16 results on '"CYTOFLUOROMETRY"'
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2. TF — A novel cell-permeable and selective inhibitor of human protein kinase CK2 induces apoptosis in the prostate cancer cell line LNCaP
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Götz, Claudia, Gratz, Andreas, Kucklaender, Uwe, and Jose, Joachim
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PROTEIN kinases , *APOPTOSIS , *PROSTATE cancer , *CELL lines , *CAPILLARY electrophoresis , *CYTOFLUOROMETRY - Abstract
Abstract: Background: Abnormally high activity of protein kinase CK2 is linked to various diseases including cancer. Therefore, the inhibition of CK2 is a promising therapeutic strategy to fight this disease. Methods: We screened a library of synthetic molecules concerning their capacity to inhibit CK2. The activity of CK2 and their IC50 and Ki values were determined by a capillary electrophoresis assay. The effects of the inhibitor in a cell culture model were analyzed by cell counting, a viability assay, cytofluorimetry and Western blot. Results: The best CK2 inhibitor found in this screen was 6,7-dichloro-1,4-dihydro-8-hydroxy-4-[(4-methylphenylamino)methylen]dibenzo [b,d]furan-3(2H)-one, which we refer to as “TF”. TF showed tight binding to CK2 with low IC50 (29nM) and Ki (15nM) values. TF inhibited only seven out of 61 human kinases tested (>70% inhibition). Incubation of LNCaP cells with 50μM TF for 48h decreased the intracellular CK2 activity by 50%, confirming that the inhibitor is membrane permeable. The decrease in activity was correlated with a severe reduction in cell viability. The reduction in cell viability is at least partly due to the induction of apoptosis. General significance: In many cancers the protein kinase CK2 is significantly up-regulated and supports the neoplastic phenotype. New therapeutic strategies should be based on diverse reliable inhibitors to reverse the abnormal high levels to normal settings. [Copyright &y& Elsevier]
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- 2012
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3. Effect of Epithermal Neutrons on Viability of Glioblastoma Tumor Cells in Vitro.
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Mostovich, L. A., Gubanova, N. V., Kutsenko, O. S., Aleinik, V. I., Kuznetsov, A. S., Makarov, A. N., Sorokin, I. N., Taskaev, S. Yu., Nepomnyashchikh, G. I., and Grigor'eva, E. V.
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GLIOBLASTOMA multiforme , *CANCER cells , *CELL proliferation , *APOPTOSIS , *BORON-neutron capture therapy , *CYTOFLUOROMETRY - Abstract
We studied in vitro effect of epithermal neutrons in various doses on viability of glioblastoma U87 tumor cells. Increasing the dose from 1.9 to 4.1 Sv promoted cell death. Cytofluorimetric analysis revealed no activation of apoptosis in the irradiated cells, which attested to necrotic death of the tumor cells exposed to epithermal neutron radiation. [ABSTRACT FROM AUTHOR]
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- 2011
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4. P2X7 receptor activation induces cell death and microparticle release in murine erythroleukemia cells
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Constantinescu, Patrick, Wang, Bin, Kovacevic, Kati, Jalilian, Iman, Bosman, Giel J.C.G.M., Wiley, James S., and Sluyter, Ronald
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MONOCLONAL antibodies , *CELL death , *ADENOSINE triphosphate , *PURINERGIC receptors , *ERYTHROCYTES , *CANCER cells , *CYTOFLUOROMETRY - Abstract
Abstract: Extracellular ATP induces cation fluxes in and impairs the growth of murine erythroleukemia (MEL) cells in a manner characteristic of the purinergic P2X7 receptor, however the presence of P2X7 in these cells is unknown. This study investigated whether MEL cells express functional P2X7. RT-PCR, immunoblotting and immunofluorescence staining demonstrated the presence of P2X7 in MEL cells. Cytofluorometric measurements demonstrated that ATP induced ethidium+ uptake into MEL cells in a concentration-dependent fashion and with an EC50 of ∼154μM. The most potent P2X7 agonist 2′- and 3′-0(4-benzoylbenzoyl) ATP, but not ADP or UTP, induced ethidium+ uptake. ATP-induced ethidium+ and YO-PRO-12+ uptake were impaired by the P2X7 antagonist, A-438079. A colourmetric assay demonstrated that ATP impaired MEL cell growth. A cytofluorometric assay showed that ATP induced MEL cell death and that this process was impaired by A-438079. Finally, cytofluorometric measurements of Annexin-V binding and bio-maleimide staining demonstrated that ATP could induce rapid phosphatidylserine exposure and microparticle release in MEL cells respectively, both of which were impaired by A-438079. These results demonstrate that MEL cells express functional P2X7, and indicate that activation of this receptor may be important in the death and release of microparticles from red blood cells in vivo. [Copyright &y& Elsevier]
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- 2010
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5. Guidelines for the use and interpretation of assays for monitoring cell death in higher eukaryotes.
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Galluzzi, L., Aaronson, S.A., Abrams, J., Alnemri, E.S., Andrews, D.W., Baehrecke, E.H., Bazan, N.G., Blagosklonny, M.V., Blomgren, K., Borner, C., Bredesen, D.E., Brenner, C., Castedo, M., Cidlowski, J.A., Ciechanover, A., Cohen, G.M., Laurenzi, V. De, Maria, R. De, Deshmukh, M., and Dynlacht, B.D.
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CELL death , *THERAPEUTICS , *TISSUES , *DEATH (Biology) , *ORGANS (Anatomy) - Abstract
Cell death is essential for a plethora of physiological processes, and its deregulation characterizes numerous human diseases. Thus, the in-depth investigation of cell death and its mechanisms constitutes a formidable challenge for fundamental and applied biomedical research, and has tremendous implications for the development of novel therapeutic strategies. It is, therefore, of utmost importance to standardize the experimental procedures that identify dying and dead cells in cell cultures and/or in tissues, from model organisms and/or humans, in healthy and/or pathological scenarios. Thus far, dozens of methods have been proposed to quantify cell death-related parameters. However, no guidelines exist regarding their use and interpretation, and nobody has thoroughly annotated the experimental settings for which each of these techniques is most appropriate. Here, we provide a nonexhaustive comparison of methods to detect cell death with apoptotic or nonapoptotic morphologies, their advantages and pitfalls. These guidelines are intended for investigators who study cell death, as well as for reviewers who need to constructively critique scientific reports that deal with cellular demise. Given the difficulties in determining the exact number of cells that have passed the point-of-no-return of the signaling cascades leading to cell death, we emphasize the importance of performing multiple, methodologically unrelated assays to quantify dying and dead cells.Cell Death and Differentiation (2009) 16, 1093–1107; doi:10.1038/cdd.2009.44; published online 17 April 2009 [ABSTRACT FROM AUTHOR]
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- 2009
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6. Histone deacetylase inhibitors induce cell death and enhance the apoptosis-inducing activity of TRAIL in Ewing’s sarcoma cells.
