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- Lomnytska, M. I., et al.
(author)
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Differential expression of ANXA6, HSP27, PRDX2, NCF2, and TPM4 during uterine cervix carcinogenesis : diagnostic and prognostic value
- 2011
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In: British Journal of Cancer. - : Springer Science and Business Media LLC. - 0007-0920 .- 1532-1827. ; 104:1, s. 110-119
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Journal article (peer-reviewed)abstract
- Background:Cytology-based diagnostics of squamous cervical cancer (SCC) precursor lesions is subjective and can be improved by objective markers.Methods:IHC-based analysis of ANXA6, HSP27, peroxiredoxin 2 (PRDX2), NCF2, and tropomyosin 4 (TPM4) during SCC carcinogenesis.Results:Expression of ANXA6, HSP27, PRDX2, and NCF2 in the cytoplasm of dysplastic cells increased from cervical intraepithelial neoplasia 2/3 (CIN2/3) to microinvasive cancer. Invasive SCC showed lower expression of TPM4 than CIN and normal epithelium. CIN2/3 with the highest sensitivity and specificity differed from normal epithelium by cytoplasmic expression of HSP27. Patients with cytoplasmic HSP27 expression in SCC deviating from that observed in normal epithelium had worse relapse-free (P0.019) and overall (P0.014) survival. Invasive SCC with the highest sensitivity and specificity differed from normal epithelium by expression of PRDX2 and TPM4 in the cytoplasm, from CIN2/3 by the expression of ANXA6 and TPM4 in the cytoplasm, and from microinvasive SCC by the expression of PRDX2 and ANXA6 in the cytoplasm. The number of sporadic ANXA6 cells between the atypical cells increased from CIN2/3 to invasive SCC.Conclusion:Detection of expression changes of the proteins ANXA6, HSP27, PRDX2, NCF2, and TPM4 in SCC precursor lesions may aid current cytological and pathological diagnostics and evaluation of prognosis.
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- Lomnytska, M. I., et al.
(author)
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Impact of genomic stability on protein expression in endometrioid endometrial cancer
- 2012
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In: British Journal of Cancer. - : Springer Science and Business Media LLC. - 0007-0920 .- 1532-1827. ; 106:7, s. 1297-1305
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Journal article (peer-reviewed)abstract
- BACKGROUND: Genomic stability is one of the crucial prognostic factors for patients with endometrioid endometrial cancer (EEC). The impact of genomic stability on the tumour tissue proteome of EEC is not yet well established.METHODS: Tissue lysates of EEC, squamous cervical cancer (SCC), normal endometrium and squamous cervical epithelium were subjected to two-dimensional (2D) gel electrophoresis and identification of proteins by MALDI TOF MS. Expression of selected proteins was analysed in independent samples by immunohistochemistry.RESULTS: Diploid and aneuploid genomically unstable EEC displayed similar patterns of protein expression. This was in contrast to diploid stable EEC, which displayed a protein expression profile similar to normal endometrium. Approximately 10% of the differentially expressed proteins in EEC were specific for this type of cancer with differential expression of other proteins observed in other types of malignancy (e.g., SCC). Selected proteins differentially expressed in 2D gels of EEC were further analysed in an EEC precursor lesion, that is, atypical hyperplasia of endometrium, and showed increased expression of CLIC1, EIF4A1 and PRDX6 and decreased expression of ENO1, ANXA4, EMD and Ku70.CONCLUSION: Protein expression in diploid and aneuploid genomically unstable EEC is different from the expression profile of proteins in diploid genomically stable EEC. We showed that changes in expression of proteins typical for EEC could already be detected in precursor lesions, that is, atypical hyperplasia of endometrium, highlighting their clinical potential for improving early diagnostics of EEC.
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- Babizhetskyy, V., et al.
