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  • 1.
    Bauden, Monika
    et al.
    Lund University.
    Tassidis, Helena
    Kristianstad University, School of Education and Environment, Avdelningen för Naturvetenskap. Kristianstad University, Research environment Man & Biosphere Health (MABH).
    Ansari, Daniel
    Lund University.
    In vitro cytotoxicity evaluation of HDAC inhibitor Apicidin in pancreatic carcinoma cells subsequent time and dose dependent treatment2015In: Toxicology Letters, ISSN 0378-4274, E-ISSN 1879-3169, Vol. 236, no 1, p. 8-15Article in journal (Refereed)
    Abstract [en]

    Apicidin is a potent histone deacetylase inhibitor (HDACI) that selectively binds to histone deacetylases (HDACs) class I and interferes with the deacetylation process, which results in modification of acetylation level of cellular proteins. The aim of the study was to investigate the potential time and dose dependent cytotoxicity of the test compound, Apicidin, in pancreatic cancer cells Capan-1 and Panc-1 as well as estimate maximal tolerable dose (MTD) of the test agent and determine EC50 using four complementary colorimetric cytotoxicity or viability assays. The cells were treated with increasing concentrations of Apicidin (0-5000nM) for 2, 4 and 6h (short term exposure) or 24, 48 and 72h (long term exposure) before conducting cytotoxic analyses with lactate dehydrogenase assay or viability analyses with sulforhodamine B (SRB), methyl tetrazolium (MTT) and crystal violet (CV) assays. In order to investigate whether Apicidin irreversibly affects the cells already during the short term exposure, the medium containing Apicidin was removed and replaced with fresh culturing medium after 6h of treatment. The cells were then incubated for additional 24, 48 or 72h before carrying out the analysis. The results obtained from cytotoxicity and viability assays indicated, that Apicidin was well tolerated by both cell lines at concentrations below 100nM at any given time point and at all applied concentrations during the short term (6h or less) treatment. Continuous prolonged term exposures (48h or greater) of the cells to Apicidin with concentration exceeding 100nM resulted in significantly increasing cytotoxicity and sustained significant loss of cell viability. Moreover, long term exposure of pancreatic cancer cells Capan-1 and Panc-1 to Apicidin concentrations exceeding 100nM showed an initial anti-proliferative effect before cytotoxicity onset. In summary, MTD was exposure time dependent and estimated to 100nM for long term treatment and to at least 5000nM for treatment not greater than 6h. EC50 concentration of Apicidin was established after long term treatment, however with some variation when comparing the different assays and cell lines. Results from this study may encourage reinvestigating the capacity of potent HDACI Apicidin as an attractive agent for interfering with the deacetylation process catalyzed by HDACs for potential pancreatic cancer intervention.

  • 2.
    Czernekova, Michaela
    et al.
    Kristianstad University, School of Education and Environment, Avdelningen för Naturvetenskap. Kristianstad University, Research environment Man & Biosphere Health (MABH). Charles University, Prague.
    Tassidis, Helena
    Kristianstad University, School of Education and Environment, Avdelningen för Naturvetenskap. Kristianstad University, Research environment Man & Biosphere Health (MABH).
    Holm, Ingvar
    Kristianstad University, School of Education and Environment, Avdelningen för Naturvetenskap. Kristianstad University, Research environment Man & Biosphere Health (MABH).
    Jönsson, K. Ingemar
    Kristianstad University, School of Education and Environment, Avdelningen för Naturvetenskap. Kristianstad University, Research environment Man & Biosphere Health (MABH).
    Primary Culture of Tardigrade Storage Cells from Richtersius coronifer Richters, 19032016Conference paper (Refereed)
    Abstract [en]

    Coelomocytes are macrophage-like cells in the body cavity or the coelomic spaces of many invertebrates and play major roles in their physiology and immunology. Their structure, function and diversity, however, is still poorly understood.

    Tardigrades are micrometazoans inhabiting a wide variety of environments and with an ability to survive extreme conditions. Coelomocytes (“storage cells”) represent an important part of tardigrade physiology, storing and distributing energy and possibly also having immunological functions. Few studies of tardigrade cell biology have been reported and neither primary nor continuous cell cultures have been established. Tardigrades are normally found and also cultured in an environment rich in microorganisms, some of which may even be of symbiotic value.