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Sonnemann, Jürgen, Dreyer, Linn, Hartwig, Maite, Palani, Chithra, Le Hong, Klier, Ulrike, Bröker, Barbara, Völker, Uwe, and Beck, James
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HISTONE deacetylase , *CELL death , *APOPTOSIS , *EWING'S sarcoma , *CYTOFLUOROMETRY - Abstract
The present in vitro study was conducted to evaluate the effects of the histone deacetylase inhibitors (HDIs) suberoyl anilide hydroxamic acid (SAHA), sodium butyrate (NaB) and MS-275 applied as single agents or in combination with TRAIL in Ewing’s sarcoma. Cytotoxic activities were assessed by cytofluorometric analysis of propidium iodide uptake, DNA fragmentation and mitochondrial depolarisation as well as by measuring caspase-9 and -3 activities. Cell-surface expression of TRAIL receptors was determined by cytofluorometry, and histone H4 acetylation was assessed by western blot. All three HDIs potently induced cell death in the two cell lines explored, SK-ES-1 and WE-68. However, they seemed to differ in their modes of action. SAHA and NaB induced mitochondrial depolarisation as well as caspase-9 and -3 activities, and their cytotoxic effects could be significantly reduced by the pan-caspase inhibitor z-VAD-fmk. MS-275 was a much weaker inducer of caspase-9 and -3 activities as well as mitochondrial injury; consistently, z-VAD-fmk had little effect on MS-275-mediated activities. Combined treatment of HDIs and TRAIL led to an additive effect in SK-ES-1 cells and a supra-additive effect in WE-68 cells. Yet, HDIs did not increase cell-surface expression of TRAIL receptor 2, but rather decreased it. Selective inhibition of caspase-8 in WE-68 cells and HDI treatment of CADO-ES-1 cells, a Ewing's sarcoma cell line deficient in caspase-8 expression, revealed that caspase-8 was not required for HDI-mediated apoptosis. These results suggest that HDIs may be considered as a novel treatment strategy for Ewing’s sarcoma either applied as monotherapy or in combination with TRAIL. [ABSTRACT FROM AUTHOR]
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- 2007
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7. Intrahepatic CD4+ T-Cell Apoptosis is Related to METAVIR Score in Patients With Chronic Hepatitis C Virus.
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Roger, P.-M., Chaillou, S., Breittmayer, J.-P., Dahman, M., St. Paul, M.-C., Chevallier, P., Benzaken, S., Ticchioni, M., Bernard, A., Dellamonica, P., and Tran, A.
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HEPATITIS C virus , *APOPTOSIS , *T cells , *CYTOFLUOROMETRY , *IMMUNOLOGY - Abstract
Hepatitis C virus (HCV) infection leads to liver injury, which is thought to be immune-mediated. Apoptosis of hepatic T cells could influence histological damage. We quantified peripheral and intrahepatic T-cell apoptosis in 28 patients with chronic hepatitis C by using cytofluorometric techniques. METAVIR score and HCV plasma viral load were determined. Six liver biopsies, obtained from controls without chronic hepatitis during hepatobiliary surgery, served as controls. In patients, liver T-cell apoptosis was upregulated compared to peripheral T cells: 35 versus 7% for CD4+ and 56 versus 13% for CD8+ T cells ( P < 0.001). Liver T-cell apoptosis levels from patients were increased compared to controls for both CD4+ ( P = 0.041) and CD8+ T cells ( P = 0.007). Nine patients exhibiting METAVIR scores A and F ≤1 showed higher intrahepatic CD4+ T-cell apoptosis compared to the 19 patients with a higher METAVIR score ( P = 0.001) and both histological activity and fibrosis were related to apoptosis level. There was also an inverse relationship between the level of intrahepatic CD8+ T-cell apoptosis and serum transaminase activity ( P = 0.023). Our study shows immune compartmentalization, suggesting that the study of peripheral blood lymphocytes may not be fully relevant to the pathophysiology of HCV hepatitis, and that the severity of liver injury is inversely correlated with intrahepatic CD4+ T-cell apoptosis. [ABSTRACT FROM AUTHOR]
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- 2005
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8. Dynamic analysis of apoptosis in primary cortical neurons by fixed- and real-time cytofluorometry.
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Lecoeur, H., Chauvier, D., Langonné, A., Rebouillat, D., Brugg, B., Mariani, J., Edelman, L., and Jacotot, E.
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APOPTOSIS ,CELL death ,CYTOLOGICAL techniques ,BIOLOGY education ,FLOW cytometry ,FLUORESCENT probes - Abstract
We describe here a cytofluorometric technology for the characterization of decision, execution, and degradation steps of neuronal apoptosis. Multiparametric flow cytometry was developped and combined to detailled fluorescence microscopy observations to establish the chronology and hierarchy of death-related events: neuron morphological changes, mitochondrial transmembrane potential (Δ Ψ
m ) collapse, caspase-3 and -9 activation, phosphatidyl-serine exposure, nuclear dismantling and final plasma membrane permeabilization. Moreover, we developped a reliable real-time flow cytometric monitoring of Δ Ψm and plasma membrane integrity in response to neurotoxic insults including MPTP treatment. Taking advantage of recently developped specific fluorescent probes and a third generation pan-caspase inhibitor, this integrated approach will be pertinent to study the cell biology of neuronal apoptosis and to characterize new neuro-toxic/protective molecules. [ABSTRACT FROM AUTHOR]- Published
- 2004
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9. Cytofluorometric quantitation of apoptosis-driven inner mitochondrial membrane permeabilization.
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Poncet, D., Boya, P., Métivier, D., Zamzami, N., and Kroemer, G.
