Sarcomeric proteins of the titin family form amyloids

• Published in: Biofizika Vol. 50; no. 5; p. 803
• Main Authors: Marsagishvili, L G, Shpagina, M D, Emel'ianenko, V I, Podlubnaia, Z A
• Format: Journal Article
• Language: Russian
• Published: Russia (Federation) 01.09.2005
• Subjects: Alzheimer Disease - metabolism; Amyloid - chemistry; Amyloid - metabolism; Amyloid - ultrastructure; Amyloid beta-Peptides - chemistry; Amyloid beta-Peptides - metabolism; Amyloid beta-Peptides - ultrastructure; Animals; Connectin; Microscopy, Electron, Transmission; Muscle Proteins - chemistry; Muscle Proteins - metabolism; Muscle Proteins - ultrastructure; Protein Conformation; Protein Kinases - chemistry; Protein Kinases - metabolism; Protein Kinases - ultrastructure; Rabbits; tau Proteins - chemistry; tau Proteins - metabolism
• ISSN: 0006-3029

It was shown for the first time that skeletal muscle sarcomeric proteins of the titin family (X-, C- and H-proteins) are able to form in vitro amyloid aggregates of different types: granular aggregates, protofibrils, helically twisted ribbons, linear fibrils, and bundles of linear fibrils. Their amyloid nature was confirmed by electron, polarization, and fluorescence microscopy and by spectral methods. As opposed to other amyloidogenic proteins, X-, C-, and H-proteins easily form amyloids under mild conditions close to physiological ones (pH, ionic strength, temperature). Like amyloid fibrils of Abeta-peptide and tau protein in Alzheimer's disease, amyloid aggregates formed by X-, C-, and H-proteins are destroyed by the antibiotic tetracycline. Thus, new proteins-precursors of amyloids and possible participants of amyloidoses in muscles were discovered. Further study of in vitro amyloidogenesis of these proteins would help to find approaches to controlling this process in organs and tissues.