    In this study we have tried to establish a primary culture of storage cells in the eutardigrade Richtersius coronifer. Different cell media and concentrations of fetal bovine serum (FBS) were tested. Extracting cells from the tardigrades in an antiseptical environment is challenging since it has to be done under a microscope and contamination from the tardigrades surface is also a problem. To avoid this we tried culturing with high concentrations of antibiotics and antimycotics. We managed to keep the cells viable for up to 18 days in Grace insect medium with 10 % FBS at 20-22°C. The medium was changed every third day. 10x Antibiotic-Antimycotic and 5x of Penicillin-Streptomycin were used to minimize contamination. These concentrations reduce the bacterial abundance, but contamination with fungi was still an issue. Cell morphology evaluation was performed daily and no obvious toxic effects on the cells was observed. Cell viability and cell division were evaluated with Trypan blue staining and cell counting in a haemocytometer. The results indicate that the cells are viable and that some cell division occurs, however more studies need to be performed to confirm this. Still, this study provides the first evidence that primary cultures of storage cells from tardigrades are possible to establish, but the culturing method has to be refined to avoid contamination.

  • 3.
    El-Schich, Zahra
    et al.
    Malmö University.
    Mölder, Anna
    Phase Holographic Imaging AB, Lund.
    Tassidis, Helena
    Kristianstad University, School of Education and Environment, Avdelningen för Naturvetenskap. Kristianstad University, Research environment Man & Biosphere Health (MABH).
    Härkönen, Pirkko
    Finland.
    Miniotis, Maria Falck
    Malmö University.
    Gjörloff Wingren, Anette
    Malmö University.
    Induction of morphological changes in death-induced cancer cells monitored by holographic microscopy2015In: Journal of Structural Biology, ISSN 1047-8477, E-ISSN 1095-8657, Vol. 189, no 3, p. 207-212Article in journal (Refereed)
    Abstract [en]

    We are using the label-free technique of holographic microscopy to analyze cellular parameters including cell number, confluence, cellular volume and area directly in the cell culture environment. We show that death-induced cells can be distinguished from untreated counterparts by the use of holographic microscopy, and we demonstrate its capability for cell death assessment. Morphological analysis of two representative cell lines (L929 and DU145) was performed in the culture flasks without any prior cell detachment. The two cell lines were treated with the anti-tumour agent etoposide for 1-3days. Measurements by holographic microscopy showed significant differences in average cell number, confluence, volume and area when comparing etoposide-treated with untreated cells. The cell volume of the treated cell lines was initially increased at early time-points. By time, cells decreased in volume, especially when treated with high doses of etoposide. In conclusion, we have shown that holographic microscopy allows label-free and completely non-invasive morphological measurements of cell growth, viability and death. Future applications could include real-time monitoring of these holographic microscopy parameters in cells in response to clinically relevant compounds.

  • 4.
    Fridberg, Marie
    et al.
    Lund University.
    Tassidis, Helena
    Lund University.
    Gjörloff Wingren, Anette
    Malmö University.
    PTPN7 (protein tyrosine phosphatase, nonreceptor type 7)2010In: Atlas of Genetics and Cytogenetics in Oncology and Haematology, ISSN 0187-6236, E-ISSN 1768-3262, Vol. 14, no 11, p. 1032-1033Article in journal (Other academic)
  • 5.
    Hadzic, Radinka
    et al.
    Malmö University Hospital.
    Nita, Izabela
    Malmö University Hospital.
    Tassidis, Helena
    Malmö University Hospital.
    Riesbeck, Kristian
    Malmö University Hospital.
    Wingren, Anette Gjörloff
    Malmö University Hospital.
    Janciauskiene, Sabina
    Malmö University Hospital.
    α1-Antitrypsin inhibits Moraxella catarrhalis MID protein-induced tonsillar B cell proliferation and IL-6 release2006In: Immunology Letters, ISSN 0165-2478, E-ISSN 1879-0542, Vol. 102, no 2, p. 141-147Article in journal (Refereed)
    Abstract [en]

