Isolation and Amino Acid Sequences of Tropoelastin Peptides

Foster, Jeffrey S.; Bruenger, Eveline; Gray, William R.; Sandberg, Lawrence B.

doi:10.1016/s0021-9258(19)44088-x

Cited by 260 publications

(57 citation statements)

References 16 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…In approaching the molecular basis of the chemotactic activity of elastin peptides two points seemed important: first, the presence of fibroblast chemotactic activity in tropoelastin (23), the soluble precursor of insoluble elastin (20), suggested that the lysine-derived cross-links characteristic of insoluble elastin are not essential for the chemotactic activity of elastin peptides; and second, the presence of repeating peptide sequences in tropoelastin (4,19) directed us to look at these peptide repeats as the possible source of the chemotactic activity. In this report, we present evidence that some of the chemotactic activity of elastin is associated with Val-Gly-Val-Ala-Pro-Gly (VGVAPG),~ a hexamer that repeats six times in one tryptic fragment of porcine tropoelastin (20).…”

mentioning

confidence: 99%

Val-Gly-Val-Ala-Pro-Gly, a repeating peptide in elastin, is chemotactic for fibroblasts and monocytes.

Senior¹,

Griffin²,

Mecham³

et al. 1984

The Journal of Cell Biology

368

211

View full text Add to dashboard Cite

Recent studies have demonstrated that tropoelastin and elastin-derived peptides are chemotactic for fibroblasts and monocytes. To identify the chemotactic sites on elastin, we examined the chemotactic activity of VaI-Gly-VaI-Ala-Pro-Gly (VGVAPG), a repeating peptide in tropoelastin. We observed that VGVAPG was chemotactic for fibroblasts and monocytes, with optimal activity at ~10 -8 M, and that the chemotactic activity of VGVAPG was substantial (half or greater) relative to the maximum responses to other chemotactic factors such as platelet-derived growth factor for fibroblasts and formyl-methionyl-leucylphenylalanine for monocytes. The possibility that at least part of the chemotactic activity in tropoelastin and elastin peptides is contained in VGVAPG sequences was supported by the following: (a) polyclonal antibody to bovine elastin selectively blocked the fibroblast and monocyte chemotactic activity of both elastin-derived peptides and VGVAPG; (b) monocyte chemotaxis to VGVAPG was selectively blocked by preexposing the cells to elastin peptides; and (c) undifferentiated (nonelastin producing) bovine ligament fibroblasts, capable of chemotaxis to platelet-derived growth factor, did not show chemotactic responsiveness to either VGVAPG or elastin peptides until after matrix-induced differentiation and the onset of elastin synthesis. These studies suggest that small synthetic peptides may be able to reproduce the chemotactic activity associated with elastin-derived peptides and tropoelastin.Chemotactic activity has been associated with several components of the extracellular matrix including collagen (18), fibronectin (1, 5, 17), laminin (27), peptides of insoluble elastin (6, 22,23), and tropoelastin (23). The sites of chemotactic activity on collagen (16) and fibronectin (1, 25) have been partially localized, however the chemotactically active regions of laminin and elastin have not yet been established. The present study was undertaken to identify the site(s) of chemotactic activity on elastin.In approaching the molecular basis of the chemotactic activity of elastin peptides two points seemed important: first, the presence of fibroblast chemotactic activity in tropoelastin (23), the soluble precursor of insoluble elastin (20), suggested that the lysine-derived cross-links characteristic of insoluble elastin are not essential for the chemotactic activity of elastin peptides; and second, the presence of repeating peptide sequences in tropoelastin (4, 19) directed us to look at these peptide repeats as the possible source of the chemotactic activity. In this report, we present evidence that some of the chemotactic activity of elastin is associated with Val-Gly-ValAla-Pro-Gly (VGVAPG),~ a hexamer that repeats six times in one tryptic fragment of porcine tropoelastin (20). MATERIALS AND METHODS Preparation of Elastin-derived Peptides:Bovine ligament elastin, obtained from Elastin Products (St. Louis, MO), was solubilized with porcine pancreatic elastase (Sigma Chemical Co., St. Louis, MO) by incubation a...

show abstract

mentioning

confidence: 99%

Val-Gly-Val-Ala-Pro-Gly, a repeating peptide in elastin, is chemotactic for fibroblasts and monocytes.

