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Lu, Shuqing, Jianmin Wang, Jianmin Yang, Shenglan Gong, Hong Zhou, Li Chen, and Xianmin Song. "Amplification and Mutation of PSMB5 Gene in Bortezomib Resistant Lymphoblastic Leukemia Cells Derived from Jurkat Line." Blood 110, no. 11 (November 16, 2007): 2373. http://dx.doi.org/10.1182/blood.v110.11.2373.2373.
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Abstract Bortezomib, the first selective proteasome inhibitor in this new category of anti-cancer drug, inhibits chymotrypsin-like activity sited at beta 5 subunit of proteasome (PSMB5). To study the mechanism of proteasome inhibitor resistance in tumor cells, we established a series of bortezomib resistant lymphoblastic leukemia cell lines, named JurkatBs, from Jurkat line by repeated drug induction. There were no significant differences observed in the growth curves, colony formation rates, or cell cycle distribution between the JurkatBs and Jurkat cells. However, the effects of bortezomib, namely cytotoxicity, cell cycle arrest at G2 phase and induction of apoptosis, were decreased significantly in JurkatBs cells. There were no significant differences of intracellular mean fluorescence intensities of daunorubicin between JurkatBs and Jurkat cells (P>0.05) after treated with daunorubicin. Accordingly, the JurkatBs showed no cross-resistance to anthracycline, alkaloid and topoisomerase inhibitor. Quantitative PCR analysis showed no significant overexpression of MDR1 gene in JurkatB1, JurkatB2, JurkatB5 cells in comparison with that of Jurkat cells (22.77±5.58, 1.17±0.23, 8.30±2.62 vs 1.00±0.50; P>0.05). P-gp expression analysis was also negative in JurkatBs and Jurkat cells by Western bloting. By using quantitative PCR, we found that the PSMB5 gene was significantly amplified in JurkatB1 (5.82±0.60) and JurkatB5 cells (6.78±1.21) in comparison with that of Jurkat cells (1±0.49)(P<0.001), but not in JurkatB2 cells(0.16±0.03, P=1.000). A specific chromosome abnormality, i(14q), was found in all JurkatB5 cells (highly resistant to bortezomib), 4/16 JurkatB1 cells (moderately resistant), but not in JurkatB2 cells (slightly resistant). This results suggested that i(14q) may be resulted from the amplification of PMSB5 gene, which is located at 14q11. The chymotrypsin-like activities, determined by measuring the release of the fluorescent AMC from the substrate N- Suc-Leu-Leu-Val- Tyr-AMC, increased significantly in JurkatB1 (relative activity 3.27±0.12) and JurkatB5 cells (5.75±0.22) in comparison with that in Jurkat cells (1.00±0.14; P<0.001), but not in JurkatB2 cells (0.92±0.09; P>0.05). These results were coincident with the amplication of PSMB5, which may partly elucidated the bortezomib resistance in JurkatB cells. We then cloned and sequenced the full-length cDNA product of the PSMB5 gene from JurkatBs and Jurkat cells. A mutation at position 322 (G322A) of PSMB5 gene, causing an an amino acid substitution (Ala108Thr), was found in all selected JurkatB clones. The inhibition of chymotrypsin-like activities in JurartB2 (39.66±2.89) and JurartB5 cells (1.71±3.51), incubated with 10nM bortezomib up to 18h, were decreased significantly in comparison with that of Jurkat cells (86.87±0.97; P<.001), suggesting a decreased binding affinity of bortezomib to the chymotrypsin-like active site caused by Ala108Thr in JurkatB cells, which may resulted in conformation change in β5 subunit. In conclusion, we established bortezomib resistant leukemia cell lines with a different mechanism from that of multi-drug resistance (MDR). Both amplification and G322A mutation of PSMB5 gene are the important mechanisms of bortezomib resistance, by increasing chymotrypsin-like activity, and decreasing binding affinity of bortezomib to the chymotrypsin-like site, respectively.
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Li, M., S. Zhou, X. Liu, and G. Li. "The role of alpha-fetoprotein in maintaining the growth of human hepatoma cells." Journal of Clinical Oncology 24, no. 18_suppl (June 20, 2006): 14081. http://dx.doi.org/10.1200/jco.2006.24.18_suppl.14081.
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14081 Background: This study was to explored the functional mechanism of alpha-fetoprotein (AFP) in maintaining the proliferation of human hepatoma cells line Bel 7402 and the immunsuppression of lymphocyte Jurkat cells. Methods: Western blot was used to detecting the expression of some apoptosis-related gene, fluorescence labeled AFP and confocal microscopy scanning for receptor binding assay in the membrane in Jurkat cells. Results: It showed that AFP could enhance the expression of survivin and c-ras, but restrain caspase-3 express in Bel 7402 cells by Western blotting analysis. It also showed that AFP could bind to the membrane of Jurkat cells by confocal microscopy scanning, and when treated Jurkat with AFP, it indicated that AFP could repress the expression of survivin and Livin and elevated the activity of caspase-3 in the cells; Co-cultured Bel 7402 cells with Jurkat cells, the expression of tumor necrosis related-apoptosis induced ligand (TRAIL) in Jurkt cells was inhibited, when pretreatment with monoclonal antibody of AFP (Anti-AFP), the restrained effect of TRAIL express and the activity of caspase-3 was elevated in Jurkat cells was removed. It also indicated that Anti-AFP had an ability to block these functions of AFP. Conclusions: AFP has a capability to promote the growth and escape from immune surveillance of human hepatoma cells through enhancing the expression of ras and survivin gene in Bel 7402 cells, suppressing TRAIL, survivin and Livin expressed and upregulated activity of caspase-3 in Jurkat cells. No significant financial relationships to disclose.
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Yoon, Jinsun, Eun Shil Kim, Sujung Kim, and Young Lee. "In Vitro and in Vivo Effect of Sodium Metaarsenite (KML001) in Non-Hodgkin's Lymphoma." Blood 120, no. 21 (November 16, 2012): 1656. http://dx.doi.org/10.1182/blood.v120.21.1656.1656.
