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Elfineh, Lioudmila
Alternative names
Publications (8 of 8) Show all publications
Xie, Y., Bergström, T., Jiang, Y., Johansson, P., Marinescu, V. D., Lindberg, N., . . . Uhrbom, L. (2015). The Human Glioblastoma Cell Culture Resource: Validated Cell Models Representing All Molecular Subtypes. EBioMedicine, 2(10), 1351-1363
Open this publication in new window or tab >>The Human Glioblastoma Cell Culture Resource: Validated Cell Models Representing All Molecular Subtypes
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2015 (English)In: EBioMedicine, ISSN 0360-0637, E-ISSN 2352-3964, Vol. 2, no 10, p. 1351-1363Article in journal (Refereed) Published
Abstract [en]

Glioblastoma (GBM) is the most frequent and malignant form of primary brain tumor. GBM is essentially incurable and its resistance to therapy is attributed to a subpopulation of cells called gliomastem cells (GSCs). To meet the present shortage of relevant GBM cell (GC) lines we developed a library of annotated and validated cell lines derived from surgical samples of GBM patients, maintained under conditions to preserve GSC characteristics. This collection, which we call the Human Glioblastoma Cell Culture (HGCC) resource, consists of a biobank of 48 GC lines and an associated database containing high-resolution molecular data. We demonstrate that the HGCC lines are tumorigenic, harbor genomic lesions characteristic of GBMs, and represent all four transcriptional sub-types. The HGCC panel provides an open resource for in vitro and in vivo modeling of a large part of GBM diversity useful to both basic and translational GBM research.

Keywords
Glioblastoma, Cell culture, Stem cell culture condition, Molecular subtype, Xenograft models
National Category
Cancer and Oncology Medical Biotechnology (with a focus on Cell Biology (including Stem Cell Biology), Molecular Biology, Microbiology, Biochemistry or Biopharmacy)
Identifiers
urn:nbn:se:uu:diva-274354 (URN)10.1016/j.ebiom.2015.08.026 (DOI)000365959700034 ()26629530 (PubMedID)
Note

De två sista författarna delar sistaförfattarskapet.

Available from: 2016-01-21 Created: 2016-01-21 Last updated: 2018-02-04Bibliographically approved
Elfineh, L., Classon, C., Asplund, A., Pettersson, U., Kamali-Moghaddam, M. & Lind, S. B. (2014). Tyrosine phosphorylation profiling via in situ proximity ligation assay. BMC Cancer, 14, 435
Open this publication in new window or tab >>Tyrosine phosphorylation profiling via in situ proximity ligation assay
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2014 (English)In: BMC Cancer, ISSN 1471-2407, E-ISSN 1471-2407, Vol. 14, p. 435-Article in journal (Refereed) Published
Abstract [en]

Background: Tyrosine phosphorylation (pTyr) is an important cancer relevant posttranslational modification since it regulates protein activity and cellular localization. By controlling cell growth and differentiation it plays an important role in tumor development. This paper describes a novel approach for detection and visualization of a panel of pTyr proteins in tumors using in situ proximity ligation assay. Methods: K562 leukemia cells were treated with tyrosine kinase and/or phosphatase inhibitors to induce differences in pTyr levels and mimic cells with different malignant properties. Cells were then probed with one antibody against the pTyr modification and another probe against the detected protein, resulting in a detectable fluorescent signal once the probes were in proximity. Results: Total and protein specific pTyr levels on ABL, SHC, ERK2 and PI3K proteins were detected and samples of control and treated cells were distinguished at the pTyr level using this novel approach. Promising results were also detected for formalin fixed and paraffin embedded cells in the micro array format. Conclusions: This application of in situ proximity ligation assay is valuable in order to study the pTyr modification of a panel of proteins in large data sets to validate mass spectrometric data and to be combined with tissue microarrays. The approach offers new opportunities to reveal the pTyr signatures in cells of different malignant properties that can be used as biomarker of disease in the future.

