Emilin, a component of elastic fibers preferentially located at the elastin-microfibrils interface.

Bressan, Giorgio M.; Daga-Gordini, D.; Colombatti, Alfonso; Castellani, I.; Marigo, Valeria; Volpin, Dino

doi:10.1083/jcb.121.1.201

Cited by 150 publications

(125 citation statements)

References 26 publications

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“…Nevertheless, we found that the FB1 epitope is localized immunoelectron-microscopically in the bundles of subectodermal microfibrils, and that the electrophoretic mobility and immunohistochemical distribution of the FB1 antigen are indistinguishable from those of JB3 antigen, or chicken fibrillin-2 Rongish et al, 1998). The spatial pattern of the fibers demonstrated in this study also overlaps in part the pattern of elastin immunoreactivity in the limb bud (Hurle et al, 1994;Ros et al, 1995;Hurle and Colombatti, 1996), but appears to be more comparable to the pattern of emilin (Hurle and Colombatti, 1996), which is known to be localized in the elastin-microfibril interface (Bressan et al, 1993). On the basis of these and other findings in this study, we discuss the functional and developmental significance of a parallel spatial array of extracellular subectodermal microfibrils.…”

supporting

confidence: 61%

Subectodermal microfibrillar bundles are organized into a distinct parallel array in the developing chick limb bud

et al. 2004

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In this study, a unique fiber system in the subectodermal mesenchyme of the chick limb bud was visualized immunohistochemically with the use of a novel monoclonal antibody termed "FB1." This antibody stained a subset of extracellular fibers in the embryonic mesenchyme. Among the fibers visualized, those running perpendicularly to the limb bud ectoderm became progressively prominent in their thickness and length, and organized into a parallel array in the subectodermal region. This fiber system was distinct from that of major collagens, fibronectin, or tenascin. A molecule immunoprecipitated with FB1 comigrated with JB3 antigen, or chicken fibrillin-2. The fibers visualized immunohistochemically by FB1 and JB3 were indistinguishable from each other, and ultrastructurally appeared to be bundles composed of tubular-like microfibrils that originated directly from the ectodermal basal lamina. They lacked the amorphous deposits that are characteristic of elastin. A similar array of subectodermal fibers was also found in the developing axilla and some truncal regions, again well before the development of a definitive dermis. These findings suggest that a parallel array of subectodermal FB1-positive fibers constitutes a precocious fiber system in the presumptive dermis prior to the substantial formation of collagenous fibers. These fibers could be developmentally linked to oxytalan fibers, which are known to be present in the papillary dermis in mature cutaneous tissue.

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confidence: 61%

Subectodermal microfibrillar bundles are organized into a distinct parallel array in the developing chick limb bud

et al. 2004

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“…By combining immunolabeling of specific elastic components with the use of whole-mount specimens we were able to discern important features undetected in previous studies of the heart extracellular matrix. We found that the valvular leaflets contain all the elastic components described in studies of other typical elastic fetal or adult tissues (Sakai et al, 1986;Bressan et al, 1993) including elastin, fibrillin, emilin, and collagen type VI, a component not always associated with elastic matrices (Knight et al, 1984;Sakai et al, 1986). Each of these components exhibited a fibrillar pattern in the atrioventricular valve leaflets oriented in the direction of the blood flow.…”

Section: Third Periodmentioning

confidence: 73%

“…The most characteristic feature of this period is the formation of a prominent elastic layer in the wall of the outflow tract of the heart. This elastic matrix contains primarily elastin, and is associated with fibrillin and emilin as observed in several fetal and adult elastic matrices (Sakai et al, 1986;Bressan et al, 1993), but appears to lack collagen type VI. The presence of elastin in the heart at these stages has been previously reported by Rosenquist et a1 (1988).…”

Section: Second Periodmentioning

confidence: 85%

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Elastic extracellular matrix of the embryonic chick heart: An immunohistological study using laser confocal microscopy