    α1-Antitrypsin (AAT) is a major circulating and tissues inhibitor of serine proteinases implicated in the regulation of inflammation and host defence. There is now increasing evidence that AAT may also exhibit anti-inflammatory activities independent of its protease inhibitor function. This study was undertaken to investigate the effects of native (inhibitory) and polymerized (non-inhibitory) forms of AAT on MID (Moraxella IgD binding protein)-induced human tonsillar B cell activation in vitro. We found that 0.5 μg/ml MID induces B cell proliferation and stimulates IL-6 release (p < 0.001) relative to non-stimulated controls. Both native and polymerized AAT (0.5 mg/ml) inhibited MID-stimulated B cell proliferation in a similar manner (by 70%, p < 0.001), whereas MID-induced IL-6 release was more strongly suppressed by polymerized (9.9-fold, p < 0.001) as compared to native AAT (2.8-fold, p < 0.01). Electrophoretic analysis of cell culture media did not indicate any interaction between AAT and MID, and flow cytometry data showed no competition for the same receptor. The effects of AATs were observed whether added together with MID or 2 h after MID-addition to cell cultures. Thus, our data demonstrate that AAT inhibits MID-induced B cell activation in vitro that is unrelated to its protease inhibitory activity and is not dependent on MID binding to the cell surface.

  • 6.
    Hernroth, Bodil
    et al.
    Kristianstad University, School of Education and Environment, Avdelningen för Naturvetenskap. Kristianstad University, Research environment Man & Biosphere Health (MABH).
    Baden, S.
    University of Gothenburg.
    Tassidis, Helena
    Kristianstad University, School of Education and Environment, Avdelningen för Naturvetenskap. Kristianstad University, Research environment Man & Biosphere Health (MABH).
    Hörnaeus, K.
    Uppsala University.
    Guillemant, J.
    Uppsala University.
    Bergström Lind, S.
    Uppsala University.
    Bergquist, J.
    Uppsala University.
    Impact of ocean acidification on antimicrobial activity in gills of the blue mussel (Mytilus edulis)2016In: Fish and Shellfish Immunology, ISSN 1050-4648, E-ISSN 1095-9947, Vol. 55, p. 452-459Article in journal (Refereed)
    Abstract [en]

    Here, we aimed to investigate potential effects of ocean acidification on antimicrobial peptide (AMP) activity in the gills of Mytilus edulis, as gills are directly facing seawater and the changing pH (predicted to be reduced from ∼8.1 to ∼7.7 by 2100). The AMP activity of gill and haemocyte extracts was compared at pH 6.0, 7.7 and 8.1, with a radial diffusion assay against Escherichia coli. The activity of the gill extracts was not affected by pH, while it was significantly reduced with increasing pH in the haemocyte extracts. Gill extracts were also tested against different species of Vibrio (V. parahaemolyticus, V. tubiashii, V. splendidus, V. alginolyticus) at pH 7.7 and 8.1. The metabolic activity of the bacteria decreased by ∼65–90%, depending on species of bacteria, but was, as in the radial diffusion assay, not affected by pH. The results indicated that AMPs from gills are efficient in a broad pH-range. However, when mussels were pre-exposed for pH 7.7 for four month the gill extracts presented significantly lower inhibit of bacterial growth. A full in-depth proteome investigation of gill extracts, using LC-Orbitrap MS/MS technique, showed that among previously described AMPs from haemocytes of Mytilus, myticin A was found up-regulated in response to lipopolysaccharide, 3 h post injection. Sporadic occurrence of other immune related peptides/proteins also pointed to a rapid response (0.5–3 h p.i.). Altogether, our results indicate that the gills of blue mussels constitute an important first line defence adapted to act at the pH of seawater. The antimicrobial activity of the gills is however modulated when mussels are under the pressure of ocean acidification, which may give future advantages for invading pathogens.

  • 7.
    Hernroth, Bodil
    et al.
    Kristianstad University, Research environment Man & Biosphere Health (MABH). Kristianstad University, School of Education and Environment, Avdelningen för Naturvetenskap. The Royal Swedish Academy of Sciences.
    Holm, Ingvar
    Kristianstad University, School of Education and Environment, Avdelningen för Naturvetenskap. Kristianstad University, Research environment Man & Biosphere Health (MABH).
    Gondikas, Andreas
    University of Gothenburg.
    Tassidis, Helena
    Kristianstad University, School of Education and Environment, Avdelningen för Naturvetenskap. Kristianstad University, Research environment Man & Biosphere Health (MABH).
    Manganese inhibits viability of prostate cancer cells2018In: Anticancer Research, ISSN 0250-7005, E-ISSN 1791-7530, Vol. 38, no 1, p. 137-145Article in journal (Refereed)
    Abstract [en]

    BACKGROUND/AIM: Androgen deprivation therapy is usually in the initial phase a successful treatment for prostate cancer but eventually most patients develop androgen-independent metastatic disease. This study investigated if manganese (Mn) reduces viability of prostate cancer via induction of apoptosis.