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Abstract Abstract 1656 Arsenic trioxide has been used for treatment of hematological malignancies including acute promyelocytic leukemia (APL), multiple myeloma. Sodium metaarsenite (NaAs2O3: code name KML001) is an orally bio-available arsenic compound with potential anti-cancer activity. However, the effect of KML001 has not been well studied in non-Hodgkin's lymphoma. The aim of this study is to determine the anti-tumoral effect of KML001 and to investigate the mechanism of anti-tumoral effect of KML001 in malignant lymphoma. KML001 inhibited the cellular proliferation in all lymphoma cell lines as well as JurkatR cells (adriamycin-resistant Jurkat cells) in a dose-dependent manner with IC50 of 5 × 10−8M. KML001 induced G1 cell cycle arrest which was associated with decreased expression of cyclin B1, cyclin E1, CDK1 (cdc2p34), CDK2, CDK4, and CDK6. KML001- induced p27 was bound to CDK4 and CDK6 in Jurkat cells, and bound to CDK2, CDK4 and CDK6 in JurkatR cells. CDK4 and CDK6 kinase activities were reduced in Jurkat and JurkatR cells. KML001 increased early apoptotic fraction using annexin V-PI staining in a time-dependent manner. In addition, Apoptotic molecules of Bcl-2, Bcl-XL, Mcl-1, proform of caspase-3, caspase-8, and caspase-9 were decreased; in contrast, expressions of PARP active form and Bax, were increased in Jurkat and JurkatR cells treated with KML001 in a dose-dependent manner. In addition, KML001 inhibited the activation of STAT1, 3, 5, NF-κB (p65 and p50 subunits), pAKT, p-mTOR, p-GSK3 ß in a dose-dependent manner, but p-PTEN was up-regulated in KML001-treated Jurkat and JurkatR cells. In MAP kinase signaling, pERK was down regulated, while pp38 and pJNK were increased in a dose-dependent manner. Real-time PCR with RNA extracted from KML001-treated Jurkat and JurkatR cells showed a reduction of catalytic subunit of telomerase, hTERT, in a time- dependent manner. When treated KML001, DNA damage molecule (p-γ-H2AX) was increased in a time-dependent manner, and the telomere length was shorten in Jurkat and JurkatR cells. In vivo anti-tumoral activity of KML001 was confirmed using a xenograft-murine model of human lymphoma cell. Tumor burden was significantly reduced (P < 0.01) for 42 days. Especially, in-vivo anti-tumoral effect of 3.5 mg/Kg KML001 was comparable to that of doxorubicin (2.5 mg/Kg, P < 0.05). Furthermore, three refractory or relapsed malignant lymphoma patients (Diffuse large cell lymphoma, Follicular lymphoma. Mantle cell lymphoma) were treated with 10 mg of KML001 daily, resulting in decrease of lymphoma mass in 4 weeks without severe toxicities. In summary, KML001(sodium metaarsenite) demonstrated anti-tumoral effect via various mechanisms including cell cycle arrest, induction of apoptosis, and inhibition of JAK/STAT, PI3K and MAPK pathways. Especially, KML001 might target telomerase with DNA damage. Furthermore, it is probable that KML001 may overcome the resistance of chemotherapeutic agents. Collectively, KML001 may be a candidate agent for the treatment of de novo, refractory and relapsed malignant lymphoma. Disclosures: No relevant conflicts of interest to declare.
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BRAGADIN, MARCANTONIO, ANTONIO TONINELLO, ALBERTO BINDOLI, MARIA PIA RIGOBELLO, and MARCELLA CANTON. "Thallium Induces Apoptosis in Jurkat Cells." Annals of the New York Academy of Sciences 1010, no. 1 (December 2003): 283–91. http://dx.doi.org/10.1196/annals.1299.049.
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Scaringi, L., P. Cornacchione, E. Ayroldi, L. Corazzi, E. Capodicasa, R. Rossi, and P. Marconi. "Omeprazole Induces Apoptosis in Jurkat Cells." International Journal of Immunopathology and Pharmacology 17, no. 3 (September 2004): 331–42. http://dx.doi.org/10.1177/039463200401700313.
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Buenz, Eric J. "Aloin induces apoptosis in Jurkat cells." Toxicology in Vitro 22, no. 2 (March 2008): 422–29. http://dx.doi.org/10.1016/j.tiv.2007.10.013.
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Di Pasqua, Anthony J., Jerry Goodisman, Deborah J. Kerwood, Bonnie B. Toms, and James C. Dabrowiak. "Modification of carboplatin by Jurkat cells." Journal of Inorganic Biochemistry 101, no. 10 (October 2007): 1438–41. http://dx.doi.org/10.1016/j.jinorgbio.2007.06.018.
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Singhal, Pravin C., Aditi A. Kapasi, Krishna Reddy, Nicholas Franki, Nora Gibbons, and Guohua Ding. "Morphine promotes apoptosis in Jurkat cells." Journal of Leukocyte Biology 66, no. 4 (October 1999): 650–58. http://dx.doi.org/10.1002/jlb.66.4.650.
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Acharya, Tathagata, and Ram V. Devireddy. "Cryomicroscopic Investigations of Freezing Processes in Cell Suspensions." Open Biotechnology Journal 4, no. 1 (May 11, 2010): 26–35. http://dx.doi.org/10.2174/1874070701004010026.