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APOPTOSIS ,CELL death ,MITOCHONDRIAL membranes ,CELLS ,CYTOFLUOROMETRY - Abstract
The mitochondrial matrix can be specifically labeled by loading cells with calcein and simultaneous quenching of the non-mitochondrial calcein fluorescence with cobalt (Co
2+ ). Positive staining of mitochondria thus requires that the inner mitochondrial membrane functions as a barrier separating calcein (within the matrix) from Co2+ (outside of the matrix). Upon induction of apoptosis, such calcein/Co2+ -labeled cells, demonstrate a decrease in the overall calcein fluorescence resulting from inner mitochondrial membrane permeabilization. This decrease can be quantified by cytofluorometry and can be dissociated from other apoptosis-associated mitochondrial perturbations such as the loss of the mitochondrial transmembrane potential (ΔΨm ), the local overproduction of reactive oxygen species, and the mitochondrial release of cytochrome c. In some paradigms of apoptosis the loss of calcein/Co2+ (CC) staining can be dissociated from the ΔΨm loss, both of which may occur in a caspase-dependent or caspase-independent fashion, depending on the apoptosis inducer. Importantly, inner membrane permeabilization to CC may occur without a permanent ΔΨm dissipation in apoptosis, suggesting that transient permeabilization events could participate at the apoptotic cascade. Altogether, our data demonstrate that inner mitochondrial membrane permeabilization constitutes an early event in the apoptotic cascade. [ABSTRACT FROM AUTHOR]- Published
- 2003
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10. Versatility of analytical capabilities of laser scanning cytometry (LSC)
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Grabarek, Jerzy and Darzynkiewicz, Zbigniew
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CYTOFLUOROMETRY , *CELL cycle , *LASERS in biochemistry - Abstract
The microscope-based cytofluorometer laser scanning cytometer (LSC) combines many attributes of flow- and image-cytometry. Laser-excited fluorescence emitted from individual cells is measured at multiple wavelengths, rapidly, with high sensitivity and accuracy. In this review the following analytical capabilities of LSC are discussed: (a) analysis of hyperchromicity of nuclear DNA to identify cell types that differ in chromatin condensation, mitotic or apoptotic cells; (b) topographic distribution of fluorescence within the cell, e.g., cytoplasm vs. nucleus, nucleoplasm vs. nucleolus, translocation of regulatory molecules such as NF-κB, p53, Bax; (c) analysis of micronuclei in mutagenicity assays; (d) fluorescence in situ hybridization (FISH); (e) morphometry and enumeration of nucleoli; (f) analysis of progeny of individual cells in clonogenicity assay; (g) cell immunophenotyping; (h) relocation of the measured cell for visual examination, imaging or sequential analysis using different immunochemical or cytochemical stains, or genetic probes; (i) analysis of in situ enzyme kinetics and other time resolved processes; (j) analysis of tissue section architecture. Other advantages and limitations of LSC are discussed and compared with flow cytometry. [Copyright &y& Elsevier]
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- 2002
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11. In vitro induction of apoptosis vs. necrosis by widely used preservatives: 2-phenoxyethanol, a mixture of isothiazolinones, imidazolidinyl urea and 1,2-pentanediol
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Anselmi, Cecilia, Ettorre, Anna, Andreassi, Marco, Centini, Marisanna, Neri, Paolo, and Di Stefano, Anna
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CYTOFLUOROMETRY , *APOPTOSIS , *NECROSIS - Abstract
Preservatives are added to many final products, such as detergents, cosmetics, pharmaceuticals and vaccines. We conducted an in vitro investigation of the apoptosis- and necrosis-inducing potential of brief applications (10 min) of four common preservatives: ethylene glycol monophenyl ether, 2-phenoxyethanol (EGPE), imidazolidinyl urea (IMU), a mixture of 5-chloro-2-methyl-4-isothiazolin-3-one and 2-methyl-4-isothiazolin-3-one (CMI/MI), and 1,2-pentanediol, a “preservative-non-preservative” best known as pentylene glycol. Using HL60 cells, we monitored the kinetics of cell toxicity with the MTT test and analysed extranuclear end points of apoptosis, i.e. phosphatidylserine exposure and nuclear fragmentation. Preservative treatment resulted in a dose-dependent decrease of cell viability. The mode of cell death was dose-dependent: necrosis occurred at high concentrations while apoptosis, shown by DNA laddering, DNA sub-diploid peak and caspase-3 activation, occurred at lower concentrations 0–24 hr after exposure to a single dose: CMI/MI induced apoptosis at low concentrations (0.001–0.01%) and necrosis at high concentrations (0.5–0.1%); IMU and EGPE required higher concentrations to induce apoptosis (IMU 0.01–0.1% and EGPE 0.01–0.5%) or necrosis (IMU 0.5–1% and EGPE only at 1%). PG induced apoptosis only at 5%. Externalization of PS, a hallmark of apoptosis, occurred early in HL60 treated with low concentrations of CMI/MI and EGPE and was concomitant with the subdiploid peak in HL60 treated with PG. However, it did not occur in HL60 treated with IMU. In conclusion, at appropriate concentrations, each of the four preservatives modulates the apoptotic machinery by a caspase-dependent mechanism. Thus, apoptosis could be a good parameter to evaluate the cytoxicity of these chemical compounds. [Copyright &y& Elsevier]
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- 2002
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12. Change in Functional State of Bone Marrow-Derived Mesenchymal Stem Cells After Incubation with Silver Nanoparticles
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E. V. Pavlovich, M. S. Yukhta, Nataliia Volkova, and Anatoliy N. Goltsev
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Necrosis ,Apoptosis ,Annexin ,02 engineering and technology ,Mitochondrion ,010402 general chemistry ,01 natural sciences ,In vitro ,Suspension ,medicine ,Incubation ,Inhibition ,Mesenchymal stem cell ,021001 nanoscience & nanotechnology ,Mitochondria ,0104 chemical sciences ,Cell biology ,medicine.anatomical_structure ,Toxicity ,Cytofluorometry ,Mesenchymal stem cells ,Bone marrow ,Silver nanoparticles ,medicine.symptom ,0210 nano-technology ,7AAD - Abstract
Volkova, N.A., Yukhta, M.S., Pavlovich, E.V., Goltsev, A.N. (2019). Change in Functional State of Bone Marrow-Derived Mesenchymal Stem Cells After Incubation with Silver Nanoparticles. In: Fesenko, O., Yatsenko, L. (eds) Nanophotonics, Nanooptics, Nanobiotechnology, and Their Applications. NANO 2018. Springer Proceedings in Physics, vol 222. Springer, Cham. https://doi.org/10.1007/978-3-030-17755-3_19 Despite of silver nanopaticles’ (AgNPs) widespread use, there is a serious lack of information concerning the toxicity of AgNPs to humans and their key cellular actions. The aim of the present study was an effect of different concentrations of 40 nm AgNPs and time of incubation on the viability, CD 44 expression, mitochondrial state, and apoptotic/necrotic processes in bone marrow-derived mesenchymal stem cells (MSCs). The obtained results suggested that 1-hour incubation with AgNPs in the concentrations of 2 and 4 μg/ml did not affect the viability and content of CD44-positive cells, as well as did not cause the development of necrosis/apoptosis processes and alteration of mitochondrial activity in MSCs. After AgNPs’ addition in the concentrations of 6 and 10 μg/ml there were a decrease of mitochondrial activity, percentage of viability cells and an increase of the number of apoptotic cells compared with the control samples of MSCs. An increase in the period of incubation with AgNPs (4–10 μg/ml) up to 1 day leads to a toxic effect on MSCs, which was manifested in the decrease of viability, content of CD44-positive cells (AgNPs 10 μg/ml), mitochondrial activity, and activation of apoptosis and necrosis. The obtained results are related to the field of applied nanotechnology, which extends to clinical medicine, especially in the development of addressed drug delivery to the target cells or organs.