Keywords
Cancer biomarkers, Protein signaling, Protein tyrosine phosphorylation, in situ proximity ligation assay (in situ PLA)
National Category
Cancer and Oncology
Identifiers
urn:nbn:se:uu:diva-229297 (URN)10.1186/1471-2407-14-435 (DOI)000338162100001 ()
Available from: 2014-08-06 Created: 2014-08-05 Last updated: 2017-12-05Bibliographically approved
Lind, S. B., Artemenko, K. A., Elfineh, L., Zhao, Y., Bergquist, J. & Pettersson, U. (2013). Post translational modifications in adenovirus type 2. Virology, 447(1-2), 104-111
Open this publication in new window or tab >>Post translational modifications in adenovirus type 2
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2013 (English)In: Virology, ISSN 0042-6822, E-ISSN 1096-0341, Vol. 447, no 1-2, p. 104-111Article in journal (Refereed) Published
Abstract [en]

We have combined 2-D SOS-PAGE with liquid chromatography-high resolving mass spectrometry (LC-MS) to explore the proteome of the adenovirus type 2 (Ad2) at the level of post translational modifications (PTMs). The experimental design included in-solution digestion, followed by titanium dioxide enrichment, as well as in-gel digestion of polypeptides after separation of Ad2 capsid proteins by 1-D and 2-D SOS-PAGE. All samples were analyzed using LC-MS with subsequent manual verification of PTM positions. The results revealed new phosphorylation sites that can explain the observed trains of protein spots observed for the pIII, pIIIa and ply proteins. The pin protein was found to be the most highly modified protein with now 18 verified sites of phosphorylation, three sites of nitrated tyrosine and one sulfated tyrosine. Nitrated tyrosines were also identified in pII. Lysine acetylations were detected in pII and pVI. The findings make the Ad2 virion much more complex than hitherto believed. 

Keywords
Adenovirus type 2, Post translational modification analysis, 2-D SOS-PAGE, High resolving mass spectrometry
National Category
Medical and Health Sciences
Identifiers
urn:nbn:se:uu:diva-212309 (URN)10.1016/j.virol.2013.08.033 (DOI)000326553500011 ()
Available from: 2013-12-10 Created: 2013-12-09 Last updated: 2017-12-06Bibliographically approved
Bergström Lind, S., Artemenko, K. A., Elfineh, L., Zhao, Y., Bergquist, J. & Pettersson, U. (2012). The phosphoproteome of the adenovirus type 2 virion. Virology, 433(1), 253-261
Open this publication in new window or tab >>The phosphoproteome of the adenovirus type 2 virion
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2012 (English)In: Virology, ISSN 0042-6822, E-ISSN 1096-0341, Vol. 433, no 1, p. 253-261Article in journal (Refereed) Published
Abstract [en]

We have used a proteomics approach to identify sites of phosphorylation in the structural proteins of the Adenovirus type 2 particle. This protein modification might play an important role during infection. Peptides from highly purified virus were enriched for phosphorylations and analyzed by liquid chromatography-high-resolving mass spectrometry. Phosphorylations were identified in 11 structural peptides and 29 non-redundant phosphorylation sites were unambiguously assigned to specific amino acid. An unexpected result was the finding of phosphotyrosine in two of the viral polypeptides. The most highly phosphorylated protein was pIIIa with 12 identified phosphorylation sites. An identified preference for proline or leucine residue flanking the phosphorylation sites downstream suggests that cellular kinases are involved in many of the phosphorylations. Structural modeling showed that one site in the hexon is located on the outer side of the virus and could be of importance for the virus when attaching and entering cells.

National Category
Medical and Health Sciences
Identifiers
urn:nbn:se:uu:diva-180351 (URN)10.1016/j.virol.2012.08.012 (DOI)000309797600029 ()22939182 (PubMedID)
Available from: 2012-09-04 Created: 2012-09-04 Last updated: 2017-12-07Bibliographically approved
Bergström Lind, S., Artemenko, K. A., Elfineh, L., Mayrhofer, C., Zubarev, R. A., Bergquist, J. & Pettersson, U. (2011). Toward a comprehensive characterization of the phosphotyrosine proteome. Cellular Signalling, 23(8), 1387-1395
Open this publication in new window or tab >>Toward a comprehensive characterization of the phosphotyrosine proteome
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2011 (English)In: Cellular Signalling, ISSN 0898-6568, E-ISSN 1873-3913, Vol. 23, no 8, p. 1387-1395Article in journal (Refereed) Published
Abstract [en]

Tyrosine phosphorylation (pTyr) regulates important cell functions and plays a key role in carcinogenesis. The purpose of this study was to perform a comprehensive study of the phosphotyrosine proteome. Immunoaffinity enriched pTyr proteins and peptides from K562 leukemia cells were analyzed with high-resolving liquid chromatography mass spectrometry. Two different antibodies selective for the pTyr modification were used in repeated enrichments to identify as many pTyr peptides as possible. Stringent verification of putative pTyr sites was performed to assure high reliability in the subsequent biological interpretation of the data. Identified pTyr proteins were subjected to pathway analysis by using different analytical tools. In total, 294 pTyr peptides belonging to 217 pTyr proteins were identified, 15 of which had not previously been reported to be modified by pTyr. The pTyr proteins were clustered in six major groups based on the biological functions "cellular signaling", "cell motility and shape", "cell cycle process", "transport", "RNA processing" and "protein processing". The pTyr proteins were mainly positioned in the following cellular compartments: cytoplasm, cytoskeleton, nucleus and ribonucleoprotein complexes. An interesting finding was that many proteins were related to RNA processing and were found to be heterogeneous nuclear ribonucleoproteins. Also, more than half of the novel pTyr proteins were localized to the nucleus, of which three (PBX2, TEAD1 and DIDO1) were classified as transcription factors and two (CENPC1 and MAD2L1) are associated with cell division control.