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This study evaluates the freezing response of three different cell types, Pacific oyster embryos (~50 µm in diameter), Jurkat cells and HeLa cells (~12 to 15 µm’s in diameter), using cryomicroscopy. Freezing experiments were performed on oyster embryos at cooling rates of either 5 or 10 °C/min, while Jurkats were cooled at either 1 or 10 °C/min and HeLa cells were cooled at either 1, 15 or 20 °C/min, respectively. The experiments with oyster embryos were primarily designed to investigate the phenomena of intracellular ice formation (IIF) while the experiments for Jurkat and HeLa cells were designed to investigate both cellular dehydration and IIF during freezing. IIF was characterized by the abrupt black flashing during the cooling steps while the cellular dehydration experiments were characterized by the volumetric (projected area) shrinkage of the cells during the cooling steps. Mathematical models were fit to the cellular dehydration data to obtain the Jurkat and HeLa cell membrane permeability (Lpg) at the reference temperature (273.15 K), the apparent activation energy of the cellular dehydration process (ELp) or the temperature dependence of Lpg. The temperature dependence of IIF in the oyster embryos, the Jurkat cells and the HeLa cells were also determined.
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Sokolovskaya, Alisa, Ekaterina Korneeva, Danila Zaichenko, Edward Virus, Dmitry Kolesov, Aleksey Moskovtsev, and Aslan Kubatiev. "Changes in the Surface Expression of Intercellular Adhesion Molecule 3, the Induction of Apoptosis, and the Inhibition of Cell-Cycle Progression of Human Multidrug-Resistant Jurkat/A4 Cells Exposed to a Random Positioning Machine." International Journal of Molecular Sciences 21, no. 3 (January 28, 2020): 855. http://dx.doi.org/10.3390/ijms21030855.
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Experiments from flight- and ground-based model systems suggest that unexpected alterations of the human lymphoblastoid cell line Jurkat, as well as effects on cell growth, metabolism, and apoptosis, can occur in altered gravity conditions. Using a desktop random positioning machine (RPM), we investigated the effects of simulated microgravity on Jurkat cells and their multidrug-resistant subline, Jurkat/A4 cells. The viability of Jurkat/A4 cells decreased after simulated microgravity in contrast with the Jurkat cells. At the same time, the viability between the experimental Jurkat cells and control Jurkat cells was not significantly different. Of note, Jurkat cells appeared as less susceptible to apoptosis than their multidrug-resistant clone Jurkat/A4 cells, whereas cell-cycle analysis showed that the percentage of Jurkat/A4 cells in the S-phase was increased after 72 and 96 h of RPM-simulated microgravity relative to their static counterparts. The differences in Jurkat cells at all phases between static and simulated microgravity were not significant. The surface expression of the intercellular adhesion molecule 3 (ICAM-3)—also known as cluster of differentiation (CD)50—protein was changed for Jurkat/A4 cells following exposure to the RPM. Changes in cell morphology were observed in the Jurkat/A4 cells after 96 h of RPM-simulated microgravity. Thus, we concluded that Jurkat/A4 cells are more sensitive to RPM-simulated microgravity as compared with the parental Jurkat cell line. We also suggest that intercellular adhesion molecule 3 may be an important adhesion molecule involved in the induction of leukocyte apoptosis. The Jurkat/A4 cells with an acquired multidrug resistance phenotype could be a useful model for studying the effects of simulated microgravity and testing anticancer drugs.
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Starikova, Ye G., N. V. Ryazantseva, V. V. Novitsky, L. A. Tashireva, Yu V. Starikov, Ye A. Stepovaya, I. A. Osikhov, O. A. Vasiliyeva, and Y. D. Yakushina. "The role of intracellular gaseous transmitters hydrogen sulfide and nitric oxide in apoptosis regulation of normal and cancer cells." Bulletin of Siberian Medicine 10, no. 6 (December 28, 2011): 40–44. http://dx.doi.org/10.20538/1682-0363-2011-6-40-44.
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Investigation of influence of gases nitric oxide and hydrogen sulfide on apoptotic cell death of Jurlat cells and mononuclear leucocytes of healthy donors was conducted. It was shown that 100 mmol sodium nitroprussidi increased the apoptosis of T lymphoblast leukemia cells after 15’ incubation. 10 and 100 mmol donor of hydrogen sulfide caused apoptotic death of Jurkat cells after 15’ incubation. 15’ exposure of nitric oxide and hydrogen sulfide donors did not lead to the changes of cell death of mononuclear leucocytes. Gaseous transmitters NO and H2S increased necrosis of Jurkat cells and mononuclear leucocytes after 24 h incubation with the appropriate gase’s donor.
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Teixeira, José E., and Barbara J. Mann. "Entamoeba histolytica-Induced Dephosphorylation in Host Cells." Infection and Immunity 70, no. 4 (April 2002): 1816–23. http://dx.doi.org/10.1128/iai.70.4.1816-1823.2002.
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ABSTRACT Activation of host cell protein tyrosine phosphatases (PTPases) and protein dephosphorylation is an important mechanism used by various microorganisms to deactivate or kill host defense cells. To determine whether protein tyrosine dephosphorylation played a role in signaling pathways affecting Entamoeba histolytica-mediated host cell killing, we investigated the involvement of PTPases during the attachment of E. histolytica to target cells. We observed a rapid decrease in cellular protein tyrosine levels in Jurkat cells, as measured with an antiphosphotyrosine monoclonal antibody, following adherence to E. histolytica. Ameba-induced protein dephosphorylation was contact dependent and required intact parasite, since blocking amebic adherence with galactose inhibited tyrosine dephosphorylation and amebic lysates had no effect on phosphotyrosine levels. Moreover, disruption of amebic adherence with galactose promoted recovery of phosphorylation in Jurkat cells, indicating that dephosphorylation precedes target cell death. The evidence suggests that ameba-induced dephosphorylation is mediated by host cell phosphatases. Prior treatment of Jurkat cells with phenylarsine oxide, a PTPase inhibitor, inhibited ameba-induced dephosphorylation. We also found proteolytic cleavage of the PTPase 1B (PTP1B) in Jurkat cells after contact with amebae. The calcium-dependent protease calpain is responsible for PTP1B cleavage and enzymatic activation. Pretreatment of Jurkat cells with calpeptin, a calpain inhibitor, blocked PTP1B cleavage and inhibited ameba-induced dephosphorylation. In addition, inhibition of Jurkat cell PTPases with phenylarsine oxide blocked Jurkat cell apoptosis induced by E. histolytica. These results suggest that E. histolytica-mediated host cell death occurs by a mechanism that involves PTPase activation.
