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Tassidis, Helena
Publications (10 of 15) Show all publications
Hernroth, B., Holm, I., Gondikas, A. & Tassidis, H. (2018). Manganese inhibits viability of prostate cancer cells. Anticancer Research, 38(1), 137-145
Open this publication in new window or tab >>Manganese inhibits viability of prostate cancer cells
2018 (English)In: Anticancer Research, ISSN 0250-7005, E-ISSN 1791-7530, Vol. 38, no 1, p. 137-145Article in journal (Refereed) Published
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.

Keywords
DU145, LNCaP, Manganese, PC3, apoptosis, cell viability, prostate cancer
National Category
Medical and Health Sciences
Identifiers
urn:nbn:se:hkr:diva-17770 (URN)10.21873/anticanres.12201 (DOI)000419130100018 ()29277766 (PubMedID)
Available from: 2018-01-08 Created: 2018-01-08 Last updated: 2018-01-18Bibliographically approved
Holm, I., Hernroth, B. & Tassidis, H. (2018). Miljö, medicin och undervisning, hur hänger det ihop?: exempel från projektet mangan och prostatacancer. In: Ann-Sofi Rehnstam-Holm (Ed.), Man and Biosphere Health: en komplett akademisk miljö (pp. 16-21). Kristianstad: Högskolan Kristianstad
Open this publication in new window or tab >>Miljö, medicin och undervisning, hur hänger det ihop?: exempel från projektet mangan och prostatacancer
2018 (Swedish)In: Man and Biosphere Health: en komplett akademisk miljö / [ed] Ann-Sofi Rehnstam-Holm, Kristianstad: Högskolan Kristianstad , 2018, p. 16-21Chapter in book (Other academic)
Abstract [sv]

Forskningsmiljön ”Man and Biosphere Health” är engruppering där forskare från helt olika biologiskakunskapsområden träffas och knyter kontakter. Forskning inom området ”Life Science” (Livsvetenskap), som framförallt innefattar biologi, medicin och biokemi, är världens största tvärdisciplinära forskningsområde med studier av biologisktliv samt de förutsättningar som utgör grunden för fortsatt liv. Unikt för samarbetet inom MABH är kombinationen avekologisk och biomedicinsk kompetens, vilket i vårt fall har inneburit att cellbiologisk forskning har knutits ihop med miljöforskning på ett nyskapande sätt.

Place, publisher, year, edition, pages
Kristianstad: Högskolan Kristianstad, 2018
Series
Kristianstad University Press ; 11:2018
National Category
Other Social Sciences Biological Sciences
Identifiers
urn:nbn:se:hkr:diva-19176 (URN)978-91-87973-35-2 (ISBN)
Available from: 2019-03-18 Created: 2019-03-18 Last updated: 2019-03-18Bibliographically approved
Stanezai, S., Sahlen, E., El-Schich, Z., Fridberg, M., Fredriksson, G. N., Anagnostaki, L., . . . Gjorloff Wingren, A. (2016). 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-survivors. Austin Biology (2), Article ID 1009.
Open this publication in new window or tab >>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-survivors
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2016 (English)In: Austin Biology, no 2, article id 1009Article in journal (Refereed) Published
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.

Keywords
ACP1, B cell, DLBCL, Germinal center, LMWPTP, Lymphoma, Non-germinal center, Prognosis
National Category
Medical Bioscience
Identifiers
urn:nbn:se:hkr:diva-17542 (URN)
Available from: 2017-10-25 Created: 2017-10-25 Last updated: 2017-10-25Bibliographically approved
Hernroth, B., Baden, S., Tassidis, H., Hörnaeus, K., Guillemant, J., Bergström Lind, S. & Bergquist, J. (2016). Impact of ocean acidification on antimicrobial activity in gills of the blue mussel (Mytilus edulis). Fish and Shellfish Immunology, 55, 452-459
Open this publication in new window or tab >>Impact of ocean acidification on antimicrobial activity in gills of the blue mussel (Mytilus edulis)
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2016 (English)In: Fish and Shellfish Immunology, ISSN 1050-4648, E-ISSN 1095-9947, Vol. 55, p. 452-459Article in journal (Refereed) Published
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.

Keywords
Ocean acidification, Mytilus edulis, Antimicrobial peptide, Gill tissue, Vibrio, LPS, Proteome analysis, LC-Orbitrap MS/MS analysis
National Category
Immunology
Identifiers
urn:nbn:se:hkr:diva-15677 (URN)10.1016/j.fsi.2016.04.007 (DOI)000381537000048 ()27288994 (PubMedID)
Funder
Swedish Research Council, 621-2011-4423Swedish Research Council, 2015-4870 JB
Available from: 2016-08-11 Created: 2016-08-11 Last updated: 2017-09-19Bibliographically approved
Hernroth, B., Baden, S., Tassidis, H., Hörnaeus, K., Guillemant, J., Bergström Lind, S. & Bergquist, J. (2016). Impact of oceanacidification on antimicrobial activity in gills of the blue mussel (Mytilusedulis). Fish and Shellfish Immunology, 55, 452-459
Open this publication in new window or tab >>Impact of oceanacidification on antimicrobial activity in gills of the blue mussel (Mytilusedulis)
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2016 (English)In: Fish and Shellfish Immunology, ISSN 1050-4648, E-ISSN 1095-9947, Vol. 55, p. 452-459Article in journal (Refereed) Published
National Category
Natural Sciences
Identifiers
urn:nbn:se:hkr:diva-18683 (URN)10.1016/j.fsi.2016.04.007 (DOI)
Available from: 2018-09-08 Created: 2018-09-08 Last updated: 2018-09-11Bibliographically approved
Czernekova, M., Tassidis, H., Holm, I. & Jönsson, K. I. (2016). Primary Culture of Tardigrade Storage Cells from Richtersius coronifer Richters, 1903. In: : . Paper presented at 12th International Congress on Cell Biology, Prague, 21-25 July.
Open this publication in new window or tab >>Primary Culture of Tardigrade Storage Cells from Richtersius coronifer Richters, 1903
2016 (English)Conference paper, Poster (with or without abstract) (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.