Senior¹,

Griffin²,

Mecham³

et al. 1984

The Journal of Cell Biology

368

211

View full text Add to dashboard Cite

show abstract

“…The sequences were deposited in the DDBJ database under the accession numbers LC005979 (elastin, long form), LC005980 (elastin, short form), and LC060063 (osteoglycin). All the partial amino acid sequences of porcine elastin reported previously 16) were found in the amino acid sequence translated from LC005979. The sequences determined in the present study were used to interpret the results given in the text.…”

Section: Methodsmentioning

confidence: 99%

Small leucine-rich repeat proteoglycans associated with mature insoluble elastin serve as binding sites for galectins

Itoh

Nonaka

Ogawa

et al. 2017

Bioscience, Biotechnology, and Biochemistry

View full text Add to dashboard Cite

We previously reported that galectin-9 (Gal-9), an immunomodulatory animal lectin, could bind to insoluble collagen preparations and exerted direct cytocidal effects on immune cells. In the present study, we found that mature insoluble elastin is capable of binding Gal-9 and other members of the human galectin family. Lectin blot analysis of a series of commercial water-soluble elastin preparations, PES-(A) ~ PES-(E), revealed that only PES-(E) contained substances recognized by Gal-9. Gal-9-interacting substances in PES-(E) were affinity-purified, digested with trypsin and then analyzed by reversed-phase HPLC. Peptide fragments derived from five members of the small leucine-rich repeat proteoglycan family, versican, lumican, osteoglycin/mimecan, prolargin, and fibromodulin, were identified by N-terminal amino acid sequence analysis. The results indicate that Gal-9 and possibly other galectins recognize glycans attached to small leucine-rich repeat proteoglycans associated with insoluble elastin and also indicate the possibility that mature insoluble elastin serves as an extracellular reservoir for galectins.

show abstract

“…One interesting group of elastin-based biomaterials are elastinlike polymers (ELPs) and, especially, their recombinant versions (ELRs). These are protein-like materials whose composition is based on the repetition of conserved motifs found in the hydrophobic domains of native tropoelastin (Foster et al, 1973). Both ELPs and ELRs refer to the same kind of polypeptide, with differences in the production process.…”

Section: Elastin-like Recombinamers (Elrs)mentioning

confidence: 99%

Fibrous Scaffolds From Elastin-Based Materials

Rodríguez‐Cabello

Torre

González-Pérez

et al. 2021

Front. Bioeng. Biotechnol.

View full text Add to dashboard Cite

Current cutting-edge strategies in biomaterials science are focused on mimicking the design of natural systems which, over millions of years, have evolved to exhibit extraordinary properties. Based on this premise, one of the most challenging tasks is to imitate the natural extracellular matrix (ECM), due to its ubiquitous character and its crucial role in tissue integrity. The anisotropic fibrillar architecture of the ECM has been reported to have a significant influence on cell behaviour and function. A new paradigm that pivots around the idea of incorporating biomechanical and biomolecular cues into the design of biomaterials and systems for biomedical applications has emerged in recent years. Indeed, current trends in materials science address the development of innovative biomaterials that include the dynamics, biochemistry and structural features of the native ECM. In this context, one of the most actively studied biomaterials for tissue engineering and regenerative medicine applications are nanofiber-based scaffolds. Herein we provide a broad overview of the current status, challenges, manufacturing methods and applications of nanofibers based on elastin-based materials. Starting from an introduction to elastin as an inspiring fibrous protein, as well as to the natural and synthetic elastin-based biomaterials employed to meet the challenge of developing ECM-mimicking nanofibrous-based scaffolds, this review will follow with a description of the leading strategies currently employed in nanofibrous systems production, which in the case of elastin-based materials are mainly focused on supramolecular self-assembly mechanisms and the use of advanced manufacturing technologies. Thus, we will explore the tendency of elastin-based materials to form intrinsic fibers, and the self-assembly mechanisms involved. We will describe the function and self-assembly mechanisms of silk-like motifs, antimicrobial peptides and leucine zippers when incorporated into the backbone of the elastin-based biomaterial. Advanced polymer-processing technologies, such as electrospinning and additive manufacturing, as well as their specific features, will be presented and reviewed for the specific case of elastin-based nanofiber manufacture. Finally, we will present our perspectives and outlook on the current challenges facing the development of nanofibrous ECM-mimicking scaffolds based on elastin and elastin-like biomaterials, as well as future trends in nanofabrication and applications.

show abstract

Isolation and Amino Acid Sequences of Tropoelastin Peptides

Cited by 260 publications

References 16 publications

Val-Gly-Val-Ala-Pro-Gly, a repeating peptide in elastin, is chemotactic for fibroblasts and monocytes.

Val-Gly-Val-Ala-Pro-Gly, a repeating peptide in elastin, is chemotactic for fibroblasts and monocytes.

Small leucine-rich repeat proteoglycans associated with mature insoluble elastin serve as binding sites for galectins

Fibrous Scaffolds From Elastin-Based Materials

Contact Info

Product

Resources

About