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Fan, Lei, Liqian Xie, Fei Shen, Lan Dai, Jianyong Li, and Changgeng Ruan. "Ectopic Expression of Mer on Jurkat Cells and Its Anti-Apoptosis Effect." Blood 110, no. 11 (November 16, 2007): 4098. http://dx.doi.org/10.1182/blood.v110.11.4098.4098.
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Abstract BACKGROUND & OBJECTIVE: Mer is one member of Axl receptor tyrosine kinase family; its ligand Gas6 can bind Mer, then stimulate the tyrosine kinase activity and downstream cell signal pathway of Mer, and take part in cell inflammation, apoptosis and thrombosis. There are more and more reports on Mer function, while few on its association with malignant diseases. This study was to detect the expression of Mer on T-cell leukemia cell line--Jurkat, and investigate its anti-apoptosis function and the mechanism. METHODS: Flow cytometry (FCM) was used to detect Mer expression on normal T cells and Jurkat cells. RNA interference (RNAi) was used to block the expression of Mer on Jurkat cells. The effect of Mer on the proliferation of Jurkat cells was assessed by MTT assay, and its effect on serum starvation-induced apoptosis was evaluated by FCM with Annexin V/PI double staining. The expression of apoptosis-associated genes Bcl-2 and Caspase-3 in Jurkat cells was detected by real-time polymerase chain reaction (PCR) after Mer blocking. RUSELTS: Mer was not expressed in normal T cells both in peripheral blood and bone marrow, but highly expressed in Jurkat cells with a positive rate of 51.1%±5.2%. The inhibition rate of Mer expression in Jurkat cells by RNAi was 86.0%±10.3%. After 48-hour serum starvation, the apoptosis rate was 15.3%±4.3% in Mer-blocking Jurkat cells, and only 1.5%±1.0% in control Jurkat cells(P<0.01). There was no significant difference in Jurkat cell proliferation rate between these 2 groups. After Mer blocking, Bcl-2 expression was decreased by 42.7%±8.6% of control(P<0.01), Caspase-3 expression showed no significant change. CONCLUSION: Mer is highly expressed in Jurkat cells, and could inhibit cell apoptosis via Bcl-2 signaling pathway.
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Némorin, Jean-Guy, Pierre Laporte, Geneviève Bérubé, and Pascale Duplay. "p62dokNegatively Regulates CD2 Signaling in Jurkat Cells." Journal of Immunology 166, no. 7 (April 1, 2001): 4408–15. http://dx.doi.org/10.4049/jimmunol.166.7.4408.
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Dionisio, Leonardo, Verónica Arias, Cecilia Bouzat, and María del Carmen Esandi. "GABAA receptor plasticity in Jurkat T cells." Biochimie 95, no. 12 (December 2013): 2376–84. http://dx.doi.org/10.1016/j.biochi.2013.08.023.
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Wang, Chunyan, Huo Tan, Liu Lei, and Lihua Xu. "Study on Leukemia Cell Differentiation and Drug Resistance By SATB1 Gene." Blood 124, no. 21 (December 6, 2014): 5172. http://dx.doi.org/10.1182/blood.v124.21.5172.5172.
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Abstract Background and objective: In this article, four types of lymphoma cell lines U937, Raji, Hut-102, Akata, and three types of leukemia cell lines K562, HL-60, Jurkat were used the expression of SATB1 in leukemia cells, Through cell differentiation induced by all-TRANS Retinoic acid and DMSO, finds the SATB1 gene expression is reduced, suggest that the SATB1 gene may be involved in cell differentiation. By gene silencing, reduce the SATB1 gene expression, sensitivity to chemotherapy drugs is increased, suggest that the SATB1 gene may be associated with drug resistance. Methods: 1. Western Blot Assay for detection of SATB1 gene expression in cell lines. 2. DMSO and ATRA to HL-60, Jurkat cells for different times, SATB1 gene expression in the cells are detected by Western Blot. 3. Building SATB1-shRNA, transfected Jurkat cells and to HL-60. 4. Testing inhibition rate of chemotherapy drugs on HL-60, HL-60-SATB1-ctr, HL-60-SATB1-sh, Jurkat, Jurkat-SATB1-ctr, Jurkat-SATB1-sh cell, suggesting its relationship with the drug resistance. Results: 1. SATB1 gene was expression in all the plant cells. 2. The expression of SATB1 in U937, Raji, Hut-102, Akata four types of lymphoma cell line is low. 3. It was highly expression in HL-60, Jurkat cells, but low in K562. 4. DMSO and ATRA treat HL-60, Jurkat cells for 48 and 96 hours, HL-60 cells become larger, rounded, Jurkat cells into smaller, is more obvious for 96-hour. 5. For HL-60, Jurkat cells, after DMSO and ATRA treated, the expression of SATB1 was decreased, more obvious for 96-hour. 6. HL-60-SATB1-sh1, Jurkat-SATB1-sh1 cell compared with the control group, the SATB1 protein content decreased significantly, successfully building SATB1-shRNA HL-60 and Jurkat cell line. 7. HL-60-SATB1-sh1, and Jurkat-SATB1-sh1 of daunorubicin (DNR) sensitivity has improved significantly. Conclusion: 1. The SATB1 gene expression in leukemia and lymphoma cells, and higher expression in leukemia cells. 2. After DMSO and ATRA treatment, the SATB1 expression significantly reduced, suggest that SATB1 may be involved in cell differentiation. 3. Successfully built SATB1-shRNA, and successfully transferred to HL-60 and Jurkat cell lines. 4. HL-60-SATB1-sh1, and Jurkat-SATB1-sh1 of daunorubicin (DNR) sensitivity increased significantly, prompting SATB1 may be related to drug-resistance. Disclosures No relevant conflicts of interest to declare.
