Bovine Elastin and κ-Elastin Secondary Structure Determination by Optical Spectroscopies

Debelle, Laurent; Alix, Alain J. P.; Jacob, Marie‐Paule; Huvenne, J.P.; Berjot, M.; Sombret, B.; Legrand, Pierre

doi:10.1074/jbc.270.44.26099

Cited by 108 publications

(118 citation statements)

References 41 publications

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“…2. The major peaks have been labeled with the appropriate wave number, and the structural features to which they correspond are detailed in Tables I and II (12,(15)(16)(17)(18). The spectra of the native and relaxed tissue showed a high degree of homology to each other.…”

Section: Resultsmentioning

confidence: 99%

Raman Microscopy and X-ray Diffraction, a Combined Study of Fibrillin-rich Microfibrillar Elasticity

Haston

Engelsen²,

Roessle

et al. 2003

Journal of Biological Chemistry

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Fibrillin-rich microfibrils are essential elastic structures contained within the extracellular matrix of a wide variety of connective tissues. Microfibrils are characterized as beaded filamentous structures with a variable axial periodicity (average 56 nm in the untensioned state); however, the basis of their elasticity remains unknown. This study used a combination of small angle x-ray scattering and Raman microscopy to investigate further the packing of microfibrils within the intact tissue and to determine the role of molecular reorganization in the elasticity of these microfibrils. The application of relatively small strains produced no overall change in either molecular or macromolecular microfibrillar structure. In contrast, the application of larger tissue extensions (up to 150%) resulted in a markedly different structure, as observed by both Raman microscopy and small angle x-ray scattering. These changes occurred at different levels of architecture and are interpreted as ranging from alterations in peptide bond conformation to domain rearrangement. This study demonstrates the importance of molecular elasticity in the mechanical properties of fibrillin-rich microfibrils in the intact tissue.

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Section: Resultsmentioning

confidence: 99%

Raman Microscopy and X-ray Diffraction, a Combined Study of Fibrillin-rich Microfibrillar Elasticity

Haston

Engelsen²,

Roessle

et al. 2003

Journal of Biological Chemistry

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“…The Amide I band decomposition exhibits some modifications according to the tissue type. It has been previously reported that two different types of beta sheet structure are present at 1629 cm À1 and 1635 cm À1 in tropoelastin [21]. For aneurismal tissues, the most important modification observed is a decrease of beta sheet structures present at 1635 cm…”

mentioning

confidence: 92%

“…The number and frequency position of these peaks seem to match with the secondary structure components observed in previous studies based on pure elastin. The study based on tropoelastin [21] was used to assign the second derivative peaks and bands positions for the curve-fitting procedure. The observed decomposition of FTIR spectra from aortic tissues and elastin were very similar, probably because the media contains a high proportion of elastin.…”

mentioning

confidence: 99%

FTIR protein secondary structure analysis of human ascending aortic tissues

Bonnier

Rubin

Debelle

et al. 2008

Journal of Biophotonics

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Journal of BIOPHOTONICSThe advent of moderate dilatations in ascending aortas is often accompanied by structural modifications of the main components of the aortic tissue, elastin and collagen. In this study, we have undertaken an approach based on FTIR microscopy coupled to a curve-fitting procedure to analyze secondary structure modifications in these proteins in human normal and pathological aortic tissues. We found that the outcome of the aortic pathology is strongly influenced by these proteins, which are abundant in the media of the aortic wall, and that the advent of an aortic dilatation is generally accompanied by a decrease of parallel b-sheet structures. Elastin, essentially composed of b-sheet structures, seems to be directly related to these changes and therefore indicative of the elastic alteration of the aortic wall. Conventional microscopy and confocal fluorescence microscopy were used to compare FTIR microscopy results with the organization of the elastic fibers present in the tissues. This in-vitro study on 6 patients (three normal and three pathologic), suggests that such a spectroscopic marker, specific to aneurismal tissue characterization, could be important information for surgeons who face the dilemma of moderate aortic tissue dilatation of the ascending aortas.Infrared spectroscopy and imaging was applied to analyse Human thoracic ascending aortas with the aim to highlight the protein secondary structure reorganisation after an aneurism outcome. We used a curve-fitting procedure to visualise modifications in the protein spectral profile where alteration of b structures in pathological aortas could be detected. Our spectroscopic observations on tissue sections corroborated with confocal fluorescence microscopy clearly demonstrating that elastic fibres of aortic wall are strongly altered. Elastin appears as the privileged target during the pathological process.