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- 2019
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13. The Cell Membrane is the Main Target of Resveratrol as Shown by Interdisciplinary Biomolecular/Cellular and Biophysical Approaches
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Gianfranco Risuleo, Marisa Colone, Adalberto Bonincontro, Annarita Stringaro, and G. L. Milardi
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Cell Survival ,Physiology ,Cytotoxicity ,Cell ,Biophysics ,Apoptosis ,Phosphatidylserines ,Resveratrol ,Cell Line ,Cell membrane ,Dose-Response Relationship ,chemistry.chemical_compound ,Mice ,Cytofluorometry ,Electrorotation ,Animals ,Biological Transport ,Cell Cycle ,Cell Membrane ,Dose-Response Relationship, Drug ,Kinetics ,Stilbenes ,Cell Biology ,medicine ,Membrane structure ,food and beverages ,Cell cycle ,Cell biology ,Membrane ,medicine.anatomical_structure ,chemistry ,Drug ,Function (biology) - Abstract
One of the research lines developed in our laboratory is focused on the study of the bioactivity of natural substances. Resveratrol (RV) is a polyphenol nonflavonoid compound present in a number of plant species but mainly in the berries of the red grape Vitis vinifera. The powerful antioxidant action of this molecule is well documented. In this work we evaluated the effects of this substance by adopting diverse experimental strategies. In particular, we studied the effects on cell vitality and cycle by MTT and cytofluorimetric assays. In addition, we explored the action of RV on the cell membrane by a well-consolidated biophysical approach: electrorotation. This technique allows assessment of the structure/function of the cell membrane. The results presented here demonstrate that RV shows a modest effect on the biological properties of the cell in terms of cytotoxicity and cell cycle alterations. On the contrary, a significant effect on the membrane structure/function was observed, consisting of an enhanced intramembrane ion transport. The implications and interpretation of these membrane alterations are discussed.
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- 2014
14. Guidelines for the use and interpretation of assays for monitoring cell death in higher eukaryotes
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Aaron Ciechanover, Eric H. Baehrecke, Josef M. Penninger, Moshe Oren, Marja Jäättelä, Cecília M. P. Rodrigues, Seamus J. Martin, Lorenzo Galluzzi, Dale E. Bredesen, Stuart A. Aaronson, Donald W. Nicholson, Frank Madeo, Mikhail V. Blagosklonny, Gabriel Núñez, Hans-Uwe Simon, Adi Kimchi, Karen H. Vousden, Yoshihide Tsujimoto, David W. Andrews, Simone Fulda, J. Tschopp, John M. Abrams, Hinrich Gronemeyer, Nicolas G. Bazan, Michael O. Hengartner, Richard A. Flavell, Beth Levine, Thomas Rudel, Ilio Vitale, Eugenia Morselli, Rosario Rizzuto, Boris Zhivotovsky, Douglas R. Green, J. M. Hardwick, Maria Castedo, Guido Kroemer, Pierluigi Nicotera, Christoph Borner, David C. Rubinsztein, Junying Yuan, Jan Paul Medema, Oliver Kepp, Carmen Garrido, V De Laurenzi, Jean-Christophe Marine, Richard J. Youle, Hidenori Ichijo, Daniel J. Klionsky, Hamsa Puthalakath, Ute M. Moll, Shigekazu Nagata, R De Maria, Pierre Golstein, Marie-Lise Gougeon, Mohanish Deshmukh, Enrico Lugli, Brian David Dynlacht, Emad S. Alnemri, John A. Cidlowski, Luca Scorrano, Stuart A. Lipton, Hermann Steller, Sally Kornbluth, Gerry Melino, György Hajnóczky, Gabriel A. Rabinovich, Peter Vandenabeele, Gerald M. Cohen, Shazib Pervaiz, Marcus E. Peter, Richard A. Knight, Jochen H. M. Prehn, Sharad Kumar, Klas Blomgren, Walter Malorni, Wafik S. El-Deiry, Patrick Mehlen, Mauro Piacentini, Catherine Brenner, Apoptose, cancer et immunité (U848), Université Paris-Sud - Paris 11 (UP11)-Institut Gustave Roussy (IGR)-Institut National de la Santé et de la Recherche Médicale (INSERM), Department of Oncological Sciences, Icahn School of Medicine at Mount Sinai [New York] (MSSM), Department of Cell Biology, University of Texas Southwestern Medical Center [Dallas], Department of Biochemistry and Molecular Biology, Thomas Jefferson University-Sidney Kimmel Cancer Center, Jefferson (Philadelphia University + Thomas Jefferson University)-Jefferson (Philadelphia University + Thomas Jefferson University), Department of Biochemistry and Biomedical Sciences, McMaster University [Hamilton, Ontario], Department of Cancer Biology, University of Massachusetts Medical School [Worcester] (UMASS), University of Massachusetts System (UMASS)-University of Massachusetts System (UMASS), Neuroscience Center of Excellence, LSU Health Sciences Center, Roswell Park Cancer Institute [Buffalo] (RPCI), Center for Brain Repair and Rehabilitation, Institute of Neuroscience and Physiology [Göteborg]-University of Gothenburg (GU), Department of Pediatric Oncology, The Queen Silvia Children's Hospital, Institute of Molecular Medicine and Cell Research (ZBMZ), University of Freiburg [Freiburg], Buck Institute for Age Research, Laboratoire de génétique et biologie cellulaire (LGBC), Université de Versailles Saint-Quentin-en-Yvelines (UVSQ)-École Pratique des Hautes Études (EPHE), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL), National Institutes of Environmental Health Sciences, National Institutes of Health [Bethesda] (NIH), Vascular and Tumor Biology Research Center, Israel Institute of Technology, Toxicology Unit, University of Leicester, Dipartimento di Scienze Biomediche, Università degli studi 'G. d'Annunzio' Chieti-Pescara [Chieti-Pescara] (Ud'A), Department of Hematology, Oncology and Molecular Medicine, Istituto Superiore di Sanità (ISS), Mediterranean Institute of Oncology, Department of Cell and Developmental Biology, University of North Carolina [Chapel Hill] (UNC), University of North Carolina System (UNC)-University