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Feng, Xiaoqin, Wenjiao Ding, and Chunfu Li. "CXCR3 Upregulation Effect of T Lymphocytic Leukemia Cell Invasion in Vitro." Blood 128, no. 22 (December 2, 2016): 5892. http://dx.doi.org/10.1182/blood.v128.22.5892.5892.
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Abstract Objective The study was to explore chemokine receptor CXCR3 influence on invasion of T lymphocytic leukemia cell. Methods Mouse CXCR3 gene was amplified from T vector containing mouse CXCR3 by PCR, and constructed the mouse CXCR3 overexpressing lentivirus carrying GFP & Puromycin (puro). Jurkat cell line was infected by the constructed CXCR3 overexpression lentivirus. Puromycin was added to screene the successfully infected lymphoblastic leukemia cells. CXCR3 expression on Jurkat cells was analyzed by flow cytometre. Constructed CXCR3-LV5-Jurkat cells were added into the Transwell upper chamber covered with Matrigel. Ligand of CXCR3(CXCL10) was added to the lower chamber. Cell number in the upper chamber and lower chamber which used to calculate the invasion rate was counted by flow cytometry respectively. Results GFP+ Jurkat cells was observed less than <10% after lentivirus infection 96h. GFP+Jurkat cells achieved to 90% by Puromycin selection. The expression of CXCR3 on CXCR3-LV5-Jurkat cell group was 90% higher than LV5-Jurkat cell group. CXCR3-LV5-Jurkat cell line stably overexpressed CXCR3 was successfully constructed. The invasion rate of CXCR3-LV5-Jurkat cell lines was significantly higher than LV5-Jurkat control group (12.71 %± 1.03% vs 6.82% ± 0.49%, p <0.0001). Conclusion Overexpression of CXCR3 on T lymphocytic leukemia cell line (Jurkat cell) can enhance the invasion of leukemia cells in vitro, CXCR3/CXCL10 path way may induce the T lymphoblastic leukemic cell invading the central nervous system. Disclosures No relevant conflicts of interest to declare.
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LÓPEZ, José M., Antonio F. SANTIDRIÁN, Clara CAMPÀS, and Joan GIL. "5-Aminoimidazole-4-carboxamide riboside induces apoptosis in Jurkat cells, but the AMP-activated protein kinase is not involved." Biochemical Journal 370, no. 3 (March 15, 2003): 1027–32. http://dx.doi.org/10.1042/bj20021053.
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5-Aminoimidazole-4-carboxamide (AICA) riboside, a precursor of purine nucleotide biosynthesis, induces apoptosis in Jurkat cells. Incorporation of AICAriboside into the cells is necessary for this effect since addition of nitrobenzylthioinosine, a nucleoside-transport inhibitor, completely protects Jurkat cells from apoptosis. Adenosine, but not other nucleosides, also protects Jurkat cells from AICAriboside-induced apoptosis. The apoptotic effect is caspase-dependent since caspases 9 and 3 are activated and the caspase inhibitor benzyloxycarbonyl-Val-Ala-Asp-fluoromethylketone (Z-VAD.fmk) blocks apoptosis. Furthermore, AICAriboside induces mitochondrial cytochrome c release. AICAriboside, when phosphorylated to AICAribotide (ZMP), is a specific activator of the AMP-activated protein kinase (AMPK) in certain cell types. However, AICAriboside does not activate AMPK in Jurkat cells. Moreover, 5-iodotubercidin, an inhibitor of AICAriboside phosphorylation, does not inhibit apoptosis in Jurkat cells. These results indicate that AICAriboside induces apoptosis independently of ZMP synthesis and AMPK activation in Jurkat cells.
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Azad, N., N. LaPaglia, L. Kirsteins, S. Uddin, J. Steiner, D. W. Williams, A. M. Lawrence, and N. V. Emanuele. "Jurkat cell proliferative activity is increased by luteinizing hormone-releasing hormone." Journal of Endocrinology 153, no. 2 (May 1997): 241–49. http://dx.doi.org/10.1677/joe.0.1530241.
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Abstract Jurkat cells were used to study the immunomodulatory role of luteinizing hormone-releasing hormone (LHRH) in immune cells. The Jurkat cell, a human mature leukemic cell line, phenotypically resembles resting human T lymphocytes and has been widely used to study T cell physiology. The data from this study demonstrate that the Jurkat cell concentration of immunoreactive LHRH was 210 ± 36 pg/106 cells and that of proLHRH was 188 ± 27 pg/106 cells (means ± s.e.m.). The authenticity of this LHRH immunoreactivity is documented in two ways. First, both Jurkat LHRH and proLHRH immunoreactivity demonstrate dilutional parallelism with hypothalamic LHRH and proLHRH. Second, Jurkat lysates show LHRH bioactivity by releasing luteinizing hormone from rat anterior pituitary cells in culture. The presence of substantial amounts of LHRH in medium in which Jurkat cells were cultured for 72 h indicated that LHRH can be released from the cells. Using specific primers to exons 2 and 4 of the LHRH gene, we have found that Jurkat cells (like human T cells) express LHRH mRNA. The LHRH agonist, des-Gly10,d-Trp6-LHRH ethylamide, significantly increases the proliferative activity of Jurkat cells, as assessed by tritiated thymidine incorporation, from 15 980 ± 1491 c.p.m. in controls to 28 934 ± 3395, 30 457 ± 3861 (P=0·05 vs control) or 35 299 ± 5586 c.p.m. (P<0·01 vs control) with 10−11, 10−9 or 10−7 m agonist respectively. LHRH antagonist, [d-pGlu1,d-Phe2,d-Trp3,6]-LHRH, at a concentration of 10−8 m decreases Jurkat cell proliferative activity from 17 145 ± 526 c.p.m. in control medium to 10 653 ± 1323 c.p.m. (P=0·05). Co-incubation with the LHRH antagonist completely inhibits the proliferative stimulation induced by the LHRH agonist. Furthermore, applying monoclonal LHRH antibody to Jurkat cells inhibits the cell proliferative activity assessed by tritiated thymidine incorporation from 19 900 ± 2675 c.p.m. in controls to 15 680 ± 2254, 15 792 ± 1854 and 9700 ± 908 c.p.m. in media with 1:40, 1:20 and 1:10 dilution of purified antibody respectively (P<0·01, 1:10 dilution compared with control). In addition, the cAMP level in LHRH-stimulated Jurkat cells is decreased to 74, 27 and 57% of control levels after 15, 30 and 45 min respectively of exposure to 10−7 m LHRH agonist. In summary, Jurkat cells produce, process and release immunoreactive and bioactive LHRH, as do normal human T cells. Endogenous and exogenous LHRH increase Jurkat cell proliferative activity, and cAMP may be involved in LHRH-induced Jurkat cell proliferation. The Jurkat cell may be a useful model with which to study the role of LHRH in human T cell function. Journal of Endocrinology (1997) 153, 241–24
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Jänicke, R., and D. N. Männel. "Distinct tumor cell membrane constituents activate human monocytes for tumor necrosis factor synthesis." Journal of Immunology 144, no. 3 (February 1, 1990): 1144–50. http://dx.doi.org/10.4049/jimmunol.144.3.1144.
