1510715119. Another region of note is domain 36, which contains lysines but does not participate in cross-linking (Hedtke et al., 2019). For Allergan, contact: Lisa Brown 1-862-261-7320, 1985 - 2023 BioSpace.com. 19:e1800250. All authors contributed to writing and editing the review. The resultant bending motion rather than scissors-twist motion that stemmed from this stabilization highlights the mutants diminished flexibility as a key driver of impaired fiber assembly in cutis laxa (Tarakanova et al., 2018). Acad. doi: 10.1016/0014-4800(65)90015-8, He, D., Chung, M., Chan, E., Alleyne, T., Ha, K. C. H., Miao, M., et al. Elastagens tropoelastin is identical to that present in human tissue, and has many potential clinical applications, including treatment for acne scars, stretch marks, aesthetic skin repair and surgical wound repair. Coacervation of recombinant human tropoelastin is strongly influenced by the concentration of protein and NaCl and to a lesser extent on pH. Albert, E. N. (1972). 31, 261272. Matrix Biol. 589(19 Pt A), 24772486. The authors wrote and submitted this manuscript in response to an invitation by the Editor. Computational approaches have gained popularity in recent decades as their methodologies have been refined to provide accurate atomistic scale insights into molecular structure and movement (Tarakanova et al., 2018). Biotechnol. Tropoelastin is a low complexity protein on both primary and secondary sequence levels. Structural analysis of photocrosslinkable methacryloyl-modified protein derivatives. This suggests the ERCs primary signal pathways are involved in wound recognition through fragments of elastin, where EDPs are formed as a result of elastic tissue damage. Coarse-grained model of tropoelastin self-assembly into nascent fibrils. Baul, U., Bley, M., and Dzubiella, J. The process of tropoelastin aggregation is initially reversible, as spherules dissipate if the temperature is lowered (Clarke et al., 2006), however, maintenance of a physiological temperature results in maturation, which is indicated by spherule coalescence and the irreversible formation of fibrillar structures (Cox et al., 1974; Bressan et al., 1983; Mithieux et al., 2005). Cryo-electron microscopy for structural analysis of dynamic biological macromolecules. Tropoelastin, the soluble precursor to elastin, and the degradation products of fragmented elastic fibers also have important chemical signaling properties. The Wellcome Trust Centre for Cell-Matrix Research is supported by funding from Wellcome Trust (203128/Z/16/Z). Protein Eng. Arch. 3:100016. doi: 10.1016/j.mtbio.2019.100016, Tarakanova, A., Yeo, G. C., Baldock, C., Weiss, A. S., and Buehler, M. J. 10, 441454. Unlike hydrophobic domains, cross-linking domains in isolation are unable to self-assemble; thus, they have been studied in the context of the cross-linking of elastin-derived biomaterials (Annabi et al., 2017; Yue et al., 2017). Multiple copies of the tropoelastin protein attach to one another and are processed to form a mature protein called elastin. Cross-linking requires the modification of at least one of the lysine participants by a member of the copper-containing LOX or lysine oxidase-like (LOXL) enzyme families. Remodelling the extracellular matrix in development and disease. Chem. Characterization of the complete human elastin gene. Tropoelastin is typically used as a thin coating on tissue culture surfaces. Tropoelastin was revealed to be an asymmetric molecule with distinct N- and C-terminal regions that are respectively referred to as the "head" and "foot" of the molecule. Evidence for the presence of alpha-aminoadipic acid delta-semialdehyde and its aldol condensation product. Biophys. (2021). The Weiss Lab's research focuses on the use of human tropoelastin in tissue assembly and wound repair. Hailed as a giant leap forward in hair rejuvenation, NULASTIN transforms the look of eyelashes up to 120% thicker and 61% longer. 1, 2 Elastogenesis, the process of elastin formation, mainly occurs during the fetal and early neonatal development of organs such as blood vessels, lungs, and skin. Chem. doi: 10.1038/sj.jid.5700047, Indik, Z., Yeh, H., Ornstein-Goldstein, N., Kucich, U., Abrams, W., Rosenbloom, J. C., et al. . No use, distribution or reproduction is permitted which does not comply with these terms. (2017). Coacervation characteristics of recombinant human tropoelastin. Thus, at lower temperatures, the water surrounding these domains forms ordered, clathrate-like shells that prevent aggregation until the appropriate temperature is reached (Wu and Weiss, 1999; Miao et al., 2003; Dandurand et al., 2015). We are very interested in the blend of biochemistry and cell biology, as well as the tissue engineering and regenerative medicine opportunities provided by this amazing elastic protein. 