of North Carolina System (UNC), Department of Pathology, New York University School of Medicine, NYU System (NYU)-NYU System (NYU), Hematology-Oncology Division, Perelman School of Medicine, University of Pennsylvania-University of Pennsylvania, Section of Immunobiology, Yale School of Medicine [New Haven, Connecticut] (YSM), Howard Hughes Medical Institute [Chevy Chase] (HHMI), Howard Hughes Medical Institute (HHMI), University Children's Hospital, Lipides - Nutrition - Cancer (U866) (LNC), Université de Bourgogne (UB)-Institut National de la Santé et de la Recherche Médicale (INSERM)-AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement-Ecole Nationale Supérieure de Biologie Appliquée à la Nutrition et à l'Alimentation de Dijon (ENSBANA), Centre d'Immunologie de Marseille - Luminy (CIML), Aix Marseille Université (AMU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Immunité Antivirale, Biothérapie et Vaccins, Institut Pasteur [Paris] (IP)-Institut National de la Santé et de la Recherche Médicale (INSERM), Department of Immunology, St Jude Children's Research Hospital, Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), Université de Strasbourg (UNISTRA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Department of Pathology, Anatomy and Cell Biology, Thomas Jefferson University, Department of Pharmacology and Molecular Sciences, Johns Hopkins University (JHU), Institute of Molecular Biology, Universität Zürich [Zürich] = University of Zurich (UZH), Graduate School of Medecine, The University of Tokyo (UTokyo), Danish Cancer Society, Institute of Cancer Biology, Department of Molecular Genetics, Weizmann Institute of Science [Rehovot, Israël], Life Sciences Institute and Department of Molecular, Cellular, and Developmental Biology and Biological Chemistry, University of Michigan [Ann Arbor], University of Michigan System-University of Michigan System, Institute of Child Health [London], University College of London [London] (UCL), Duke University School of Medicine, Centre for Cancer Biology, Hanson Institute, Adelaide, Burnham Institute for Medical Research, The Salk Institute for Biological Studies, The Scripps Research Institute [La Jolla, San Diego], University of California [San Diego] (UC San Diego), University of California (UC), Immunotechnology Section, Vaccine Research Center, National Institutes of Health [Bethesda] (NIH)-National Institute of Allergy and Infectious Diseases, Institute of Molecular Biosciences, Karl-Franzens-Universität Graz, Department of Therapeutic Research and Medicines Evaluation, Laboratory for Molecular Cancer Biology, VIB-UGent, Department for Molecular Biology, Universiteit Gent = Ghent University (UGENT), Department of Genetics, Trinity College Dublin, Center for Experimental and Molecular Medicine, Academic Medical Center - Academisch Medisch Centrum [Amsterdam] (AMC), University of Amsterdam [Amsterdam] (UvA)-University of Amsterdam [Amsterdam] (UvA), University of Amsterdam [Amsterdam] (UvA), Apoptosis, Cancer, and Development Laboratory, Centre Léon Bérard [Lyon], Apoptose Cancer et Développement, Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS), Department of Experimental Medicine and Biochemical Sciences, Università degli Studi di Roma Tor Vergata [Roma], Stony Brook University [SUNY] (SBU), State University of New York (SUNY)-State University of New York (SUNY), Department of Molecular Oncology, Göttingen Center of Molecular Biosciences, Faculty of Medicine, Georg-August-University = Georg-August-Universität Göttingen, Fujitsu Laboratories LTD., Fujitsu Laboratories Ltd., Department of Medical Chemistry, Kyoto University-Graduate School of Medicine, Merck & Co. Inc, University of Michigan Medical School [Ann Arbor], Department of Molecular Cell Biology [Rehovot], Institute of Molecular Biotechnology, Austrian Academy of Sciences (OeAW), Department of Physiology, National University of Singapore (NUS)-Yong Loo Lin School of Medicine-Graduate School for Integrative Sciences and Engineering, Singapore-MIT Alliance for Research and Technology (SMART), Massachusetts Institute of Technology (MIT), Duke-NUS Medical School [Singapore], Ben May Department for Cancer Research, University of Chicago-Ben May Department for Cancer Research, Laboratory of Cell Biology, National Institute for Infectious Diseases IRCCS 'L. Spallanzani', Department of Biology, Department of Physiology and Medical Physics, Royal College of Surgeons in Ireland (RCSI), Department of Biochemistry, La Trobe University [Melbourne], Laboratorie de Inmunopatologia, Instituto de Biología y Medicina Experimental [Buenos Aires] (IBYME), Consejo Nacional de Investigaciones Científicas y Técnicas [Buenos Aires] (CONICET)-Consejo Nacional de Investigaciones Científicas y Técnicas [Buenos Aires] (CONICET), Department of Biomedical Sciences, Università degli Studi di Padova = University of Padua (Unipd), iMed.UL, Universidade de Lisboa = University of Lisbon (ULISBOA), Cambridge Institute for Medical Research (CIMR), University of Cambridge [UK] (CAM), Biocenter, Julius-Maximilians-Universität Würzburg (JMU), Department of Cell Physiology and Metabolism, University of Geneva Medical School, Dulbecco-Telethon Institute, Venetian Institute Molecular Medicine (VIMM), University of Bern, Laboratory of Apoptosis and Cancer Biology, Rockefeller University [New York], Department of Biochemistry [Lausanne], Université de Lausanne = University of Lausanne (UNIL), Department of Medical Genetics, Osaka University Medical School, Department for Molecular Biomedical Research, The Beatson Institute for Cancer Research, University of Glasgow, Biochemistry Section, Surgical Neurology Branch, National Institutes of Health [Bethesda] (NIH)-National Institute of Neurological Disorders and Stroke, Department