Serhiy Souchelnytskyi - Academia.edu (original) (raw)

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Papers by Serhiy Souchelnytskyi

Acta Biochimica Polonica, Jun 30, 2003

Ukrainian Biochemical Journal, Oct 4, 2022

Journal of Proteomics & Bioinformatics, Nov 25, 2016

Праці Наукового товариства імені Шевченка, Nov 23, 2020

Pracì Naukovogo tovaristva ìmeni Ševčenka, Apr 15, 2020

Current Protein & Peptide Science, Feb 17, 2022

: Post-translational modifications (PTMs) may affect functions of human serum albumin. Here we re... more : Post-translational modifications (PTMs) may affect functions of human serum albumin. Here we review reports of novel PTMs of human serum albumin. One hundred twenty-three recently reported novel O-phosphorylation, glycation, methylation, carbonylation, and acetylation of albumin are reviewed. Potential impact of these PTMs on albumin functions is discussed. Knowledge of these PTMs of albumin is of importance for use of albumin in medical applications, e.g., in transfusion, drug formulations and remedies.

Research Square (Research Square), Sep 1, 2020

Reproductive Biology, Mar 1, 2021

The dynamic embryo development during the early stages of gestation requires precise molecular ch... more The dynamic embryo development during the early stages of gestation requires precise molecular changes, including proteomic ones. We aimed to find unique proteins for porcine conceptuses specifically during the peri-implantation period, i.e. on days 15-16 of pregnancy. The proteomic profile of these conceptuses was compared with conceptuses at an earlier stage of the development, i.e. collected during maternal recognition of pregnancy on days 12-13 of pregnancy. The 2DE, gel image analysis, and MALDI TOF mass spectrometry were used 500 protein spots were annotated as common to conceptuses harvested during both studied periods. Proteomic profile of the conceptuses collected during the peri-implantation period contains 24 unique proteins. Identified unique for the peri-implantation period proteins are involved in adhesion processes, cadherin, and actin-binding, and actin filament organization, extracellular matrix organization, and cytoskeleton organization. Systemic analysis of identified proteins confirmed their involvement in cell adhesion and cytoskeletal organization as being two major affected functions. The unique proteins might be recognized as factors conditioning the proper peri-implantation embryo development and gaining competences for implantation. In further studies, BRCA1 might be considered as a candidate for a potential marker of embryonic competences for implantation in pigs.

Experimental Oncology, 2019

OncoTargets and Therapy, Aug 1, 2014

PubMed, Dec 1, 2022

Purpose: Serum albumin is in contact with practically all cells in the human body, including tumo... more Purpose: Serum albumin is in contact with practically all cells in the human body, including tumor cells in cancer patients. The purpose of this study was to explore whether cancer cells affect post-translational modifications (PTMs) of albumin. Material and methods: Mass spectrometry was used to identify the PTMs. Purified human serum albumin was incubated with human breast cancer cells MDA-MB-231, MDA-MB-468, MCF7, or kept in water or in cell culture media. PTMs which were affected upon exposure of the albumin to cancer cells were identified. Three-dimensional analysis was performed to locate PTMs in albumin. Results: We report here that an exposure to human breast cancer cells affected post-translational modifications (PTMs) of 14 peptides of human serum albumin (HSA). PTMs at 8 peptides were observed upon exposure of HSA to metastatic MDA-MB-231 and MDA-MB-468 breast cancer cells. PTMs at another 6 peptides were lost in MDA-MB-231 and MDA-MB-468 cells, while these 6 PTMs were observed in HSA exposed to conditionally tumorigenic MCF7 cells, or in HSA kept in water or a cell culture medium. Cancer cell altered phosphorylation, deamidation followed by methylation, acetylation, myristylation, palmitoylation, methylation, cysteine persulfide, and S-6-FMN cysteine modifications were detected in HSA. These PTMs locate predominantly in IB and IIA domains of HSA. Three-dimensional analysis showed that this region corresponds to the lipid-binding site and Sudlow's site 1. Conclusion: Data reported here show that 14 PTMs of human serum albumin can be modified upon its exposure to human breast cancer cells.

Experimental Oncology, 2002

Transforming growth factor-b (TGFb) is a polypeptide growth factor, which regulates cell prolifer... more Transforming growth factor-b (TGFb) is a polypeptide growth factor, which regulates cell proliferation, differentiation, migration and apoptosis. During the last decade an exploration of mechanisms ...

Journal of Elementology, Jul 11, 2016

(A) Graphs show distribution of connections for species of the networ... more (A) Graphs show distribution of connections for species of the network. Distribution for proteins identified by phosphoproteomics (rhombs; experimental data) and as would be expected by a power law distribution of connections of species in an ideal scale-free network (squares; predicted distribution) are shown. (B) A sub-network of 14-3-3σ (SFN). Proteins which are in proximal dependencies to 14-3-3σ were extracted from the complete network (<a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0065163#pone.0065163.s005" target="_blank">Figure S5</a>) into the presented sub-network. (C) Signaling pathways involving the proteins assembled in the 14-3-3σ sub-network. The analysis was performed using Gene Set Analysis Toolkit V2 software. (D) Validation of 14-3-3σ phosphorylation upon treatment of cells with TGFβ1. Images of the areas of 2D Fe-IMAC gels with annotation of phosphoprotein spots p72 and p74, in which 14-3-3σ was identified are shown. Values of the protein spot volumes are shown below images of gels for both protein spots. (E) Phosphorylation of endogenous 14-3-3σ in MCF10A cells was evaluated by immunoprecipitation with anti-phosphoserine, threonine and tyrosine antibodies (upper panel) or by incorporation of 32P (middle panel). Control immunoprecipitation of 14-3-3σ is shown in lower panel. Densitometry analysis of the protein immunoblots or 32P incorporation is shown in accompanying graphs. (F) Phosphorylation of Flag-14-3-3σ fusion protein expressed in HEK293T cells was evaluated in the same way as for endogenous protein. The upper panel shows detection of phosphorylation by immunoprecipitation and the middle panel shows incorporation of 32P. The lower panel shows expression of 14-3-3σ. Migration positions of 14-3-3σ are shown by the arrows and treatments with TGFβ1 are indicated. Densitometry analysis of the protein immunoblots is shown in accompanying graphs. Representative experiments out of 3 performed are shown.</p

Biochem Biophys Res Commun, 2002

Experimental oncology

Aim: to study in vitro the antiproliferative influence of interferon-α2b (²FN-α2b), transforming ... more Aim: to study in vitro the antiproliferative influence of interferon-α2b (²FN-α2b), transforming growth factor-β1 (TGF-β1), cys-platinum, cyclophosphamide, and paclitaxel on the of human microvascular endothelial cells for the development of approaches of the antiangiogenic therapy of malignancies. Methods: [3H]-methylthymidine incorporation into human microvascular endothelial derma-derived cells (HMVECd) treated with ²FN-a2b, TGF-b1, cysplatinum, cyclophosphamide, and paclitaxel have been studied. Results: studied cytokines and drugs inhibited proliferation of HMVECd cells at low concentrations (²FN-α2b — 50.0 and 100.0 IU/ml; TGF-β1 — 5.0 ng/ml; cysplatinum — 0.5 μg/ml; paclitaxel — 10.0 μg/ml; cyclophosphamide — 50.0 μg/ml). Conclusion: low concentrations of ²FN-α2b, ÒGF-β1, cysplatinum, cyclophosphamide, ànd paclitaxel inhibited proliferation of cultured endothelial cells, suggesting a possibility of low-dose antiangiogenic therapy in the long-term (“metronomic”) regimen.