Sequence Variation of Bovine Elastin mRNA Due to Alternative Splicing

Yeh, Helena; Ornstein‐Goldstein, Norma; Indik, Zena K.; Sheppard, Paul O.; Anderson, Noel; Rosenbloom, J.; Cicila, George T.; Yoon, Kyung-Chul; Rosenbloom, Joel

doi:10.1016/s0174-173x(87)80030-4

Cited by 149 publications

(51 citation statements)

References 35 publications

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“…Posttranslational modifications and alternative splicings are therefore not taken into account. 24,25 elastin. 17 Figure 5 shows that elastin was present homogeneously in elastin fibers purified according to method C. Yields for the different purification procedures (A, B, and C) were similar and were, on a dry weight basis, 21, 20, and 22% respectively, of the original ligament.…”

Section: Intact Elastin Fibers Devoid Of Microfibrilsmentioning

confidence: 99%

Isolation of Intact Elastin Fibers Devoid of Microfibrils

et al. 2005

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Purification protocols for elastin generally result in greatly damaged elastin fibers and this likely influences the biological response. We here describe a novel protocol for the isolation of elastin whereby the fibers stay intact, and introduce the term "elastin fiber" for intact elastic fibers with elastin as their sole component. As opposed to elastic fibers, elastin fibers do not contain any microfibrils or associated molecules. Elastin fibers were isolated from equine elastic ligaments according to various protocols and analyzed by sodium dodecyl sulfate polyacrylamide gel electrophoresis, amino acid quantification, immunofluorescence assay, transmission/scanning electron microscopy, and cellular reactivity in vivo. The optimal protocol comprised several extraction steps and trypsin digestion. Elastin fibers were free of contaminants and had a smooth, regular appearance. The cellular response to purified, intact elastin fibers was different in comparison with purified, but affected, fibers and to contaminated fibers. Intact fibers consisting only of elastin may be important for both fundamental and applied research, for example, tissue engineering, which need well-defined preparations to study the cellular biological effect of individual components.

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Section: Intact Elastin Fibers Devoid Of Microfibrilsmentioning

confidence: 99%

Isolation of Intact Elastin Fibers Devoid of Microfibrils

et al. 2005

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“…In bovine tropoelastin, it repeats twice, and in human tropoelastin, it repeats six times (37). Since the synthetic peptide reflecting VGVAPG sequence proved so efficient in stimulation of pro-MMP-1 production (Fig.…”

Section: Figmentioning

confidence: 99%

Conformational Dependence of Collagenase (Matrix Metalloproteinase-1) Up-regulation by Elastin Peptides in Cultured Fibroblasts

Brassart¹,

Fuchs²,

Huet³

et al. 2001

Journal of Biological Chemistry

155

147

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We have established that treatment of cultured human skin fibroblasts with tropoelastin or with heterogenic peptides, obtained after organo-alkaline or leukocyte elastase hydrolysis of insoluble elastin, induces a high expression of pro-collagenase-1 (pro-matrix metalloproteinase-1 (pro-MMP-1)). The identical effect was achieved after stimulation with a VGVAPG synthetic peptide, reflecting the elastin-derived domain known to bind to the 67-kDa elastin-binding protein. This clearly indicated involvement of this receptor in the described phenomenon. This notion was further reinforced by the fact that elastin peptides-dependent MMP-1 up-regulation has not been demonstrated in cultures preincubated with 1 mM lactose, which causes shedding of the elastin-binding protein and with pertussis toxin, which blocks the elastin-binding protein-dependent signaling pathway involving G protein, phospholipase C, and protein kinase C. Moreover, we demonstrated that diverse peptides maintaining GXXPG sequences can also induce similar cellular effects as a "principal" VGVAPG ligand of the elastin receptor. Results of our biophysical studies suggest that this peculiar consensus sequence stabilizes a type VIII ␤-turn in several similar, but not identical, peptides that maintain a sufficient conformation to be recognized by the elastin receptor. We have also established that GXXPG elastin-derived peptides, in addition to pro-MMP-1, cause up-regulation of pro-matrix metalloproteinase-3 (pro-stromelysin 1). Furthermore, we found that the presence of plasmin in the culture medium activated these MMP proenzymes, leading to a consequent degradation of collagen substrate. Our results may be, therefore, relevant to pathobiology of inflammation, in which elastin-derived peptides bearing the GXXPG conformation (created after leukocyte-dependent proteolysis) bind to the elastin receptor of local fibroblasts and trigger signals leading to expression and activation of MMP-1 and MMP-3, which in turn exacerbate local connective tissue damage.The extracellular matrix protein elastin is responsible for the elastic properties of tissues such as lung, skin, and large arteries (1-3). Due to its numerous cross-links and the extreme hydrophobicity of its tropoelastin chains, elastin is highly resistant to proteolysis. However, during inflammatory disorders, proteinases secreted from polymorphonuclear neutrophils, such as elastase, cathepsin G, and gelatinase B may cause significant elastolysis (4).It has been established that peptides derived from elastin or from the hydrophobic domains of tropoelastin interact with cells via a cell surface-resided 67-kDa elastin-binding protein identical to an enzymatically inactive, alternatively spliced form of ␤-galactosidase (5). The binding of elastin peptides to the elastin-binding protein (EBP) 1 has been shown to be responsible for chemotaxis to the peptides (6 -12), stimulation of cell proliferation (13-16), ions flux modifications (17, 18), vasorelaxation (19 -22), and enzymes secretion (23,24).Matrix metall...

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“…The primary structure of BTE 1 (3,4) consists of an alternance of cross-linking regions, where the lysyl residues are located, and of large hydrophobic domains responsible for elastin elasticity. The highly hydrophobic BTE molecule possesses a very basic C-terminal sequence where its only two Cys residues are located.…”

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confidence: 99%

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

Debelle

Alix

Jacob

et al. 1995

Journal of Biological Chemistry

109

104

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Elastin is the macromolecular polymer of tropoelastin molecules responsible for the elastic properties of tissues. The understanding of its specific elasticity is uncertain because its structure is still unknown. Here, we report the first experimental quantitative determination of bovine elastin secondary structures as well as those of its corresponding soluble -elastin. Using circular dichroism and Fourier transform infrared and near infrared Fourier transform Raman spectroscopic data, we estimated the secondary structure contents of elastin to be ϳ10% ␣-helices, ϳ45% ␤-sheets, and ϳ45% undefined conformations. These values were very close to those we had previously determined for the free monomeric tropoelastin molecule, suggesting thus that elastin would be constituted of a closely packed assembly of globular ␤ structural class tropoelastin molecules crosslinked to form the elastic network (liquid drop model of elastin architecture). The presence of a strong hydration shell is demonstrated for elastin, and its possible contribution to elasticity is discussed.

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Sequence Variation of Bovine Elastin mRNA Due to Alternative Splicing

Cited by 149 publications

References 35 publications

Isolation of Intact Elastin Fibers Devoid of Microfibrils

Isolation of Intact Elastin Fibers Devoid of Microfibrils

Conformational Dependence of Collagenase (Matrix Metalloproteinase-1) Up-regulation by Elastin Peptides in Cultured Fibroblasts

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

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