of cell biology, Harvard Medical School [Boston] (HMS), Division of Toxicology, karolinska institute-Institute of Environmental Medicine, Scorrano, Luca, Tschopp, Jean-Marie, Apoptose, cancer et immunité ( U848 ), Université Paris-Sud - Paris 11 ( UP11 ) -Institut Gustave Roussy ( IGR ) -Institut National de la Santé et de la Recherche Médicale ( INSERM ), Mount Sinai School of Medicine, Thomas Jefferson University-Kimmel Cancer Institute, University of Massachusetts Medical School [Worcester] ( UMASS ), Roswell Park Cancer Institute [Buffalo], Institute of Neuroscience and Physiology [Göteborg]-University of Gothenburg ( GU ), Institute of Molecular Medicine and Cell Research ( ZBMZ ), Albert-Ludwigs University, Laboratoire de génétique et biologie cellulaire ( LGBC ), Université de Versailles Saint-Quentin-en-Yvelines ( UVSQ ) -École pratique des hautes études ( EPHE ) -Centre National de la Recherche Scientifique ( CNRS ), National Institutes of Health ( NIH ), Università degli studi 'G. d'Annunzio' Chieti-Pescara [Chieti-Pescara] ( Ud'A ), Istituto Superiore di Sanita [Rome], The University of North Carolina at Chapel Hill, University of Pennsylvania School of Medicine, Yale School of Medicine, Howard Hughes Medical Institute, Howard Hugues Medical Institute, Lipides - Nutrition - Cancer (U866) ( LNC ), Université de Bourgogne ( UB ) -Institut National de la Santé et de la Recherche Médicale ( INSERM ) -AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement-Ecole Nationale Supérieure de Biologie Appliquée à la Nutrition et à l'Alimentation de Dijon ( ENSBANA ), Centre d'Immunologie de Marseille - Luminy ( CIML ), Aix Marseille Université ( AMU ) -Institut National de la Santé et de la Recherche Médicale ( INSERM ) -Centre National de la Recherche Scientifique ( CNRS ), Institut Pasteur [Paris]-Institut National de la Santé et de la Recherche Médicale ( INSERM ), St. Jude Children's Research Hospital, Institut de Génétique et de Biologie Moléculaire et Cellulaire ( IGBMC ), Université de Strasbourg ( UNISTRA ) -Institut National de la Santé et de la Recherche Médicale ( INSERM ) -Centre National de la Recherche Scientifique ( CNRS ), Johns Hopkins University ( JHU ), University of Zürich [Zürich] ( UZH ), The University of Tokyo, Weizmann Institute of Science, University College of London [London] ( UCL ), The Scripps Research Institute, University of California [San Diego] ( UC San Diego ), National Institutes of Health ( NIH ) -National Institute of Allergy and Infectious Diseases, University of Graz, Ghent University [Belgium] ( UGENT ), Academic Medical Center [Amsterdam] ( AMC ), University of Amsterdam [Amsterdam] ( UvA ) -University of Amsterdam [Amsterdam] ( UvA ), University of Amsterdam [Amsterdam] ( UvA ), Université Claude Bernard Lyon 1 ( UCBL ), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique ( CNRS ), Stony Brook University [The State University of New York] ( SBU ), University of Göttingen, Kyoto University [Kyoto]-Graduate School of Medicine, Merck and Co [Rahway], University of Michigan Medical School, Austrian Academy of Sciences ( OeAW ), National University of Singapore ( NUS ) -Yong Loo Lin School of Medicine-Graduate School for Integrative Sciences and Engineering, Singapore-MIT Alliance, National University of Singapore ( NUS ), Duke-NUS Graduate Medical School, Royal College of Surgeons in Ireland, Instituto de Biología y Medicina Experimental (IBYME- CONICET), Universita degli Studi di Padova = University of Padua = Université de Padoue, University of Lisbon, Cambridge Institute for Medical Research, University of Würzburg, Venetian Institute of Molecular Medicine, The Rockefeller University, Université de Lausanne ( UNIL ), Vib Ghent University, National Institutes of Health ( NIH ) -National Institute of Neurological Disorders and Stroke, Harvard Medical School [Boston] ( HMS ), Université de Versailles Saint-Quentin-en-Yvelines (UVSQ), University of Pennsylvania [Philadelphia]-University of Pennsylvania [Philadelphia], Yale University School of Medicine, Institut Pasteur [Paris]-Institut National de la Santé et de la Recherche Médicale (INSERM), Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université de Strasbourg (UNISTRA), University of California, Karl-Franzens-Universität [Graz, Autriche], Universiteit Gent = Ghent University [Belgium] (UGENT), Georg-August-University [Göttingen], Universita degli Studi di Padova, Universidade de Lisboa (ULISBOA), Julius-Maximilians-Universität Würzburg [Wurtzbourg, Allemagne] (JMU), Université de Lausanne (UNIL), Université de Versailles Saint-Quentin-en-Yvelines (UVSQ)-École pratique des hautes études (EPHE), Peney, Maité, Galluzzi, L, Aaronson, SA, Abrams, J, Alnemri, ES, Kumar, Sharad, and Kroemer, Guido
- Subjects
MESH: Cell Death ,cytofluorometry ,MESH : Microscopy, Fluorescence ,ved/biology.organism_classification_rank.species ,Cell ,MESH: Flow Cytometry ,MESH: Microscopy, Fluorescence ,Apoptosis ,fluorescence microscopy ,MESH: Eukaryotic Cells ,Annexin V ,necrosis ,0302 clinical medicine ,Eukaryotic Cells/cytology ,Mitochondrial membrane permeabilization ,Scanning ,MESH : Immunoblotting ,Genetics ,Cell Death ,Flow Cytometry ,Guidelines as Topic ,Humans ,Immunoblotting ,Microscopy, Electron, Scanning ,Microscopy, Fluorescence ,Spectrometry, Fluorescence ,0303 health sciences ,Microscopy ,MESH : Spectrometry, Fluorescence ,MESH: Immunoblotting ,MESH: Guidelines as Topic ,purl.org/becyt/ford/3.1 [https] ,Bioquímica y Biología Molecular ,3. Good health ,Tunel ,Medicina Básica ,medicine.anatomical_structure ,Eukaryotic Cells ,caspases ,030220 oncology & carcinogenesis ,purl.org/becyt/ford/3 [https] ,MESH: Spectrometry, Fluorescence ,MESH : Microscopy, Electron, Scanning ,Programmed cell death ,autophagy ,CIENCIAS MÉDICAS Y DE LA SALUD ,MESH: Microscopy, Electron, Scanning ,MESH : Flow Cytometry ,caspase ,Computational biology ,Biology ,Electron ,Fluorescence ,Article ,03 medical and health sciences ,Settore MED/04 - PATOLOGIA GENERALE ,medicine ,[SDV.BBM] Life Sciences [q-bio]/Biochemistry, Molecular Biology ,[SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology ,Model organism ,ddc:612 ,mitotic catastrophe ,Molecular Biology ,[ SDV.BBM ] Life Sciences [q-bio]/Biochemistry, Molecular Biology ,MESH : Guidelines as Topic ,030304 developmental biology ,cell death ,Oxidative stress ,MESH: Humans ,ved/biology ,Spectrometry ,Interpretation (philosophy) ,MESH: Apoptosis ,MESH : Eukaryotic Cells ,MESH : Humans ,Cell Biology ,immunofluorescence microscopy ,MESH : Cell Death ,Cancer cell ,MESH : Apoptosis - Abstract
