Smooth muscle titin forms in vitro amyloid aggregates

Amyloids are insoluble fibrous protein aggregates, and their accumulation is associated with amyloidosis and many neurodegenerative diseases, including Alzheimer's disease. In the present study, we report that smooth muscle titin (SMT; 500 kDa) from chicken gizzard forms amyloid aggregates in v...

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Bibliographic Details
Published inBioscience reports Vol. 36; no. 3
Main Authors Bobylev, Alexandr G, Galzitskaya, Oxana V, Fadeev, Roman S, Bobyleva, Liya G, Yurshenas, Darya A, Molochkov, Nikolay V, Dovidchenko, Nikita V, Selivanova, Olga M, Penkov, Nikita V, Podlubnaya, Zoya A, Vikhlyantsev, Ivan M
Format Journal Article
LanguageEnglish
Published England Portland Press Ltd 01.07.2016
Subjects
Amyloid - chemistry
Amyloid - metabolism
Amyloid - ultrastructure
Animals
Cattle
Chickens
Connectin - chemistry
Connectin - metabolism
Connectin - ultrastructure
Humans
Muscle, Smooth - metabolism
Muscle, Smooth - pathology
Original Paper
Original Papers
Protein Aggregates
Protein Aggregation, Pathological - metabolism
Protein Aggregation, Pathological - pathology
Protein Structure, Secondary
smooth muscle titin
amyloid
cytotoxicity
amyloid aggregates
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Summary:Amyloids are insoluble fibrous protein aggregates, and their accumulation is associated with amyloidosis and many neurodegenerative diseases, including Alzheimer's disease. In the present study, we report that smooth muscle titin (SMT; 500 kDa) from chicken gizzard forms amyloid aggregates in vitro This conclusion is supported by EM data, fluorescence analysis using thioflavin T (ThT), Congo red (CR) spectroscopy and X-ray diffraction. Our dynamic light scattering (DLS) data show that titin forms in vitro amyloid aggregates with a hydrodynamic radius (Rh) of approximately 700-4500 nm. The initial titin aggregates with Rh approximately 700 nm were observed beyond first 20 min its aggregation that shows a high rate of amyloid formation by this protein. We also showed using confocal microscopy the cytotoxic effect of SMT amyloid aggregates on smooth muscle cells from bovine aorta. This effect involves the disorganization of the actin cytoskeleton and result is cell damage. Cumulatively, our results indicate that titin may be involved in generation of amyloidosis in smooth muscles.
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ISSN:0144-8463
1573-4935
DOI:10.1042/BSR20160066