The primary filament of bovine elastin

Serafini‐Fracassini, A.; Field, Jacqueline; Hinnie, J.

doi:10.1016/s0022-5320(78)90056-4

Cited by 22 publications

(13 citation statements)

References 12 publications

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“…Plate shows a typical fibrillar supramolecular organization that is very similar to that exhibited by mature elastin and many elastin derived polypeptides 4, 22–26. In particular, it is quite evident the characteristic “twisted‐rope” pattern, in which fibrils, having diameters ranging from 45 to 70 nm, are made by interwond filaments with diameters of about 5 nm.…”

Section: Resultsmentioning

confidence: 79%

Chemical synthesis of cross-linked poly(KGGVG), an elastin-like biopolymer

Martino

Tamburro

2001

Biopolymers

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Previous studies afforded on peptides and polypeptides containing repetitive sequences of elastin have largely demonstrated that their molecular and supramolecular properties are fully representative of those of tropoelastin, the soluble, linear precursor of elastin itself. In the attempt to synthesize cross‐linked elastin‐mimetic polypeptides, the repeating sequence VGGVG (V: valine; G: glycine), typical of elastin, was modified to incorporate lysine residues, yielding the polymer poly(KGGVG) (K: lysine). This imparts primary amine functionality susceptible to cross‐linking reaction with appropriate bifunctional cross‐linking reagents. We report herein the chemical synthesis and cross‐linking of poly(KGGVG) with glutaraldehyde (GTA) and with disuccinimidyl glutarate (DSG). In both cases, the characterization of the polymers, both linear and cross‐linked, has been carried out by CD spectroscopy and transmission electron microscopy measurements. The obtained results, although not conclusive, demonstrate that poly(KGGVG), both linear and cross‐linked, may be considered very similar to tropoelastin and mature elastin, as concerns its molecular and supramolecular properties. © 2001 John Wiley & Sons, Inc. Biopolymers 59: 29–37, 2001

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Section: Resultsmentioning

confidence: 79%

Chemical synthesis of cross-linked poly(KGGVG), an elastin-like biopolymer

Martino

Tamburro

2001

Biopolymers

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“…About the physical and chemical character of the filaments, we have little information. It is worth noting that the protein microfibrils associated with elastic filaments are approximately 8 nm in diameter, and may be composed of finer filaments, approximately 1.5 nm (Gotte and Serafini-Fracassini, 1963) to 2.5 nm (Serafini-Fracassini, 1978). The triple helix of collagen also has a diameter of approximately 1.4 nm and associates to form fibrils of 8 nm and greater (Eyre, 1979), which are probably composed of multiple repeats of 8-nm units (Parry and Craig, 1979).…”

Section: Discussionmentioning

confidence: 99%

Structure and function of the murine muscle–tendon junction

1981

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The muscle-tendon junctions of the extensor carpi radialis longus and brevis muscles from adult Balb C Bailey/J mice have been examined tensiometrically and ultrastructurally following removal of cellular membrane and soluble cytoplasm by exposure to nonionic detergent. As judged by the ability of the extracted muscle to generate tension upon exposure to ATP and to transmit the generated tension to the tendon, detergent extraction leaves the muscle-tendon junction functionally intact. Electron microscopic analysis of the extracted muscle-tendon junctions reveals that the relationship between the terminal myofilaments and the lamina densa of the basal lamina is retained, despite the extensive extraction of the plasma membrane. Fine filaments (2-7 nm) are seen to connect the lamina densa with an electron-dense intracellular layer into which terminal actin filaments appear to insert. These fine filaments are considered to represent an important component of the structural linkage between myofilaments and connective tissue and hence to be a significant component of the tension transmitting mechanism. Their precise nature is not known, but some part of the filaments must pass through the hydrophobic compartment of the plasma membrane and thus must be a transmembrane component of considerable tensile strength. These studies suggest that detergent-extractable membrane lipids play no significant role in the transmission of tension at the muscle-tendon junction, and that fine filaments, probably protein, are responsible for transmitting tension from myofilaments, through the plasma membrane, to the lamina densa of the basal lamina.

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“…The elastin in the box is surrounded by bulk water. This portrayal is modeled on the 5 nm diameter filament beads, 6,7 and the connecting structures might correspond to the lateral bridges observed by Pasquali Ronchetti using scanning force microscopy of bovine ligament elastin. 7 But since so little of the morphology of this scale has been established, the details should not be assumed to show specific physical structures.…”

Section: Figurementioning

confidence: 99%

“…However, many questions exist about the organization of elastin within a fiber, starting with the cross-linking of a tropoelastin molecule into the rest of the network. Tropoelastins appear to be covalently linked end to end to form what has been termed a primary filament, 6 but the nature of the lateral interaction between primary filaments has not been established. Lateral bridges observed by scanning force microscopy 7 may represent cross-links, but the ease of filament dissociation suggests the interaction is weak.…”

Section: Introductionmentioning

confidence: 99%

“…Lateral bridges observed by scanning force microscopy 7 may represent cross-links, but the ease of filament dissociation suggests the interaction is weak. 6 The filaments run parallel to the fiber axis and are organized into longitudinal fibrils that form the fibers. Given the necessary mechanical continuity of the elastin, it is unlikely that this ultrastructure introduces any factor that invalidates the assumption of network continuity, but more information on the fiber substructure is necessary to fully assess the validity of our assumption.…”

Section: Introductionmentioning

confidence: 99%

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Unusual swelling of elastin

Lillie

Gosline

2002

Biopolymers

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The swelling behavior of the elastin network has been investigated by comparing the linear expansion of samples of purified elastin with the volume expansion of the network, calculated on the basis of composition. Elastin sample dimensions and sample masses were measured under three conditions in which volume changes: thermal expansion at fixed water contents, deswelling due to dehydration, and swelling to greater than normal levels due to the swelling agent, sodium dodecyl sulfate. Isotropic network swelling usually changes length in proportion to the cube root of network volume, but length was found to be directly proportional to volume, showing a greater increase in length than expected. This unusual swelling behavior is attributed to an unusual elastin structure at the subfiber level, but there is insufficient detail on elastin's molecular organization to identify a mechanism to explain how it occurs. Assuming the network swells homogeneously, we describe two models that correctly predict swelling behavior, but these models imply a significant deviation from the structure generally assumed for an elastomeric polymer network of kinetically free molecular chains. Assuming that the network swells heterogeneously removes part of the difficulty with the models, but the observed direct proportionality between length and network volume remains to be explained.

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The primary filament of bovine elastin

Cited by 22 publications

References 12 publications

Chemical synthesis of cross-linked poly(KGGVG), an elastin-like biopolymer

Chemical synthesis of cross-linked poly(KGGVG), an elastin-like biopolymer

Structure and function of the murine muscle–tendon junction

Unusual swelling of elastin

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