Key result
Titin and its elastic filaments are hypothesized to possess features of amyloid based on analysis of its structural and functional properties.
The review suggests that titin, a key protein in sarcomere mechanics, may possess amyloid-like properties and form intramolecular amyloid structures in vivo.
Titin amyloid aggregation in muscle may affect sarcomere stiffness; leaves open in vivo confirmation and clinical relevance in cardiomyopathy.
This review considers data on structural and functional features of titin, on the role of this protein in determination of mechanical properties of sarcomeres, and on specific features of regulation of the stiffness and elasticity of its molecules, amyloid aggregation of this protein in vitro, and possibilities of formation of intramolecular amyloid structure in vivo. Molecular mechanisms are described of protection of titin against aggregation in muscle cells. Based on the data analysis, it is supposed that titin and the formed by it elastic filaments have features of amyloid.
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Yakupova et al. (2017) reported a review. Titin was evaluated. Titin and its elastic filaments are hypothesized to possess features of amyloid based on analysis of its structural and functional properties.
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