Different amyloid aggregation of smooth muscles titin in vitroстатья
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Дата последнего поиска статьи во внешних источниках: 30 апреля 2021 г.
Аннотация:A comparative study of amyloid properties of the aggregates of smooth muscle titin (SMT) from chicken gizzard was
carried out. These aggregates were formed in two solutions: 0.15 M glycine-KOH, pH 7.2–7.4 (SMT(Gly)) and 0.2 M
KCl, 10 mM imidazole, pH 7.0 (SMT(KCl)). Electron microscopy data showed that SMT aggregates has an amorphous
structure in both cases. The results of atomic-force microscopy demonstrated slight differences in morphology in two
types of aggregates. The SMT(Gly) aggregates were represented as branching chains, composed of spherical aggregates
approximately 300–500 nm in diameter and up to 35 nm in height. The SMT(KCl) aggregates formed sponge-like structures
with strands of 8–10 nm in height. Structural analysis of SMT aggregates by X-ray diffraction revealed the presence
of cross-β-sheet structure in the samples under study. In the presence of SMT(Gly) aggregates, thioflavine T
fluorescence intensity was higher (~3-fold times) compared with that in the presence of SMT(KCl) aggregates. Congo
red-stained SMT(Gly) aggregates had yellow to apple-green birefringence under polarized light, which was not observed
for SMT(KCl) aggregates. Dynamic light scattering data showed the similar rate of aggregation for both types of aggregates,
though SMT(KCl) aggregates were able to partially disaggregate under increased ionic strength of the solution.
The ability of SMT to aggregation followed by disaggregation may be functionally significant in the cell.