    MATERIALS AND METHODS: The prostate cancer cell lines PC3, DU145 and LNCaP underwent dose- and time-dependent screening of viability, analyzed by the 3-(4,5-dimethyl-thiazol-2-yl)-2,5-diphenyl-tetrazolium bromide assay. Flow cytometry was used for the cell-cycle and apoptosis analyses. Intracellular Mn concentration was measured using inductively coupled plasma-mass spectrometry.

    RESULTS: At Mn concentrations of 200-1000 μM, the effect on viability was most pronounced in PC3 followed by LNCaP cells. These cell lines also showed higher intracellular concentration of Mn compared to DU145. In all cell lines, Mn increased the proportion of cells arrested in the G0/G1 phase and induced apoptosis.

    CONCLUSION: To our knowledge, this is the first report demonstrating Mn as a potential agent in prostate cancer therapy.

  • 8.
    Stanezai, S.
    et al.
    Malmö University.
    Sahlen, E.
    Malmö University.
    El-Schich, Z.
    Fridberg, Marie
    Kristianstad University, Research environment Learning in Science and Mathematics (LISMA). Kristianstad University, School of Education and Environment, Avdelningen för Naturvetenskap.
    Fredriksson, G. N.
    Lund University.
    Anagnostaki, L.
    Skåne University Hospital.
    Tassidis, Helena
    Kristianstad University, School of Education and Environment, Avdelningen för Naturvetenskap. Kristianstad University, Research environment Man & Biosphere Health (MABH).
    Persson, L.
    Lund University.
    Gjorloff Wingren, Anette
    Malmö University.
    Higher intensity of Low Molecular Weight Protein Tyrosine Phosphatase/ ACP-1 in survivors of patients diagnosed with Diffuse Large B Cell Lymphoma (DLBCL) compared to non-survivors2016In: Austin Biology, no 2, article id 1009Article in journal (Refereed)
    Abstract [en]

    Adult Diffuse Large B Cell Lymphoma (DLBCL) is a heterogeneous form of hematopoietic cancer and difficult to treat. In order to find a better diagnostic indication for the disease, we analyzed Low Molecular Weight Protein Tyrosine Phosphatase (LMWPTP) that in humans is encoded by the ACP1 gene. LMWPTP is an enzyme shown to counteract Protein Tyrosine Kinases (PTK) and was suggested to be a negative growth factor regulator. However, the 18 kDa PTP can also have a positive effect on cell growth and proliferation, indicating a controversial role in the tumorigenic process. LMWPTP exists in different isoforms which are electrophoretically, kinetically and immunologically distinct. We have studied two subgroups of DLBCL consisting of a Germinal Center B cell like (GCB) and a non-Germinal Center B cell like (non-GCB) group. The two subgroups have been defined by gene-expressing profiling and are associated with differential outcome. The expression levels of LMWPTP protein was compared and showed significant differences between the GCB and non- GCB subgroups (p=0.012). Interestingly, when the samples were divided into survivors and non-survivors, and thereafter analyzed for LMWPTP expression, the samples from patients with a higher survival rate showed increased staining intensity, whereas the samples from patients with lower intensity of LMWPTP did not survive the disease (p=0.001). In conclusion, we have shown that DLBCL patients with worse outcome express LMWPTP with a lower intensity, suggesting a tumor suppressor role for this form of the enzyme.