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Abstract Several lines of evidence point to an activation mechanism of monocytes/macrophages by tumor cells. In this study we present data for distinct surface structures on K562 and Jurkat cells to directly induce TNF-mRNA expression and TNF production by human peripheral blood monocytes. Northern analysis showed that incubation of monocytes with either K562 or Jurkat cells led to a significant increase in TNF-mRNA expression. In addition, enhanced TNF production was detected in supernatants of monocyte cultures activated by Jurkat cells. Not only viable tumor cells but also metabolically inactivated tumor cells, cytoblasts, and membrane preparations from Jurkat and K562 cells induced TNF-mRNA expression. We identified two different membrane protein fractions with relative molecular mass of 32 to 38 kDa for Jurkat cells and 46 to 54 kDa for K562 cells that were responsible for monocyte activation.
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Nosareva, O. L., E. A. Stepovaya, N. V. Ryazantseva, E. V. Shakhristova, D. S. Orlov, and V. V. Novitsky. "Ubiquitin and regulation of apoptosis in Jurkat cells." Bulletin of Siberian Medicine 17, no. 3 (September 29, 2018): 96–104. http://dx.doi.org/10.20538/1682-0363-2018-3-96-104.
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Introduction.One of the crucial tasks in medicine is studying the molecular mechanisms of selective management of tumor cell apoptosis following conformational changes in protein molecules (ubiquitination).The purpose of the study. The aim of the project is to establish the role of ubiquitin and ubiquitinligase in dexamethasone-induced apoptosis in Jurkat cells.Materials and methods.The study was carried out on the Jurkat tumor cell line (intact cells and cells cultured in the presence of an apoptosis inducer dexamethasone in the final concentration of 10 µmol. In intact and dexamethasone-affected Jurkat cells, implementation of apoptosis and the amount of FAS-, TNF Receptor 1 and cells with reduced mitochondrial membrane potential were assessed by flow cytometry using FITC-conjugated Annexin V and Propidium Iodide. The levels of NF-κB, Apaf-1, ubiquitin and ubiquitin ligase were determined by Western blot analysis. The activity of caspase-3 was measured by spectrofluorometry.Results.When adding the apoptosis inducer dexamethasone to the Jurkat cell culture, we registered a fall in the concentration of ubiquitin and a rise in the level of ubiquitinligase against the backdrop of activated receptor(an increase in the amount of Annexin V positive cells, FASand TNF Receptor 1) and mitochondrialmediated (an increase in the number of cells with reduced mitochondrial membrane potential and elevation of Apaf-1 level) pathways of apoptosis, as opposed to the intact cell culture. We estimated the completion of apoptosis by determining the activity of caspase-3 in the investigated tumor cells.Conclusion.The obtained findings allow the conclusion that ubiquitination of regulatory and effector proteins in programmed cell death is one of the molecular mechanisms that regulates and selectively controls apoptosis in Jurkat cells.
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Amet, Tohti, Daniel Byrd, Jie Lan, Nicole Shepherd, and Kai Yang. "Glycosylphosphatidylinositol deficiency attenuates the production of infectious HIV-1 and renders the virions sensitive to complement attack (VIR1P.1128)." Journal of Immunology 194, no. 1_Supplement (May 1, 2015): 74.5. http://dx.doi.org/10.4049/jimmunol.194.supp.74.5.
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Abstract Human immunodeficiency virus type 1 (HIV-1) escapes complement-mediated destruction by incorporating regulators of complement activation (RCA) from the host cells. Abrogation of RCA function leads to complement-mediated virolysis. However, little is known about the mechanism by which HIV-1 incorporates RCA from the host cell. Here we used glycosylphosphatidylinositol (GPI)-deficient Jurkat (Jurkat-7) cells that only express intracellular CD59 (a key member of RCA), but not on the surface, to study how HIV-1 incorporates CD59 from an infected cell. Compared to wild type Jurkat cells, Jurkat-7 cells are less susceptible to HIV-1 infection, and produces lower amount of virions due to the impaired GPI biosynthesis. Interestingly, virions produced from Jurkat-7 cells did not contain CD59, while virions from wild-type Jurkat cells did contain CD59 with a certain amount of viral protein expression. This indicates that HIV-1 incorporates CD59 from the surface of host cell rather than from the intracellular compartments. Virions produced from Jurkat-7 cells are less infectious, but more susceptible to complement-mediated virolysis due to the failed CD59 incorporation into the virus surface. Furthermore, transient restoration of GPI anchor in Jurkat-7 cells resulted in recovered surface expression of CD59. These results reveal a critical role of GPI anchor and GPI-anchored proteins in HIV-1 life cycle and incorporation of CD59, probably other host cell proteins into the HIV-1 virions.
