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V Lankasová

Publications and source records attributed to V Lankasová.

5 recordsLinked to original sources

Formation of collagen-like fibrils from alpha-elastin.

Collagen-like structures were formed in solutions of alpha-elastin after heating to 57 degrees C and after treatment with absolute ethanol. A complex between acetyl-alpha-elastin and cetyltrimethylammonium bromide showed a similar structure. Thick fibrils (diameter approximately 100 nm), resembling those described by Volpin, et al.12 revealed transversal banding with periodicity of 39 to 62 nm. A possible mechanism for the formation of these fibers is suggested based on hydrophobic interactions.

Animals↗

Fibrillar structure of alpha-elastin methylester complexes with glycoproteins and proteoglycans.

alpha-Elastin methylester forms with proteoglycan subunits and structural glycoproteins water-insoluble complexes which after staining with phosphotungstic acid (pH 7.0), reveal at large magnification bundles of slender smooth fibrils with a diameter from 4 to 5 nm. Similar fibrils can be observed after interaction of alpha-elastin methylester with chondroitin sulfate, but only if fixation with glutaraldehyde is used prior to staining. Phosphotungstic acid alters the organization of the complexes, in particular those formed with ligands of low molecular weight. The possible biological significance of the interactions studied is discussed.

Animals↗

Interaction of a tropoelastin model with connective tissue components.

It has been suggested that tropoelastin interacts with macromolecular components of connective tissue during the formation of elastic fibers. alpha-Elastin, used traditionally as a model of tropoelastin and mature elastin, is not suitable for the monitoring of this interaction in vitro. Therefore a new model of tropoelastin, the methyl ester of alpha-elastin, was synthesized and the interaction of this modified elastin with hyaluronic acid, chondroitin sulfate, proteoglycan subunits, solubilized structural glycoproteins and collagen was studied by turbidimetric measurement. Results indicate that alpha-elastin methyl ester is a better model of tropoelastin than alpha-elastin especially in those experiments where ionic interactions are believed to occur. It was also found that alpha-elastin methyl ester formed aggregates with hyaluronic acid, chondroitin sulfate, proteoglycan subunits and solubilized structural glycoproteins at room temperature and under conditions close to physiological ones. Alpha-elastin does not interact with these compounds under similar conditions. The character of the bonds involved in the interaction and the possible biological significance of the experiments are discussed.

Animals↗

Interaction of alpha-elastin with ionic detergents.

Coacervation is known to be a fundamental step in elastogenesis that is influenced by various naturally occurring substances in connective tissue. Therefore, interaction of alpha-elastin with ionic detergents (sodium dodecyl sulfate, dodecylbenzyldimethylammonium bromide, cetyltrimethylammonium bromide, pentadecacarbethoxytrimethylammonium bromide and cetylpyridinium bromide) was studied as a model for the elastin interaction with amphipilic substances. The course of the interactions was followed by the effect on thermal coacervation, solubilization of lipophilic dye, difference spectra measurements and fluorescence probe. The results indicate that the detergents examined interact with alpha-elastin below critical micelle concentration in two different ways. In the first case, a mixed micelle can be formed from the detergent molecules (SDS, DBD) and alpha-elastin: alternatively mixed micelles are not formed, but the detergent molecules (CT, PCT, CP) do interact with elastin. The interaction of alpha-elastin at the isoelectric point was found to depend more on the chemical structure of the detergent molecule than on its charge. If detergent concentrations above the critical micelle concentration were applied, the interaction mechanism was different from that observed at lower detergent concentration.

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