  • 9.
    Stanezai, S.
    et al.
    Malmö University.
    Sahlén, E.
    Malmö University.
    El-Schich, Z.
    Malmö University.
    Fridberg, Marie
    Kristianstad University, School of Education and Environment, Avdelningen för Naturvetenskap.
    Fredrikson, G.N.
    Malmö University.
    Anagnostaki, L.
    Skane University Hospital.
    Tassidis, Helena
    Kristianstad University, School of Education and Environment, Avdelningen för Naturvetenskap. Kristianstad University, Research environment Man & Biosphere Health (MABH).
    Persson, J.L.
    Lund University.
    Gjörloff Wingren, Anette
    Malmö University.
    Tyrosine Phosphatase/ ACP-1 in survivors of patients diagnosed with Diffuse Large B Cell Lymphoma (DLBCL) compared to non-survivors2016In: Austin Biology, Vol. 1, no 2, article id 1009Article in journal (Refereed)
  • 10.
    Tassidis, Helena
    et al.
    Lund University.
    Brokken, Leon J. S.
    Lund University.
    Jirström, Karin
    Lund University.
    Bjartell, Anders
    Skåne University Hospital, Malmö.
    Ulmert, David
    USA.
    Härkönen, Pirkko
    Finland.
    Gjörloff Wingren, Anette
    Lund University.
    Low expression of SHP-2 is associated with less favourable outcome of prostate cancer2013In: Tumor Biology, ISSN 1010-4283, E-ISSN 1423-0380, Vol. 34, no 2, p. 637-642Article in journal (Refereed)
    Abstract [en]

    Src homology 2 domain-containing tyrosine phosphatase-2 (SHP-2) is an important regulator of cell signaling because of its ability to dephosphorylate receptors of growth factors as well as the cytokines and tyrosine-phosphorylated proteins associated with these receptors. In the current study, we used four different prostate cancer cell lines: PC3, DU145, LNCaP and LNCaP-IL6+. Tumor specimens from 122 patients with prostate cancer were analyzed using a tissue microarray. Our data demonstrate that all four prostate cancer cell lines express the SHP-2 protein. Additionally, low staining intensity and SHP-2 expression in the cytoplasm of cancer cells in prostate tumor specimens was inversely correlated with prostate volume (p = 0.041 and p = 0.042, respectively) whereas nuclear staining was positively correlated with extracapsular extension (p = 0.039). In our post-prostatectomy specimens, we found that patients with low SHP-2 expression had less favorable outcomes with respect to biochemical recurrence and clinical progression (p = 0.005 and p = 0.018, respectively). The loss of cytoplasmic SHP-2 expression is associated with increased growth and prostatic cancer progression.

  • 11.
    Tassidis, Helena
    et al.
    Lund University.
    Brokken, Leon J. S.
    Lund University.
    Jirström, Karin
    Lund University.
    Ehrnström, Roy
    Lund University.
    Pontén, Fredrik
    Uppsala University.
    Ulmert, David
    Lund University.
    Bjartell, Anders
    Lund University.
    Härkönen, Pirkko
    Lund University.
    Gjörloff Wingren, Anette
    Lund University.
    Immunohistochemical detection of tyrosine phosphatase SHP-1 predicts outcome after radical prostatectomy for localized prostate cancer2010In: International Journal of Cancer, ISSN 0020-7136, E-ISSN 1097-0215, Vol. 126, no 10, p. 2296-2307Article in journal (Refereed)
    Abstract [en]

    The protein tyrosine kinase (PTK) receptors and cytosolic signaling proteins as well as the protein tyrosine phosphatases (PTPs) have important roles in regulation of growth of the benign and malignant prostate gland. Here, we studied expression of the protein tyrosine phosphatase SHP-1 in prostate cancer cell lines and in human prostatic tissues. SHP-1 is expressed at a high level in LNCaP prostate cancer cells compared with PC3 cells. Silencing of SHP-1 expression with siRNA in LNCaP cells led to an increased rate of proliferation, whereas overexpression of SHP-1 by means of transient and stable transfection in PC3 cells led to a decrease in proliferation. Corresponding changes were observed in cyclin D1 expression. We further demonstrate that LNCaP and PC3 cells respond differently to IL-6 stimulation. SHP-1 overexpression in PC3 cells reversed IL-6 stimulation of proliferation, whereas in SHP-1-silenced LNCaP cells, IL-6 inhibition of proliferation was not affected. In addition, IL-6 treatment led to higher levels of phosphorylated STAT3 in SHP-1-silenced LNCaP cells than in control cells. Next, SHP-1 expression in human prostate cancer was analyzed by immunohistochemical staining of tissue microarrays comprising tumor specimens from 100 prostate cancer patients. We found an inverse correlation between the tumor level of SHP-1 expression and time to biochemical recurrence and clinical progression among prostate cancer patients. In conclusion, our results suggest that a decreased level of SHP-1 expression in prostate cancer cells is associated with a high proliferation rate and an increased risk of recurrence or clinical progression after radical prostatectomy for localized prostate cancer.