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“…Soluble elastin peptides were obtained from insoluble elastin by organo-alkaline hydrolysis. This was achieved using 1 M KOH in 80% aqueous ethanol (36). The obtained mixture of elastin peptides is termed -elastin (kE) and exhibits the same biological and physical properties as elastin hydrolysates (5).…”

Section: Methodsmentioning

confidence: 99%

The Elastin Receptor Complex Transduces Signals through the Catalytic Activity of Its Neu-1 Subunit

Duca

Blanchevoye

Cantarelli

et al. 2007

Journal of Biological Chemistry

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The binding of elastin peptides on the elastin receptor complex leads to the formation of intracellular signals but how this is achieved remains totally unknown. Using pharmacological inhibitors of the enzymatic activities of its subunits, we show here that the elastin peptide-driven ERK1/2 activation and subsequent pro-MMP-1 production, observed in skin fibroblasts when they are cultured in the presence of these peptides, rely on a membrane-bound sialidase activity. As lactose blocked this effect, the elastin receptor sialidase subunit, Neu-1, seemed to be involved. The use of a catalytically inactive form of Neu-1 and the small interfering RNA-mediated decrease of Neu-1 expression strongly support this view. Finally, we report that N-acetyl neuraminic acid can reproduce the effects of elastin peptides on both ERK1/2 activation and pro-MMP-1 production. Altogether, our results indicate that the enzymatic activity of the Neu-1 subunit of the elastin receptor complex is responsible for its signal transduction, presumably through sialic acid generation from undetermined substrates.Elastin is the extracellular matrix protein responsible for the elasticity of tissues. It is more abundant in tissues where resilience is required, such as skin, lung, ligaments, or large arteries (1). Elastin is constituted of tropoelastin molecules covalently bound to each other by covalent cross-links (2) and its hydrophobic and highly cross-linked nature make of it a very durable polymer experiencing essentially no turnover in healthy tissues (3).The biological role of elastin was originally thought to be restricted to this mechanical function. However, when Senior et al. (4) demonstrated that elastin digestion products were chemotactic for neutrophils and macrophages, it became suddenly apparent that peptides derived from amorphous elastin could modulate cell physiology. In fact, it has been shown because that fibroblasts (5-12), smooth muscle cells (7, 13-15), endothelial cells (16 -19), leukocytes (20, 21), and lymphocytes (22) were sensitive to the presence of these peptides yielding a broad range of biological activities (see Ref. 23 for a review). A corollary of these observations was that those cells do express a receptor for elastin peptides.The elastin receptor complex is constituted of three subunits, one peripheral 67-kDa subunit, which actually binds elastin, and two membrane-associated proteins of 61 and 55 kDa, respectively (10). The 67-kDa elastin-binding protein (EBP) 2 binds the VGVAPG elastin sequence with high affinity. Additionally, EBP can be eluted from elastin affinity column by galactosugars suggesting that the elastin-EBP interaction could be regulated by galactosugars bound on a lectin site on EBP (10, 24). Consequently, galactosugars such as lactose are commonly used antagonists of EBP.Later, the nature of this subunit was revealed by the work of Privitera et al. (25) who have shown that EBP is an enzymatically spliced variant of lysosomal ␤-galactosidase (␤-Gal, EC 3.2.1.23). Consequently, it was hypot...

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Bovine Elastin and κ-Elastin Secondary Structure Determination by Optical Spectroscopies

Cited by 108 publications

References 41 publications

Raman Microscopy and X-ray Diffraction, a Combined Study of Fibrillin-rich Microfibrillar Elasticity

Raman Microscopy and X-ray Diffraction, a Combined Study of Fibrillin-rich Microfibrillar Elasticity

FTIR protein secondary structure analysis of human ascending aortic tissues

The Elastin Receptor Complex Transduces Signals through the Catalytic Activity of Its Neu-1 Subunit

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