National Category
Chemical Sciences
Identifiers
urn:nbn:se:uu:diva-151812 (URN)10.1016/j.cellsig.2011.03.021 (DOI)000291509700018 ()21447384 (PubMedID)
Available from: 2011-04-18 Created: 2011-04-18 Last updated: 2017-12-11Bibliographically approved
Sevov, M., Elfineh, L. & Cavelier, L. B. (2006). Resveratrol regulates the expression of LXR-alpha in human macrophages. Biochemical and Biophysical Research Communications - BBRC, 348(3), 1047-1054
Open this publication in new window or tab >>Resveratrol regulates the expression of LXR-alpha in human macrophages
2006 (English)In: Biochemical and Biophysical Research Communications - BBRC, ISSN 0006-291X, E-ISSN 1090-2104, Vol. 348, no 3, p. 1047-1054Article in journal (Refereed) Published
Abstract [en]

The naturally occurring polyphenol resveratrol has been associated with the beneficial effects of red wine consumption on cardiovascular disease and shown to inhibit atherosclerosis in animal models. To determine if resveratrol affects the expression of genes that control lipid homeostasis in human macrophages, we measured expression changes in the LXR-alpha pathway, crucial to cholesterol efflux, and in genes that mediate lipoprotein uptake. Resveratrol treatment of THP-1 macrophages induced LXR-alpha at mRNA and protein levels. Increased recruitment of RNA polymerase 11 to the LXR-alpha promoter suggested that up-regulation was at least partly mediated by transcriptional mechanisms. Resveratrol also induced LXR-alpha in human monocyte-derived macrophages together with elevated ABCAI and ABCGI mRNA levels. Moreover, resveratrol repressed the expression of the lipid uptake genes LPL and SR-All. The ability of resveratrol to modulate expression of the genes involved in lipid uptake and efflux suggests that polyphenols can potentially limit cholesterol accumulation in human macrophages.

Keywords
LXR-alpha, THP-1, macrophages, resveratrol, chromatin immunoprecipitation, gene regulation
National Category
Medical and Health Sciences
Identifiers
urn:nbn:se:uu:diva-10546 (URN)10.1016/j.bbrc.2006.07.155 (DOI)000240166500037 ()16901463 (PubMedID)
Available from: 2007-04-02 Created: 2007-04-02 Last updated: 2017-12-11Bibliographically approved
Nordquist, N., Yang, H.-T., Elfineh, L., Vingsbo-Lundberg, C., Bergsteinsdottir, K., Sundvall, M., . . . Pettersson, U. (1999). A genetic linkage map of the rat. Rat genome, 15, 15-20
Open this publication in new window or tab >>A genetic linkage map of the rat
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1999 (English)In: Rat genome, ISSN 1081-4205, Vol. 15, p. 15-20Article in journal (Refereed) Published
National Category
Clinical Medicine
Identifiers
urn:nbn:se:uu:diva-52259 (URN)
Available from: 2008-10-17 Created: 2008-10-17 Last updated: 2014-10-07Bibliographically approved
Johansson, P., Schmidt, L., Baskaran, S., Kundu, S., Gallant, C. J., Kling, T., . . . Nelander, S.Decoding glioblastoma drug responses using an open access library of patient derived cell models.
Open this publication in new window or tab >>Decoding glioblastoma drug responses using an open access library of patient derived cell models
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(English)Manuscript (preprint) (Other academic)
Keywords
glioblastoma, GBM, precision medicine, drug response predictions, proteasome inhibitors, bortezomib
National Category
Medical Biotechnology (with a focus on Cell Biology (including Stem Cell Biology), Molecular Biology, Microbiology, Biochemistry or Biopharmacy)
Research subject
Biology with specialization in Molecular Biology; Oncology; Bioinformatics; Medical Science
Identifiers
urn:nbn:se:uu:diva-340308 (URN)
Available from: 2018-02-04 Created: 2018-02-04 Last updated: 2018-02-04
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