  • 12.
    Tassidis, Helena
    et al.
    Lund University.
    Brokken, Leon
    Ulmert, David
    Ehrnström, Roy
    Jirström, Karin
    Bjartell, Anders
    Härkönen, Pirkko
    Gjörloff Wingren, Anette
    Immunohistochemical detection of tyrosine phosphatase SHP-1 predicts outcome after radical prostatectomy for localized prostate cancer2009In: Cancer Research, ISSN 0008-5472, E-ISSN 1538-7445, Vol. 69, no 9 Supplement, p. LB-257-Article in journal (Other academic)
    Abstract [en]

    The protein tyrosine kinase (PTK) receptors and cytosolic signalling proteins as well as the protein tyrosine phosphatases (PTP) have important roles in regulation of growth and function of the benign and malignant prostate gland. Here we studied the expression levels and functions of the protein tyrosine phosphatase SHP-1 in prostate cancer cell lines and in benign and malignant human prostatic tissues. We found that SHP-1 is expressed at a high level in LNCaP prostate cancer cells compared to PC-3 cells. Silencing of SHP-1 expression with siRNA in LNCaP cells led to an increased rate of proliferation as measured by thymidine incorporation, whereas in PC3 cells in which SHP1 was overexpressed by transient transfection proliferation rate was decreased. We also examined SHP-1 expression in prostate cancer by immunohistochemical staining of tissue microarrays comprising tumor specimens from 122 prostate cancer patients. We found an inverse correlation between SHP-1 staining intensity and the time to biochemical recurrence as measured by a rise in the serum level of prostate-specific antigen (PSA) in prostate cancer patients. In conclusion, our results suggest that a low level of SHP-1 expression in prostate cancer cells is associated with high proliferation rate and with an increased risk of biochemical recurrence after radical prostatectomy for localized prostate cancer.

  • 13.
    Tassidis, Helena
    et al.
    Lund University.
    Culig, Zoran
    Österrike.
    Gjörloff Wingren, Anette
    Lund University.
    Härkönen, Pirkko
    Lund University.
    Role of the protein tyrosine phosphatase SHP-1 in Interleukin-6 regulation of prostate cancer cells2010In: The Prostate, ISSN 0270-4137, E-ISSN 1097-0045, Vol. 70, no 14, p. 1491-1500Article in journal (Refereed)
    Abstract [en]

    BACKGROUND: Interleukin-6 (IL-6) is a multifunctional cytokine that has been implicated in the modulation of growth and progression of prostate cancer. Decreased expression of the tyrosine phosphatase SHP-1, involved in regulation of cytokine and tyrosine kinase receptor signaling, has been shown to be associated with less favorable outcome among prostate cancer patients.

    METHODS: Parental LNCaP cells and an LNCaP-IL6+ subline, derived from parental LNCaP cells by continuous culture of the cells in the presence of recombinant IL-6 were used in the study. Expression of STAT3, pSTAT3, ERK, pERK, AKT, pAKT, PTEN, and SHP-1 was analyzed by immunohistochemistry, Western blots, cDNA microarray, quantitative PCRs, and reverse transcriptase PCRs. Proliferation and apoptosis of transfected cells were analyzed by caspase3/7 assay and flow cytometry.

    RESULTS: Phosphorylation of ERK and STAT3 was increased in the LNCaP-IL6+ subline compared with LNCaP cells, whereas pAKT was decreased. Overexpression and inhibition experiments with SHP-1 siRNA showed that SHP-1 reduced proliferation and increased apoptosis in both cell lines. Microarray analysis revealed 80 up-regulated and 87 down-regulated SHP-1-related genes in the LNCaP-IL6+ cell line compared with LNCaP cells.

    CONCLUSIONS: SHP-1 suppresses growth and increases apoptosis in both LNCaP and LNCaP-IL6+ cells, which suggests that SHP-1 could be a therapeutic target in prostate cancer, even when there is an IL-6-related growth advantage.

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