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Posey, Avery D., Robert D. Schwab, Alina Boestaneau, Laura A. Johnson, and Carl H. June. "Glycopeptide-Specific Chimeric Antigen Receptor Targeting of T Cell Leukemia." Blood 124, no. 21 (December 6, 2014): 4803. http://dx.doi.org/10.1182/blood.v124.21.4803.4803.
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Abstract Background Adoptive transfer of T cells redirected with chimeric antigen receptors (CARs) has shown tremendous efficacy in targeting CD19-expressing leukemic cells; however, these CAR T cells also deplete normal CD19-expressing B cells. Although B cell lymphopenia can be overcome by gamma-globulin supplementation, other forms of on-target, off-site toxicity emphasizes the need for cancer cell-specific epitopes in CAR T cell therapy. To date, T cell leukemia has not been targeted due to possible fratricide because of shared antigens expressed on leukemic T cells and CAR T cells. Cellular transformation often produces altered glycosylation patterns, making cancer-specific glycoantigens attractive targets for CAR development. Here we demonstrate the successful eradication of the Jurkat T cell leukemia with Tn-specific CAR T cells. Methods The Jurkat E6.1 T cell leukemia line contains a frameshift mutation in the T synthase chaperone protein Cosmc that prevents core 1 structure formation on O-linked protein glycosylation, resulting in the presentation of Tn antigen on many glycoproteins. Here we describe the development of a CAR using a scFv sequence derived from the 5E5 mAb, which was developed against the Tn antigen of Mucin-1 (Muc1). A CAR was constructed by linking the 5E5 scFv to CD8alpha hinge and transmembrane region to the signaling endodomain comprised of 4-1BB and CD3zeta. The resultant Tn specific CAR was expressed in a lentiviral vector. Results In preliminary experiments Tn-CAR T cells had cytotoxicity to a variety of primary ovarian, breast and pancreatic tumor cells. Specific killing of Jurkat T leukemic cells was demonstrated by lysis of wild type Jurkat while the CAR T cells failed to kill Jurakat after overexpression of Cosmc. In specific, expression of full-length Cosmc expression in the Jurkat E6.1 cell line abolished staining by the 5E5 mAb, restoredT synthase activity, and protected the cells from lysis by 5E5-CAR T cells. Human T cells expressing the 5E5-CAR demonstrate rapid clearance of established Jurkat tumors in NSG mouse xenograft models, as assessed by serial bioluminescence imaging and prolonged survival compared to mice expressing a control CD19-specific CAR T cells (P<0.005). Conclusions These results demonstrate that the 5E5-CAR is specific for the Tn antigen and provides a potent cancer-specific immunotherapy for the targeting of non-dispensable tissues such as T cell leukemias. Disclosures June: Novartis: IP licensed by University of Pennsylvania to Novartis. Author entitled to royalties from the University. Patents & Royalties, Research Funding.
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Hwang, Eung Soo, and Jung Heon Kim. "Insoluble substances produced from human cytomegalovirus-infected cells induce deaths of nearby cells through non-classical death signal pathway (P6116)." Journal of Immunology 190, no. 1_Supplement (May 1, 2013): 128.9. http://dx.doi.org/10.4049/jimmunol.190.supp.128.9.
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Abstract Human cytomegalovirus (HCMV) has many strategies to evade the host immune system, and eventually resides in some cells in latency. Although the involvement of Fas ligand in T cell death was reported in the pathogenesis of retinitis with HCMV infection to retinal pigment epithelial cells, the cell death near other lesions caused by HCMV infection was not studied in detail by now. The insoluble substances derived from HCMV-infected fibroblasts, induce the deaths of variety of cell lines including Jurkat, HL-60, K562, U937 and THP-1 cells, but not of fibroblasts, HEK293 and U373MG. They were resistant to treatment with 56°C for 30 min to lose death induceability to Jurkat cells. Cell death of Jurkat cells by these substances were not inhibited by the simultaneous treatment with neutralizing antibodies to Fas ligand or TRAIL, or caspase inhibitors. Insoluble substances induced cleavages of poly ADP-ribose polymerase-1 into 89 kDa fragment, but not through caspase 3, 7 or 9 pathway in Jurkat cells. AIF was detected in the cytoplasmic fraction, but not in the nuclear fraction of Jurkat cells from 6 hours following exposure to them. This result suggested AIF was not translocated from mitochondria to nucleus in Jurkat cells by the stimulation with insoluble substances. Collectively human cytomegalovirus infection would induce the death of myeloid and lymphoid cells near the infection site through non-classical death signal pathway.
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Sun, Manman, Feiyue Xing, Shan Pan, Jingfang Di, Shan Zeng, and Jing Liu. "Low-dose anisomycin is sufficient to alter the bio-behaviors of Jurkat T cells." Open Life Sciences 8, no. 12 (December 1, 2013): 1230–40. http://dx.doi.org/10.2478/s11535-013-0235-4.
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AbstractAnisomycin is a pyrrolidine antibiotic isolated from Streptomyces griseolus. It has been found that a quite low dose of anisomycin is sufficient to block proliferation of primary T lymphocytes. The focus of this study is to explore the possibility of anisomycin to treat human acute leukemia Jurkat T cells in vitro. The results indicated that the low dose of anisomycin could significantly inhibit the colony formation of Jurkat T cells and elevate the inhibition rate of Jurkat T cell growth along with its increasing concentrations. Jurkat T cell cycle was blocked into S-phase by anisomycin. Consistent with the increased proportion of sub-G1 phase, anisomycin promoted Jurkat T cell apoptosis. The CD69 and CD25 expression on the surface of Jurkat T cells was also down-regulated prominently along with the enhancing concentrations of anisomycin, followed by the decreased production of IL-4, IL-10, IL-17, TGF-β and IFN-γ, and the down-regulated expression of phosphorylated-ERK1/2. The results suggest that the suppressive effect of anisomycin on Jurkat T cell growth may be related to inhibiting TGF-β production and ERK1/2 activation, arresting the cell cycle at S-phase and promoting the apoptosis of Jurkat T cells.
