Amyloid Aggregates of Smooth-Muscle Titin Impair Cell Adhesion

International Journal of Molecular Sciences

LiyaG. Bobyleva¹  IvanM. Vikhlyantsev¹  RomanS. Fadeev¹  MargaritaI. Kobyakova¹  AlexanderG. Bobylev¹  YuriM. Shlyapnikov¹  DaniilV. Popov² 

[1] Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, Pushchino, 142290 Moscow, Russia;State Research Center Institute of Biomedical Problems, Russian Academy of Sciences, 123007 Moscow, Russia;

关键词: amyloid;    amyloidosis;    amyloid aggregation;    cytotoxicity of amyloid fibrils;    protein aggregation;    smooth-muscle titin;   

DOI  :  10.3390/ijms22094579

来源: DOAJ

【 摘 要 】

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. Сells 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.

【 授权许可】

Unknown