The Elastin Receptor: A Galactoside-Binding Protein
25 Mar 1988-Science (American Association for the Advancement of Science)-Vol. 239, Iss: 4847, pp 1539-1541
TL;DR: The elastin receptor complex contains a component of 67 kilodaltons that binds to a glycoconjugate affinity column containing beta-galactoside residues and is eluted from this column with lactose.
Abstract: The elastin receptor complex contains a component of 67 kilodaltons that binds to a glycoconjugate affinity column containing beta-galactoside residues and is eluted from this column with lactose. This protein component is also released from the surface of cultured chondroblasts by incubation with lactose, and its association with immobilized elastin is inhibited by lactose. Since lactose also blocks elastic fiber formation by cultured chondroblasts, the galactoside-binding property of the elastin receptor is implicated in this process.
Citations
More filters
TL;DR: Describing de 2 categories de lectines animales: les lectines de type C, calcium-dependantes et les lectine de type S, thiol-dependante.
1,241Â citations
TL;DR: By correlating vessel mechanics with physiological blood pressure across animal species and in mice with altered vessel compliance, it is shown that cardiac and vascular development are physiologically coupled, and there is evidence for a universal elastic modulus that controls the parameters of ECM deposition in vessel wall development.
Abstract: An important factor in the transition from an open to a closed circulatory system was a change in vessel wall structure and composition that enabled the large arteries to store and release energy during the cardiac cycle. The component of the arterial wall in vertebrates that accounts for these properties is the elastic fiber network organized by medial smooth muscle. Beginning with the onset of pulsatile blood flow in the developing aorta, smooth muscle cells in the vessel wall produce a complex extracellular matrix (ECM) that will ultimately define the mechanical properties that are critical for proper function of the adult vascular system. This review discusses the structural ECM proteins in the vertebrate aortic wall and will explore how the choice of ECM components has changed through evolution as the cardiovascular system became more advanced and pulse pressure increased. By correlating vessel mechanics with physiological blood pressure across animal species and in mice with altered vessel compliance, we show that cardiac and vascular development are physiologically coupled, and we provide evidence for a universal elastic modulus that controls the parameters of ECM deposition in vessel wall development. We also discuss mechanical models that can be used to design better tissue-engineered vessels and to test the efficacy of clinical treatments.
865Â citations
Cites background from "The Elastin Receptor: A Galactoside..."
...Interestingly, in vascular injury models, high versican levels correlate with low elastin content, most likely due to inhibition of elastic fiber assembly by the chondroitin sulfate GAGs on versican (105, 117)....
[...]
Patentâ˘
17 Jan 2002
TL;DR: In this paper, binding domain-immunoglobulin fusion proteins are defined as proteins that feature a binding domain for a cognate structure such as an antigen, a counterreceptor or the like, and can be recombinantly produced at high expression levels.
Abstract: The invention relates to novel binding domain-immunoglobulin fusion proteins that feature a binding domain for a cognate structure such as an antigen, a counterreceptor or the like, a hinge region polypeptide having either zero or one cysteine residue, and immunoglobulin CH2 and CH3 domains, and that are capable of ADCC and/or CDC while occurring predominantly as monomeric polypeptides. The fusion proteins can be recombinantly produced at high expression levels. Also provided are related compositions and methods, including immunotherapeutic applications.
683Â citations
665Â citations
TL;DR: Analysis of the elastin gene has demonstrated that hydrophobic and crossâlinking domains are encoded in separate exons and that there is significant alternative splicing, resulting in multiple isoforms of tropoelastin.
Abstract: The elastic properties of many tissues such as the lung, dermis, and large blood vessels are due to the presence of elastic fibers in the extracellular space. These fibers have been shown by biochemical and ultrastructural analysis to be composed of two distinct components, a more abundant amorphous component and a 10-12 nm microfibrillar component, which is located primarily around the periphery of the amorphous component. The protein elastin makes up the highly insoluble amorphous component and is responsible for the elastic properties. Elastin is found throughout the vertebrate kingdom and possesses an unusual chemical composition rich in glycine, proline, and hydrophobic amino acids, consonant with its characteristic physical properties. The 72-kDa biosynthetic precursor, tropoelastin, is secreted into the extracellular space where it becomes highly cross-linked into a rubber-like network through the activity of the copper-requiring enzyme lysyl oxidase. Analysis of the elastin gene has demonstrated that hydrophobic and cross-linking domains are encoded in separate exons and that there is significant alternative splicing, resulting in multiple isoforms of tropoelastin. The elastin gene promoter contains many potential binding sites for various modulating factors indicative of a complex pattern of transcriptional regulation. The microfibrils contain several proteins, including fibrillin, and probably act as an organizing scaffold in the formation of the elastin network. There appears to be a fibrillin gene family in which each protein contains multiple repeats of a motif previously found in epidermal growth factor and a second motif observed in transforming growth factor beta 1-binding protein. Mutations in the fibrillin gene located on human chromosome 15 have been strongly implicated as the cause of the Marfan syndrome.
603Â citations
References
More filters
TL;DR: Interactions between the lectins and glycoconjugates appear to play a role in shaping extracellular environments, as in mucin or slime.
Abstract: Soluble lectins of cellular slime molds and vertebrates are present at extracellular sites in the developing or adult tissues that make them. Some lectins are concentrated around cell groups, as in extracellular matrix or elastic fibers. Others are at the interface between cells and the external environment, as in mucin or slime. Specific glycoproteins, proteoglycans, or polysaccharides that bind these endogenous lectins may also be present at these sites. Interactions between the lectins and glycoconjugates appear to play a role in shaping extracellular environments.
401Â citations
TL;DR: These studies suggest that small synthetic peptides may be able to reproduce the chemotactic activity associated with elastin- derived peptides and tropoelastin.
Abstract: 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 Val-Gly-Val-Ala-Pro-Gly (VGVAPG), a repeating peptide in tropoelastin. We observed that VGVAPG was chemotactic for fibroblasts and monocytes, with optimal activity at approximately 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-leucyl-phenylalanine 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.
377Â citations
01 Jan 1983
267Â citations
TL;DR: The results indicate that discoidin I functions like fibronectin to promote cell attachment and spreading as well as ordered cellular migration during morphogenesis.
181Â citations
TL;DR: The alignment of amino acid sequences of porcine tropoelastin tryptic peptides with the sequence for bovine elastin a results in the ordering of these tryptic amino acid peptides.
156Â citations