Cell death is essential for a plethora of physiological processes, and its deregulation characterizes numerous human diseases. Thus, the in-depth investigation of cell death and its mechanisms constitutes a formidable challenge for fundamental and applied biomedical research, and has tremendous implications for the development of novel therapeutic strategies. It is, therefore, of utmost importance to standardize the experimental procedures that identify dying and dead cells in cell cultures and/or in tissues, from model organisms and/or humans, in healthy and/or pathological scenarios. Thus far, dozens of methods have been proposed to quantify cell death-related parameters. However, no guidelines exist regarding their use and interpretation, and nobody has thoroughly annotated the experimental settings for which each of these techniques is most appropriate. Here, we provide a nonexhaustive comparison of methods to detect cell death with apoptotic or nonapoptotic morphologies, their advantages and pitfalls. These guidelines are intended for investigators who study cell death, as well as for reviewers who need to constructively critique scientific reports that deal with cellular demise. Given the difficulties in determining the exact number of cells that have passed the point-of-no-return of the signaling cascades leading to cell death, we emphasize the importance of performing multiple, methodologically unrelated assays to quantify dying and dead cells. Fil: Galluzzi, L.. Inserm; Francia. Universite Paris Sud; Francia. Institut Gustave Roussy; Francia Fil: Aaronson, S. A.. Mount Sinai School of Medicine; Estados Unidos Fil: Abrams, J.. University of Texas. Southwestern Medical Center; Estados Unidos Fil: Alnemri, E. S.. Thomas Jefferson University; Estados Unidos Fil: Andrews, D. W.. McMaster University; Canadá Fil: Baehrecke, E. H.. University of Massachussets; Estados Unidos Fil: Bazan, N. G.. Louisiana State University Health Sciences Center; Estados Unidos Fil: Blagosklonny, M. V.. Roswell Park Cancer Institute; Estados Unidos Fil: Blomgren, K.. Universityt of Gothenburg; Suecia. The Queen Silvia Children; Suecia Fil: Borner, C.. Albert-Ludwigs Universität Freiburg; Alemania Fil: Bredesen, E.. Buck Institute for Age Research; Estados Unidos. University of California; Estados Unidos Fil: Brenner, C.. univeristy of Versailles ; Francia Fil: Castedo, M.. Inserm; Francia. Universite Paris Sud; Francia Fil: Cidlowski, J. A.. National Institutes of Health; Estados Unidos Fil: Ciechanover, A.. The Rappaport Faculty of Medicine; Israel Fil: Cohen, G. M.. University of Leicester; Reino Unido Fil: De Laurenzi, V.. Università ‘G. d’Annunzio’ Chieti Pescara; Italia Fil: De Maria, R.. Istituto Superiore di Sanità; Italia. Mediterranean Institute of Oncology; Italia Fil: Deshmukh, M.. University of North Carolina; Estados Unidos Fil: Dynlacht, B. D.. University of New York; Estados Unidos Fil: El Deiry, W. S.. University of Pennsylvania; Estados Unidos Fil: Flavell, R. A.. University of Yale; Estados Unidos Fil: Fulda, S.. University Children; Alemania Fil: Garrido, C.. Inserm; Francia. University of Burgundy; Francia Fil: Golstein, P.. Inserm; Francia. Aix Marseille Université; Francia Fil: Gougeon, M. L.. Instituto Pasteur; Francia Fil: Green, D. R.. St. Jude Children′s Research Hospital; Estados Unidos Fil: Gronemeyer, H.. Institut de Génétique et de Biologie Moléculaire et Cellulaire; Francia. Inserm; Francia Fil: Hajnóczky, G.. Thomas Jefferson University; Estados Unidos Fil: Hardwick, J. M.. Johns Hopkins University; Estados Unidos Fil: Hengartner, M.O.. University Johns Hopkins; Estados Unidos Fil: Ichijo, H.. University of Tokyo; Japón Fil: Jäättelä, M.. Institute of Cancer Biology; Dinamarca Fil: Kepp, O.. Inserm; Francia. Universite Paris Sud; Francia. Institut Gustave Roussy; Francia Fil: Kimchi, A.. Weizmann Institute of Science; Israel Fil: Klionsky, D. J.. University of Michigan; Estados Unidos Fil: Knight, R. A.. University College London; Estados Unidos Fil: Kornbluth, S.. University of Duke; Estados Unidos Fil: Kumar, S.. Hanson Institute; Australia Fil: Levine, B.. Howard Hughes Medical Institute; Estados Unidos. University of Texas; Estados Unidos Fil: Lipton, S. A.. Burnham Institute for Medical Research; Estados Unidos. The Salk Institute for Biological Studies; Estados Unidos. The Scripps Research Institute; Estados Unidos. University of California at San Diego; Estados Unidos Fil: Lugli, E.. National Institutes of Health; Estados Unidos Fil: Madeo, F.. university of Graz; Austria Fil: Malorni, W.. Istituto Superiore di Sanità; Italia Fil: Marine, J. C.. VIB; Bélgica. Ghent University; Bélgica Fil: Martin, S. J.. Trinity College; Irlanda Fil: Medema, J. P.. Academic Medical Center; Países Bajos. University of Amsterdam; Países Bajos Fil: Mehlen, P.. Centre Léon Berard; Francia. Centre National de la Recherche Scientifique; Francia. Universite Lyon 2; Francia Fil: Melino, G.. University of Leicester; Reino