Keywords
tardigrada, björndjur, cellbiologi
National Category
Zoology
Identifiers
urn:nbn:se:hkr:diva-15943 (URN)
Conference
12th International Congress on Cell Biology, Prague, 21-25 July
Available from: 2016-09-06 Created: 2016-09-06 Last updated: 2016-10-12Bibliographically approved
Stanezai, S., Sahlén, E., El-Schich, Z., Fridberg, M., Fredrikson, G., Anagnostaki, L., . . . Gjörloff Wingren, A. (2016). Tyrosine Phosphatase/ ACP-1 in survivors of patients diagnosed with Diffuse Large B Cell Lymphoma (DLBCL) compared to non-survivors. Austin Biology, 1(2), Article ID 1009.
Open this publication in new window or tab >>Tyrosine Phosphatase/ ACP-1 in survivors of patients diagnosed with Diffuse Large B Cell Lymphoma (DLBCL) compared to non-survivors
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2016 (English)In: Austin Biology, Vol. 1, no 2, article id 1009Article in journal (Refereed) Published
Keywords
ACP1, B cell, DLBCL, Germinal center, LMWPTP, Lymphoma, Non-germinal center, Prognosis
National Category
Medical and Health Sciences
Identifiers
urn:nbn:se:hkr:diva-15673 (URN)
Available from: 2016-08-10 Created: 2016-08-10 Last updated: 2016-08-10Bibliographically approved
Bauden, M., Tassidis, H. & Ansari, D. (2015). In vitro cytotoxicity evaluation of HDAC inhibitor Apicidin in pancreatic carcinoma cells subsequent time and dose dependent treatment. Toxicology Letters, 236(1), 8-15
Open this publication in new window or tab >>In vitro cytotoxicity evaluation of HDAC inhibitor Apicidin in pancreatic carcinoma cells subsequent time and dose dependent treatment
2015 (English)In: Toxicology Letters, ISSN 0378-4274, E-ISSN 1879-3169, Vol. 236, no 1, p. 8-15Article in journal (Refereed) Published
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.

Keywords
Apicidin, Cytotoxicity, Colorimetric assay, Capan-1, Panc-1
National Category
Pharmacology and Toxicology
Identifiers
urn:nbn:se:hkr:diva-13905 (URN)10.1016/j.toxlet.2015.03.017 (DOI)000354289200002 ()25917448 (PubMedID)
Available from: 2015-05-22 Created: 2015-05-20 Last updated: 2018-01-11Bibliographically approved
El-Schich, Z., Mölder, A., Tassidis, H., Härkönen, P., Miniotis, M. F. & Gjörloff Wingren, A. (2015). Induction of morphological changes in death-induced cancer cells monitored by holographic microscopy. Journal of Structural Biology, 189(3), 207-212
Open this publication in new window or tab >>Induction of morphological changes in death-induced cancer cells monitored by holographic microscopy
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2015 (English)In: Journal of Structural Biology, ISSN 1047-8477, E-ISSN 1095-8657, Vol. 189, no 3, p. 207-212Article in journal (Refereed) Published
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.

Keywords
Digital holographic microscopy, Volume, Cell death, Viability, Cell morphology, Imaging
National Category
Cell and Molecular Biology
Identifiers
urn:nbn:se:hkr:diva-13491 (URN)10.1016/j.jsb.2015.01.010 (DOI)000351249500005 ()25637284 (PubMedID)
Available from: 2015-02-06 Created: 2015-02-06 Last updated: 2018-01-11Bibliographically approved
Tassidis, H., Brokken, L. J. S., Jirström, K., Bjartell, A., Ulmert, D., Härkönen, P. & Gjörloff Wingren, A. (2013). Low expression of SHP-2 is associated with less favourable outcome of prostate cancer. Tumor Biology, 34(2), 637-642
Open this publication in new window or tab >>Low expression of SHP-2 is associated with less favourable outcome of prostate cancer
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2013 (English)In: Tumor Biology, ISSN 1010-4283, E-ISSN 1423-0380, Vol. 34, no 2, p. 637-642Article in journal (Refereed) Published
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.

National Category
Cell and Molecular Biology
Identifiers
urn:nbn:se:hkr:diva-14765 (URN)10.1007/s13277-012-0590-1 (DOI)000316364500004 ()23192641 (PubMedID)
Available from: 2015-09-24 Created: 2015-09-24 Last updated: 2018-01-11Bibliographically approved
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