Elastin

Franzblau, Carl; Faris, Barbara

doi:10.1007/978-1-4613-0881-2_4

Cited by 15 publications

(12 citation statements)

References 74 publications

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“…The formation of insoluble proteins depends on the composition of the connective tissue matrix. For example, GAGs help to position elastin precursors for appropriate cross‐linking and formation of elastin fibers (Franzblau and Faris, 1981). Special GAG composition in the bulbus of C. hamatus could block this cross‐linking and prevent formation of the elastic fibers.…”

Section: Discussionmentioning

confidence: 99%

“…Special GAG composition in the bulbus of C. hamatus could block this cross‐linking and prevent formation of the elastic fibers. On the other hand, the amorphous material that accumulates at the transition between the bulbus and the ventral aorta resembles ultrastructurally (Franzblau and Faris, 1981) elastin or elastin‐like matrix. Thus, we favor the later hypothesis.…”

Section: Discussionmentioning

confidence: 99%

“…Smooth muscle cells synthesize, besides elastin and collagen, glycoproteins, and glycosaminoglycans (GAGs; Franzblau and Faris, 1981). The relative amount of each synthesized component depends on the system studied.…”

Section: Discussionmentioning

confidence: 99%

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Bulbus arteriosus of the antarctic teleosts. I. The white-bloodedChionodraco hamatus

et al. 1999

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The bulbus arteriosus of teleost fish is a thick-walled chamber that extends between the single ventricle and the ventral aorta. The functional importance of the bulbus resides in the fact that it maintains a steady blood flow into the gill system through heart contraction. Despite of this, a thorough study of the structure of the bulbus in teleost fish is still lacking. We have undertaken a morphologic study of the bulbus arteriosus in the stenothermal teleosts of the Antarctic sea. The structural organization of the bulbus arteriosus of the icefish Chionodraco hamatus has been studied here by conventional light, scanning, and transmission electron microscopy.The inner surface of the bulbus shows a festooned appearance due to the presence of longitudinal, unbranched ridges that extend between the ventricle and the arterial trunk. The wall of the bulbus is divided into endocardial, subendocardial, middle, and external layers. Endocardial cells show a large number of moderately-dense bodies. The endocardium invaginates into the subendocardium forming solid epithelial cords that contain numerous secretory vacuoles. Cells in the subendocardium group into small domains, have some of the morphological characteristics of smooth muscle cells, and appear enmeshed in a three-dimensional network of matrix filaments. Cells in the middle layer are typical smooth muscle cells. They appear arranged into layers and are surrounded by a filamentous meshwork that excludes collagen fibers. Orientation of this meshwork occurs in the vicinity of the smooth muscle cells. Elastin fibers are never observed. The external layer is formed by wavy collagen bundles and fibroblast-like cells. This layer lacks blood vessels and nerve fibers.The endocardium and the endocardium-derived cords are secretory epithelia that may be involved in the formation of mucins or glycosaminoglycans. These mucins may have a protecting effect on the endocardium. The subendocardium and the middle layer appear to be formed by the same cell type, smooth muscle, with a gradient of differentiation from the secretory (subendocardium) to the contractile (middle layer) phenotype. Despite the absence of elastin fibers, the filamentous matrix could maintain the elastic properties of the bulbus wall. Smooth muscle cells appear to be actively involved in bulbus wall dynamics. The restriction of collagen to the external layer suggests that it may control wall dilatation and bulbus compliance.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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Bulbus arteriosus of the antarctic teleosts. I. The white-bloodedChionodraco hamatus

et al. 1999

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“…Elastin is secreted from the cell as a soluble monomer (tropoelastin) that must be cross-linked into a functional polymer (9). The first step in the cross-linking reaction is the formation of the ␦-aldehyde allysine through oxidation of lysyl ⑀-amino groups by a member of the lysyl oxidase enzyme family (10).…”

Section: Tropoelastinmentioning

confidence: 99%

The Stumbling Block in Lung Repair of Emphysema: Elastic Fiber Assembly

Shifren¹

2006

Proceedings of the American Thoracic Society

126

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The mechanical properties of the lung are largely determined by the connective tissue networks laid down during development. The macromolecules most important for lung mechanics and structural integrity are collagen, elastin, and proteoglycans. Members of the fibrillar collagen gene family provide the structural framework of the various lung compartments and elastic fibers provide elastic recoil. Elastin is also an important architectural component that influences lung development, predominantly during the alveolar stage. Previous studies have conclusively shown that elastin degradation is a key step in the pathogenesis of chronic obstructive pulmonary disease. Exacerbating the disease process is the inability of lung cells to repair damaged elastic fibers, which leads to permanently compromised lung function and ongoing degenerative disease. Elastic fibers are among the most difficult matrix structures to repair because of their size, molecular complexity, and the requirement for numerous helper proteins to facilitate fiber assembly. Recent studies of elastin assembly combined with new insight into the functional role of elastic fiber proteins obtained from gene inactivation studies and linkage of human disease to elastin mutations provide new insight into the molecular and cellular complexities of elastin homeostasis.

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“…Elastases are a diverse group of endopeptidases that are active at neutral pH towards most connective tissue components, including elastin (Ross and Bornstein, 1967;Franzblau and Faris, 1981), type IV and V collagens (Davies et al, 1978), proteoglycans (Keiser et al, 1976;Bartholomew et al, 1984), and fibronectin (McDonald et al, 1979;McDonald and Kelley, 1980). The broad substrate specificity of elastases and their activity at neutral pH endows them with great potential for causing extracellular damage.…”

mentioning

confidence: 99%

Binding sites for elastase on cultured human fibroblasts that do not mediate internalization

Campbell

Cunningham

1987

Journal Cellular Physiology

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The proteolytic actions of elastases have been implicated in extracellular matrix damage, which is characteristic of a variety of pathological conditions including emphysema and rheumatoid arthritis. In order to elucidate the molecular events involved in elastase interaction with connective tissue cells, the present study was designed to investigate the association of elastase with human fibroblasts at 4 degrees C. Elastase bound saturably to binding sites that were present on the surface of these cells. Analysis of cell-bound elastase by sodium dodecyl sulfate-polyacrylamide gel electrophoresis revealed the presence of a high molecular weight complex (Mr 54,000) that was not formed with elastase whose catalytic site serine was derivatized with a diisopropylphosphate group. The complex did not represent elastase bound to either protease nexin or contaminating serum. The cellular component with which elastase formed a complex could not be detected in the cell culture medium. Unexpectedly, elastase that had been pre-bound at 4 degrees C was not internalized after cells were warmed to 37 degrees C. The elastase binding site described in this report is therefore distinct from high affinity binding sites involved in receptor-mediated endocytosis and intracellular degradation.

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Elastin

Cited by 15 publications

References 74 publications

Bulbus arteriosus of the antarctic teleosts. I. The white-bloodedChionodraco hamatus

Bulbus arteriosus of the antarctic teleosts. I. The white-bloodedChionodraco hamatus

The Stumbling Block in Lung Repair of Emphysema: Elastic Fiber Assembly

Binding sites for elastase on cultured human fibroblasts that do not mediate internalization

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