Regulation of cancer cell migration remains one of the main tasks of practical biochemistry and molecular biology. One way to solve this problem is to control the elastic properties of nucleus since it is one as the biggest and stiffest compartment that determines the cell flexibility. At the same time, the nuclear rigidity is affected by the mechanical properties of the nuclear lamina (NL), a protein meshwork underlying the inner nuclear membrane. Ratio changing of its main structural components – an A- and B-type lamins – is likely to be a key factor in the mechanical properties of nucleus. Furthermore, progerin, a mutant form lamin A, which induces Hutchinson Gilford Progeria Syndrome, is involved in aging by accumulation in NL, leading to nuclear stiffness increasing. However, how progerin presence in NL and changing of lamins ratio effect on cell migration processes is still unclear. To estimate the effect of lamins ratio changing on cell migration, we obtained HT1080 cell lines expressing GFP–lamin A, GFP–progerin and shRNA_LMNA, which specifically prevents the production of lamin A. Cell migration ability was estimated by using scratch and transwell (with 3 and 8 μm pore size) assays. The changing of NL composition is turned out to have no effect on migration in unrestricted space (scratch assay). Both overexpression of lamin A and progerin expression reduce the efficiency of cell migration through 3 μm pore size membranes. Meanwhile, the suppression of lamin A expression has no effect on migration in a transwell. Our data, especially, from scratch assay show the absence of toxic effects of transfection on cell activity and migration in unrestricted space and through pores are larger than nucleus. The presence of various lamin A isoforms in NL is likely to lead to a reduction of migration ability due to the increase of the nuclear rigidity. The absence of effect of lamin A knockdown on migration may be explained that HT1080 cell line is supposed to have initially high migration ability and, possibly, more elastic NL and, consequently, it has originally reduced lamin A level. Therefore our next target is to estimate the level of lamin A isoforms by RT-PCR and WB and to conduct similar experiments by using other cell lines. This work was supported by Russian Science Fund (RSF) № 17-15-01290.