Saint Petersburg Technological Institute

Saint Petersburg, Russia

Saint Petersburg Technological Institute

Saint Petersburg, Russia
Time filter
Source Type

Smirnov A.S.,Saint Petersburg State University | Nikolaev D.N.,Research Institute of Experimental Medicine | Gurzhiy V.V.,Saint Petersburg State University | Smirnov S.N.,Saint Petersburg State University | And 3 more authors.
RSC Advances | Year: 2017

Isatin Schiff base derivatives have a wide range of biological effects. Unfortunately, these compounds possess a serious topological shortcoming: the conformational E Z interconversion. Two ways of conformation stabilization are reported here: complexation with metals that stabilize the E-conformer and substitution in the 4th position of the isatin core stabilizing the Z-form. © The Royal Society of Chemistry.

Formosa A.,University of Rome Tor Vergata | Markert E.K.,Institute for Advanced Study | Lena A.M.,University of Rome Tor Vergata | Italiano D.,University of Rome Tor Vergata | And 6 more authors.
Oncogene | Year: 2013

miRNAs act as oncogenes or tumor suppressors in a wide variety of human cancers, including prostate cancer (PCa). We found a severe and consistent downregulation of miRNAs, miR-154, miR-299-5p, miR-376a, miR-376c, miR-377, miR-381, miR-487b, miR-485-3p, miR-495 and miR-654-3p, mapped to the 14q32.31 region in metastatic cell lines as compared with normal prostatic epithelial cells (PrEC). In specimens of human prostate (28 normals, 99 primary tumors and 13 metastases), lower miRNA levels correlated significantly with a higher incidence of metastatic events and higher prostate specific antigen (PSA) levels, with similar trends observed for lymph node invasion and the Gleason score. We transiently transfected 10 members of the 14q32.31 cluster in normal prostatic epithelial cell lines and characterized their affect on malignant cell behaviors, including proliferation, apoptosis, migration and invasion. Finally, we identified FZD4, a gene important for epithelial-to-mesenchymal transition in (PCa), as a target of miR-377.Oncogene advance online publication, 28 October 2013; doi:10.1038/onc.2013.451.

Tucci P.,Medical Research Council | Tucci P.,University of Calabria | Porta G.,University of Insubria | Agostini M.,Medical Research Council | And 6 more authors.
Cell Cycle | Year: 2013

The mammalian target of rapamycin (mTOR) kinase is a master regulator of protein synthesis that couples nutrient sensing to cell growth, and deregulation of this pathway is associated with tumorigenesis. p53, and its less investigated family member p73, have been shown to interact closely with mTOR pathways through the transcriptional regulation of different target genes. To investigate the metabolic changes that occur upon inhibition of the mTOR pathway and the role of p73 in this response primary mouse embryonic fibroblast from control and TAp73-/- were treated with the macrocyclic lactone rapamycin. Extensive gas chromatography/mass spectrometry (GC/MS) and liquid chromatography/mass spectrometry (LC/MS/MS) analysis were used to obtain a rapamycin-dependent global metabolome profile from control or TAp73 -/- cells. In total 289 metabolites involved in selective pathways were identified; 39 biochemical metabolites were found to be significantly altered, many of which are known to be associated with the cellular stress response. © 2013 Landes Bioscience.

Davidovich P.,Saint Petersburg Technological Institute | Novikova D.,Saint Petersburg Technological Institute | Tribulovich V.,Saint Petersburg Technological Institute | Smirnov S.,Saint Petersburg State University | And 3 more authors.
Journal of Molecular Structure | Year: 2014

Isatin (1H-indole-2,3-dione) is an endogenous natural compound under intense development in medicinal chemistry. Here, we characterize isatin Schiff base derivative by X-ray crystallography. We describe a derivative that crystallizes E-isomer form in the triclinic space group P 1¯; a = 5.9580 (4) A˚, b = 8.4184 (7) A˚, c = 14.1801 (14) A˚, α = 73.962 (8)°, β = 83.184 (7)°, γ = 81.143 (6)°. NMR data show that E-conformer interconverts to the Z-conformer when dissolved, this equilibrium weakly depends on the solvent type. The Z-isomer geometry and the energetics of ΔEE - Zinterconversion barriers were determined by quantum chemical calculations. The isomers are further characterized by means of FT-IR and UV-Vis spectroscopy. © 2014 Elsevier B.V. All rights reserved.

Aksenova V.,Russian Academy of Sciences | Turoverova L.,Russian Academy of Sciences | Khotin M.,Russian Academy of Sciences | Magnusson K.-E.,Linköping University | And 5 more authors.
Oncotarget | Year: 2013

ACTN4 is an actin-binding protein that participates in cytoskeleton organisation. It resides both in the cytoplasm and nucleus and physically associates with various transcription factors. Here, we describe an effect of ACTN4 expression on transcriptional activity of the RelA/p65 subunit of NF-kB. We demonstrate that ACTN4 enhances RelA/p65-dependant expression of c-fos, MMP-3 and MMP-1 genes, but it does not affect TNC, ICAM1 and FN1 expression. Importantly, actin-binding domains of ACTN4 are not critical for the nuclear translocation and co-activation of RelA/p65-dependent transcription. Collectively, our data suggest that in the nucleus, ACTN4 functions as a selective transcriptional co-activator of RelA/p65.

Chillemi G.,CINECA | Davidovich P.,Saint Petersburg Technological Institute | D'Abramo M.,CINECA | Mametnabiev T.,Saint Petersburg Technological Institute | And 4 more authors.
Cell Cycle | Year: 2013

The p53 protein is frequently mutated in a very large proportion of human tumors, where it seems to acquire gain-offunction activity that facilitates tumor onset and progression. A possible mechanism is the ability of mutant p53 proteins to physically interact with other proteins, including members of the same family, namely p63 and p73, inactivating their function. Assuming that this interaction might occurs at the level of the monomer, to investigate the molecular basis for this interaction, here, we sample the structural flexibility of the wild-type p53 monomeric protein. The results show a strong stability up to 850 ns in the DNA binding domain, with major flexibility in the N-terminal transactivations domains (TAD1 and TAD2) as well as in the C-terminal region (tetramerization domain). Several stable hydrogen bonds have been detected between N-terminal or C-terminal and DNA binding domain, and also between N-terminal and C-terminal. Essential dynamics analysis highlights strongly correlated movements involving TAD1 and the proline-rich region in the N-terminal domain, the tetramerization region in the C-terminal domain; Lys120 in the DNA binding region. The herein presented model is a starting point for further investigation of the whole protein tetramer as well as of its mutants. © 2013 Landes Bioscience.

Loading Saint Petersburg Technological Institute collaborators
Loading Saint Petersburg Technological Institute collaborators