(author)
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Investigation in the ternary Ta-Ni-P system : Solid state phase equilibria at T=1070 K, crystal and electronic structures of new ternary phosphides
- 2021
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In: Journal of Alloys and Compounds. - : Elsevier BV. - 0925-8388 .- 1873-4669. ; 864
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Journal article (peer-reviewed)abstract
- The solid state phase diagram for the ternary Ta-Ni-P system was established at T=1070 K in the region of up to 67 at% of P by means of X-ray powder diffraction methods (PXRD). Six ternary compounds, namely Ta4NiP (Nb4CoSi-type), Ta1.10-0.82Ni0.90-1.18P (TiNiSi-type), TaNiP2 (NbNiP2-type), Ta(5.00-4.81)Ni(4.00-4.19)P4 (Nb5Cu4Si4-type), TaNi2P (own structure type) and Ta1-0.08(1)Ni0.08(1)P2 (OsGe2-type) have been confirmed to exist. Rather minor Ta/Ni homogeneity ranges have been found for alpha-Ta3-xNixP (x=0.2) (Ti3P-type), Ta1-xNixP (x=0.18) (NbAs-type), Ni3-xTaxP (x=0.2) (Ni3P-type) and Ni2-xTaxP (x=0.25) (Fe2P-type). The crystal structure of Ta4.811(9)Ni4.189(9)P4 has been refined from single crystal X-ray diffraction data (Nb5Cu4Si4-type, space group I4/m, a =9.8474(17), c=3.5182(7) angstrom, R1=0.0283, wR2=0.0470), while that of the new TaNi2P compound was determined by means of PXRD. This phosphide crystalizes in its own structure type (space group Pnma, a=8.3588(3), b=3.5208(1), c=6.7051(3) angstrom, R-I=0.044, R-P=0.161). A new isostructural Fe-compound, TaFe2P (a=8.358(2), b=3.5194(7), c=6.703(1) angstrom), was also synthetized. The electronic structures of Ta5Ni4P4 and TaNi2P were analyzed using the tight-binding linear muffin-tin orbital (TB-LMTO) and extended Huckel methods.
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- Stasyk, T, et al.
(author)
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Phosphoproteome profiling of transforming growth factor (TGF)-beta signaling: abrogation of TGFbeta1-dependent phosphorylation of transcription factor-II-I (TFII-I) enhances cooperation of TFII-I and Smad3 in transcription
- 2005
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In: Molecular biology of the cell. - : American Society for Cell Biology (ASCB). - 1059-1524 .- 1939-4586. ; 16:10, s. 4765-4780
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Journal article (peer-reviewed)abstract
- Transforming growth factor-β (TGFβ) signaling involves activation of a number of signaling pathways, several of which are controlled by phosphorylation events. Here, we describe a phosphoproteome profiling of MCF-7 human breast epithelial cells treated with TGFβ1. We identified 32 proteins that change their phosphorylation upon treatment with TGFβ1; 26 of these proteins are novel targets of TGFβ1. We show that Smad2 and Smad3 have different effects on the dynamics of TGFβ1-induced protein phosphorylation. The identified proteins belong to nine functional groups, e.g., proteins regulating RNA processing, cytoskeletal rearrangements, and proteasomal degradation. To evaluate the proteomics findings, we explored the functional importance of TGFβ1-dependent phosphorylation of one of the targets, i.e., transcription factor-II-I (TFII-I). We confirmed that TGFβ1 stimulated TFII-I phosphorylation at serine residues 371 and 743. Abrogation of the phosphorylation by replacement of Ser371 and Ser743 with alanine residues resulted in enhanced complex formation between TFII-I and Smad3, and enhanced cooperation between TFII-I and Smad3 in transcriptional regulation, as evaluated by a microarray-based measurement of expression of endogenous cyclin D2, cyclin D3, and E2F2 genes, and by a luciferase reporter assay. Thus, TGFβ1-dependent phosphorylation of TFII-I may modulate TGFβ signaling at the transcriptional level.
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