Hurlé

Kitten

Sakai

et al. 1994

Developmental Dynamics

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The "elastic matrix" constitutes a specialized component of the extracellular matrix which confers resiliency to tissues and organs subjected to repeated deformations. The role of the elastic matrix in living organisms appears to be of key importance since diseases characterized by expression of defective inherited genes which encode components of the elastic matrix lead to premature death. While the elastic matrix of adult organs has received a great deal of attention, little is known about when it first appears in embryonic tissues or its possible role in developing organs. In the present study we have performed an immunohistochemical study of the distribution of elastin and three additional components often associated with elastic matrices in adult tissues (i.e., fibrillin, emilin, and type VI collagen) during the development of the chicken embryonic heart. The threedimensional arrangement of these components was established through the observation of wholemount specimens with scanning laser confocal microscopy. Our results revealed three different periods of heart development regarding the composition of the elastic matrix. Prior to stage 21 the embryonic heart lacks elastin but exhibits a matrix scaffold of fibrillin and emilin associated with the endocardium and the developing cardiac jelly. Between stages 22 and 29 the heart shows a transient elastic scaffold in the outflow tract which contains elastin, fibrillin, and emilin. Elastin-positive fibrillar material is also observed during these stages in the base of the atrioventricular cushion adjacent to the myocardial wall. In addition, emilin-positive material appears to be associated with the zones of formation of ventricular trabeculae. Collagen type VI was not detected during these early stages. From stage 30 to stage 40 a progressive modification of the pattern of distribution of elastin, fibrillin, emilin, and collagen type VI is observed in association with the formation of the definitive four-chambered heart. The distribution of the elastic scaffold in the outflow tract appears to be rearranged and becomes restricted to the roots of the main arteries. Each of the components studied here is also deposited at increasing levels in the developing valvular appa-ratus including the valve leaflets and the chordae tendinea. The components are also present in the subendocardial space where they form aligned fibrillar tracts, an arrangement suggestive of a role in ventricular contractile function. The epicardium constitutes an additional region of elastic matrix deposition during these later stages and contains elastic, fibrillin, and collagen type VI. Finally, during the later stages the intramyocardial matrix (''myocardial interstitium") is formed and characterized by an abundance of collagen type VI, emilin, and fibrillin but lacks elastin-positive material. This study suggests that during cardiac development there is not a fixed composition of the so-called "elastic matrix.'' Rather, combinations of the different components of the elastic matrice...

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“…As the name suggests, EMILIN-1 is found in elastin-rich tissues and is localized to the interface between amorphous elastin and microfibrils. Anti-EMILIN-1 antibodies promote the formation of elastin aggregates rather than fibers in SMC cultures (Bressan et al, 1993). EMILIN-1 binds elastin in solid-phase binding assays and both elastin and fibulin-5 in immunoprecipitation assays (Zanetti et al, 2004).…”

Section: Elastin Microfibril Interface Located Protein (Emilin)-1mentioning

confidence: 99%

New insights into elastic fiber assembly

Wagenseil

Mecham

2007

Birth Defects Research Pt C

355

354

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Elastic fibers provide recoil to tissues that undergo repeated stretch, such as the large arteries and lung. These large extracellular matrix (ECM) structures contain numerous components, and our understanding of elastic fiber assembly is changing as we learn more about the various molecules associated with the assembly process. The main components of elastic fibers are elastin and microfibrils. Elastin makes up the bulk of the mature fiber and is encoded by a single gene. Microfibrils consist mainly of fibrillin, but also contain or associate with proteins such as microfibril associated glycoproteins (MAGPs), fibulins, and EMILIN-1. Microfibrils were thought to facilitate alignment of elastin monomers prior to cross-linking by lysyl oxidase (LOX). We now know that their role, as well as the overall assembly process, is more complex. Elastic fiber formation involves elaborate spatial and temporal regulation of all of the involved proteins and is difficult to recapitulate in adult tissues. This report summarizes the known interactions between elastin and the microfibrillar proteins and their role in elastic fiber assembly based on in vitro studies and evidence from knockout mice. We also propose a model of elastic fiber assembly based on the current data that incorporates interactions between elastin, LOXs, fibulins and the microfibril, as well as the pivotal role played by cells in structuring the final functional fiber. Birth Defects Research (Part C) 81:229-240,

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Emilin, a component of elastic fibers preferentially located at the elastin-microfibrils interface.

Cited by 150 publications

References 26 publications

Subectodermal microfibrillar bundles are organized into a distinct parallel array in the developing chick limb bud

Subectodermal microfibrillar bundles are organized into a distinct parallel array in the developing chick limb bud

Elastic extracellular matrix of the embryonic chick heart: An immunohistological study using laser confocal microscopy

New insights into elastic fiber assembly

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