26, 17001709. 26, 115124. Tropoelastin is frequently described in the literature as an unstructured protein, mainly because models of elasticity invoke an element of disorder within the structure (4, 9, 10).While this concept appears to be the case at the fine, more subtle intramolecular level, chaos alone is unlikely to explain the ordered assembly of tropoelastin which culminates in the formation of organized . Cell Biol. (2019). Genet. This temperature is also known as the transition temperature. Proc. 2:e1501145. J. Biochem. They are ubiquitous across most vertebrates other than lower vertebrates such as species from the superclass Agnatha (jawless fish) (Debelle and Tamburro, 1999). Elastin as a random-network elastomer: a mechanical and optical analysis of single elastin fibers. Cell Biol. Conformational transitions of the cross-linking domains of elastin during self-assembly. Figure 2. Cell Biol. Forty tropoelastin molecules were subjected to simulations using a MARTINI-based coarse-grained model, integrated with an elastic network model (Tarakanova et al., 2019a). doi: 10.1021/bi060289i, Tarakanova, A., and Buehler, M. J. The remaining authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest. Macromol. The N-terminal head caps an extended coil region that consists of domains 218. J. Pathol. A new amino acid from hydrolysates of elastin. Tropoelastin bridge region positions the cell-interactive C terminus and contributes to elastic fiber assembly. This review focuses on recent developments that have shaped our current knowledge of elastin assembly through understanding the relationship between tropoelastins structure and function. doi: 10.1074/jbc.M004265200, Kadler, K. E. (2017). Nature 451, 977980. doi: 10.1016/0005-2795(73)90368-1, Franzblau, C., Faris, B., and Papaioannou, R. (1969). Allergan's Medical Aesthetics business - a comprehensive portfolio of facial aesthetics, body contouring and plastic and regenerative medicine products - is expected to grow at an 8-10 percent CAGR from 2017 to 2025. doi: 10.1016/j.ajhg.2009.09.013. 11 Articles, This article is part of the Research Topic, Tropoelastin-Cell Receptor Interactions and Implications for Assembly, https://doi.org/10.3389/fbioe.2021.643110, Creative Commons Attribution License (CC BY). Implications for microfibril and elastic fiber assembly. Tropoelastin aggregates at physiological temperature due to interactions between hydrophobic domains in a process called coacervation. Engineering a highly elastic human protein-based sealant for surgical applications. With leaps in the improvement of cryogenic electron microscopy to characterize flexible molecules, we predict that this approach will contribute to a deeper understanding of tropoelastin structure and self-assembly in the context of endogenous fiber formation and biomaterials fabrication. Partridge, S. M. (1966). (2015). KA domains were initially thought to form -helices and poly-proline II helices (PPII) due to the presence of cross-links which require a lysine arrangement that was postulated to be achieved via -helical configuration (Brown-Augsburger et al., 1995). Hydrophobic domains of human tropoelastin interact in a context-dependent manner. Tropoelastin is a unique protein with biochemical and physical properties that allow it to rapidly self-assemble into fibrous structures. Soluble matrix protein is a potent modulator of mesenchymal stem cell performance. Tropoelastin interacts with microfibril components including fibrillin-1, fibulin-4, and -5, and other associated molecules such as latent transforming growth factor binding protein-4 (Visconti et al., 2003; McLaughlin et al., 2006; Urban et al., 2009; Yamauchi et al., 2010; Noda et al., 2013; Lockhart-Cairns et al., 2020). 289, 1005710068. doi: 10.1016/j.jsb.2004.11.005, Muiznieks, L. D., Jensen, S. A., and Weiss, A. S. (2003). Received: 17 December 2020; Accepted: 08 February 2021;Published: 25 February 2021. This suggests a high level of conformational sampling during this phase of coacervation, indicating that the flexibility of tropoelastin plays a key role in assembly that may persist, to some extent, into later stages of assembly (Reichheld et al., 2020). 258, 118. Matrix Biol. Elastin binding protein and FKBP65 modulate in vitro self-assembly of human tropoelastin. 275, 2844928454. Cryo-electron microscopy is a rapidly developing method and likely to contribute to structural knowledge of tropoelastin. Fibrillin-rich microfibrils of the extracellular matrix: ultrastructure and assembly.
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