Unido. Göttingen Center of Molecular Biosciences; Alemania Fil: Moll, U. M.. Stony Brook University; Estados Unidos. Göttingen Center of Molecular Biosciences; Alemania. University of Göttingen; Alemania Fil: Morselli, E.. Inserm; Francia. Universite Paris Sud; Francia. Institut Gustave Roussy; Francia Fil: Nagata, S.. University of Kyoto; Japón Fil: Nicholson, D. W.. Merck Research Laboratories; Estados Unidos Fil: Nicotera, P.. University of Leicester; Reino Unido Fil: Nuñez, G.. University of Michigan; Estados Unidos Fil: Oren, M.. Weizmann Institute of Science; Israel Fil: Penninger, J.. Institute of Molecular Biotechnology of the Austrian Academy of Science; Austria Fil: Pervaiz, S.. National University of Singapore; Singapur. Duke-NUS Graduate Medical School; Singapur Fil: Peter, M. E.. University of Chicago; Estados Unidos Fil: Piacentini, M.. National Institute for Infectious Diseases IRCCS "L. Spallanzani"; Italia. University of Rome "Tor Vergata"; Italia Fil: Prehn. J. H.. Royal College of Surgeons in Ireland; Irlanda Fil: Puthalakath, H.. La Trobe University; Australia Fil: Rabinovich, Gabriel Adrián. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología y Medicina Experimental. Fundación de Instituto de Biología y Medicina Experimental. Instituto de Biología y Medicina Experimental; Argentina Fil: Rizzuto, R.. Università di Padova; Italia Fil: Rodrigues, C. M.. Universidade de Lisboa; Portugal Fil: Rubinsztein, D. C.. Cambridge Institute for Medical Research; Reino Unido Fil: Rudel, T.. University of Würzburg; Alemania Fil: Scorrano, L.. University of Geneva ; Suiza. Venetian Institute of Molecular Medicine; Italia Fil: Simon, H. U.. University of Bern; Suiza Fil: Steller, H.. Howard Hughes Medical Institute; Estados Unidos. The Rockefeller University; Estados Unidos Fil: Tschoop, J.. University of Lausanne; Suiza Fil: Tsujimoto, Y.. Osaka University Medical School; Japón Fil: Vandenabeele, P.. Ghent University; Bélgica. VIB; Bélgica Fil: Vitale, I.. Inserm; Francia. Universite Paris Sud; Francia. Institut Gustave Roussy; Francia Fil: Vousden, K. H.. The Beatson Institute for Cancer Research; Reino Unido Fil: Youle, J. R.. National Institutes of Health; Estados Unidos Fil: Yuan, J.. Harvard Medical School; Estados Unidos Fil: Zhivotovsky, B.. Karolinska Huddinge Hospital. Karolinska Institutet; Suecia Fil: Kroemer, G.. Inserm; Francia. Universite Paris Sud; Francia. Institut Gustave Roussy; Francia
- Published
- 2009
- Full Text
- View/download PDF
15. Galectin-1: Biphasic growth regulation of Leydig tumor cells
- Author
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Biron, V.A., Iglesias, M., Troncoso, M.F., Besio-Moreno, M., Patrignani, Z.J., Pignataro, O.P., and Wolfenstein-Todel, C.
- Subjects
Male ,Cytoplasm ,FAS ligand ,Galectin 1 ,cytofluorometry ,Proliferation ,Apoptosis ,Lactose ,DNA Fragmentation ,Leydig cells ,animal cell ,growth regulation ,Membrane Potentials ,Sertoli-Leydig Cell Tumor ,Leydig cell ,Testicular Neoplasms ,caspase 8 ,mitochondrial membrane ,Cell Line, Tumor ,protein secretion ,Galectin-1 ,caspase 3 ,carbohydrate analysis ,Humans ,cell growth ,controlled study ,caspase 8 inhibitor ,caspase 9 ,protein expression ,mouse ,pathophysiology ,Cell Proliferation ,nonhuman ,Dose-Response Relationship, Drug ,DNA fragment ,article ,enzyme activation ,protein function ,Leydig cell tumor ,Mitochondria ,Neoplasm Proteins ,Gene Expression Regulation, Neoplastic ,cell membrane potential ,cytochrome c ,priority journal ,death receptor ,disaccharide ,protein determination ,caspase 9 inhibitor - Abstract
Galectin-1 (Gal-1) is a widely expressed β-galactoside-binding protein that exerts pleiotropic biological functions. To gain insight into the potential role of Gal-1 as a novel modulator of Leydig cells, we investigated its effect on the growth and death of MA-10 tumor Leydig cells. In this study, we identified cytoplasmic Gal-1 expression in these tumor cells by cytofluorometry. DNA fragmentation, caspase-3, -8, and -9 activation, loss of mitochondrial membrane potential (ΔΨ m), cytochrome c (Cyt c) release, and FasL expression suggested that relatively high concentrations of exogenously added recombinant Gal-1 (rGal-1) induced apoptosis by the mitochondrial and death receptor pathways. These pathways were independently activated, as the presence of the inhibitor of caspase-8 or -9 only partially prevented Gal-1-effect. On the contrary, low concentrations of Gal-1 significantly promoted cell proliferation, without inducing cell death. Importantly, the presence of the disaccharide lactose prevented Gal-1 effects, suggesting the involvement of the carbohydrate recognition domain (CRD). This study provides strong evidence that Gal-1 is a novel biphasic regulator of Leydig tumor cell number, suggesting a novel role for Gal-1 in the reproductive physiopathology. © Copyright 2006 Oxford University Press. Fil:Troncoso, M.F. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Patrignani, Z.J. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Pignataro, O.P. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
- Published
- 2006
16. Apoptosis and CD4+, CD8+ lymphocyte depletion following triphenyltin acetate (TPTA) exposure in mice thymic primary culture
- Author
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Bollo, E., Dacasto, Mauro, and Cornaglia, E.
- Subjects
CD4-Positive T-Lymphocytes ,Mice, Inbred BALB C ,Time Factors ,Dose-Response Relationship, Drug ,cytofluorometry ,apoptosis ,triphenyltin acetate ,cytotoxicity ,organotin ,mouse ,thymocytes ,Apoptosis ,Thymus Gland ,CD8-Positive T-Lymphocytes ,Lymphocyte Depletion ,Immunophenotyping ,Mice ,Microscopy, Electron ,Organotin Compounds ,Animals ,Cells, Cultured - Published
- 1997
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