Next Article in Journal
Mesenchymal Stem Cells Antagonize IFN-Induced Proinflammatory Changes and Growth Inhibition Effects via Wnt/β-Catenin and JAK/STAT Pathway in Human Outer Root Sheath Cells and Hair Follicles
Next Article in Special Issue
Trypsin Induced Degradation of Amyloid Fibrils
Previous Article in Journal
Serum APOA4 Pharmacodynamically Represents Administered Recombinant Human Hepatocyte Growth Factor (E3112)
Previous Article in Special Issue
Stress Response Is the Main Trigger of Sporadic Amyloidoses
Open AccessArticle

Amyloid Aggregates of Smooth-Muscle Titin Impair Cell Adhesion

1
Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, Pushchino, 142290 Moscow, Russia
2
State Research Center Institute of Biomedical Problems, Russian Academy of Sciences, 123007 Moscow, Russia
*
Authors to whom correspondence should be addressed.
Academic Editor: Konstantin K. Turoverov
Int. J. Mol. Sci. 2021, 22(9), 4579; https://doi.org/10.3390/ijms22094579
Received: 31 March 2021 / Revised: 21 April 2021 / Accepted: 24 April 2021 / Published: 27 April 2021
(This article belongs to the Special Issue Pathological and Functional Amyloid Fibrils)
Various amyloid aggregates, in particular, aggregates of amyloid β-proteins, demonstrate in vitro and in vivo cytotoxic effects associated with impairment of cell adhesion. We investigated the effect of amyloid aggregates of smooth-muscle titin on smooth-muscle-cell cultures. The aggregates were shown to impair cell adhesion, which was accompanied by disorganization of the actin cytoskeleton, formation of filopodia, lamellipodia, and stress fibers. Cells died after a 72-h contact with the amyloid aggregates. To understand the causes of impairment, we studied the effect of the microtopology of a titin-amyloid-aggregate-coated surface on fibroblast adhesion by atomic force microscopy. The calculated surface roughness values varied from 2.7 to 4.9 nm, which can be a cause of highly antiadhesive properties of this surface. As all amyloids have the similar structure and properties, it is quite likely that the antiadhesive effect is also intrinsic to amyloid aggregates of other proteins. These results are important for understanding the mechanisms of the negative effect of amyloids on cell adhesion. View Full-Text
Keywords: amyloid; amyloidosis; amyloid aggregation; cytotoxicity of amyloid fibrils; protein aggregation; smooth-muscle titin amyloid; amyloidosis; amyloid aggregation; cytotoxicity of amyloid fibrils; protein aggregation; smooth-muscle titin
Show Figures

Figure 1

MDPI and ACS Style

Bobylev, A.G.; Fadeev, R.S.; Bobyleva, L.G.; Kobyakova, M.I.; Shlyapnikov, Y.M.; Popov, D.V.; Vikhlyantsev, I.M. Amyloid Aggregates of Smooth-Muscle Titin Impair Cell Adhesion. Int. J. Mol. Sci. 2021, 22, 4579. https://doi.org/10.3390/ijms22094579

AMA Style

Bobylev AG, Fadeev RS, Bobyleva LG, Kobyakova MI, Shlyapnikov YM, Popov DV, Vikhlyantsev IM. Amyloid Aggregates of Smooth-Muscle Titin Impair Cell Adhesion. International Journal of Molecular Sciences. 2021; 22(9):4579. https://doi.org/10.3390/ijms22094579

Chicago/Turabian Style

Bobylev, Alexander G.; Fadeev, Roman S.; Bobyleva, Liya G.; Kobyakova, Margarita I.; Shlyapnikov, Yuri M.; Popov, Daniil V.; Vikhlyantsev, Ivan M. 2021. "Amyloid Aggregates of Smooth-Muscle Titin Impair Cell Adhesion" Int. J. Mol. Sci. 22, no. 9: 4579. https://doi.org/10.3390/ijms22094579

Find Other Styles
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Article Access Map by Country/Region

1
Search more from Scilit
 
Search
Back to TopTop