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Aune, T. M., K. M. McGrath, T. Sarr, M. P. Bombara, and K. A. Kelley. "Expression of 5HT1a receptors on activated human T cells. Regulation of cyclic AMP levels and T cell proliferation by 5-hydroxytryptamine." Journal of Immunology 151, no. 3 (August 1, 1993): 1175–83. http://dx.doi.org/10.4049/jimmunol.151.3.1175.
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Abstract The neurotransmitter, serotonin (5-hydroxytryptamine, 5HT), has been shown to affect function of cells of the immune system. More recently, specific 5HT receptors have been identified and partially characterized on Jurkat cells. Results presented here characterize the receptor on Jurkat cells as the 5HT1a receptor subtype and show that mitogen-activated but not resting human T cells also express the 5HT1a receptor subtype. Analysis of mRNA in Jurkat cells and activated and resting T cells by PCR or by Northern analysis revealed the presence of 5HT1a receptor. Pharmacologic analysis of this receptor demonstrated that the receptors on Jurkat cells and activated T cells are similar to each other and that they resemble the 5HT1a receptor found in the brain. Analysis of the second messenger pathways activated by the 5HT1a receptor show that ligand-binding to the Jurkat cell 5HT1a receptor results in elevation of intracellular inositol phosphates and Ca2+ and that ligand binding to the 5HT1a receptor on activated T cells modulated intracellular levels of cAMP.
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Felce, Suet Ling, Gillian Farnie, Michael L. Dustin, and James H. Felce. "RNA-Seq analysis of early transcriptional responses to activation in the leukaemic Jurkat E6.1 T cell line." Wellcome Open Research 5 (June 17, 2021): 42. http://dx.doi.org/10.12688/wellcomeopenres.15748.2.
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Background: The leukaemia-derived Jurkat E6.1 cell line has been used as a model T cell in the study of many aspects of T cell biology, most notably activation in response to T cell receptor (TCR) engagement. Methods: We present whole-transcriptome RNA-Sequencing data for Jurkat E6.1 cells in the resting state and two hours post-activation via TCR and CD28. We compare early transcriptional responses in the presence and absence of the chemokines CXCL12 and CCL19, and perform a basic comparison between observed transcriptional responses in Jurkat E6.1 cells and those in primary human T cells using publicly deposited data. Results: Jurkat E6.1 cells have many of the hallmarks of standard T cell transcriptional responses to activation, but lack most of the depth of responses in primary cells. Conclusions: These data indicate that Jurkat E6.1 cells hence represent only a highly simplified model of early T cell transcriptional responses.
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Felce, Suet Ling, Gillian Farnie, Michael L. Dustin, and James H. Felce. "RNA-Seq analysis of early transcriptional responses to activation in the leukaemic Jurkat E6.1 T cell line." Wellcome Open Research 5 (March 3, 2020): 42. http://dx.doi.org/10.12688/wellcomeopenres.15748.1.
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Background: The leukaemia-derived Jurkat E6.1 cell line has been used as a model T cell in the study of many aspects of T cell biology, most notably activation in response to T cell receptor (TCR) engagement. Methods: We present whole-transcriptome RNA-Sequencing data for Jurkat E6.1 cells in the resting state and two hours post-activation via TCR and CD28. We compare early transcriptional responses in the presence and absence of the chemokines CXCL12 and CCL19, and perform a basic comparison between observed transcriptional responses in Jurkat E6.1 cells and those in primary human T cells using publicly deposited data. Results: Jurkat E6.1 cells have many of the hallmarks of standard T cell transcriptional responses to activation, but lack most of the depth of responses in primary cells. Conclusions: These data indicate that Jurkat E6.1 cells hence represent only a highly simplified model of early T cell transcriptional responses.
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Kurita-Ochiai, Tomoko, Shintaro Seto, and Kuniyasu Ochiai. "Role of Cell-Cell Communication in Inhibiting Butyric Acid-Induced T-Cell Apoptosis." Infection and Immunity 72, no. 10 (October 2004): 5947–54. http://dx.doi.org/10.1128/iai.72.10.5947-5954.2004.
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ABSTRACT We have previously demonstrated that human gingival fibroblasts rescue butyric acid-induced T-cell apoptosis via proinflammatory cytokines such as interleukin 6 (IL-6) and IL-11, which are produced by fibroblasts stimulated with butyric acid. In this study, we determined if T-cell adhesion to human gingival fibroblasts influenced the susceptibility of T cells to butyric acid-induced apoptosis. We have shown that the number of Jurkat T cells adherent to gingival fibroblasts (Gin-1 cells) was significantly increased by the addition of butyric acid. All Jurkat cells that adhered to Gin-1 cells remained viable, while the nonadherent Jurkat cells dropped into apoptosis. The increase in T-cell adhesion to fibroblasts was also observed when Jurkat cells, but not Gin-1 cells, were pretreated with butyric acid. The expression levels of CD44, very late antigen 2 (VLA-2) and VLA-5 but not of leukocyte function-associated antigen 1 (LFA-1) and VLA-4 on Jurkat cells were increased following treatment with butyric acid. Furthermore, pretreatment of butyric acid-sensitized Jurkat cells with monoclonal antibodies against CD44, VLA-2, and VLA-5, but not LFA-1 and VLA-4, followed by coculture with Gin-1 cells inhibited T-cell adhesion to fibroblasts and increased apoptosis of nonadherent T cells after coculture of gingival fibroblasts and Jurkat cells. These results indicate that T-cell adherence to fibroblasts is enhanced by butyric acid and that butyric acid-induced T-cell apoptosis is down-regulated by T-cell adhesion to gingival fibroblasts through an interaction with the adhesion molecules CD44, VLA-2, and VLA-5 expressed on T cells stimulated with butyric acid.
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Shatrova, A. N., E. V. Mityushova, N. A. Aksenov, and I. I. Marakhova. "CD25 expression on the surface of Jurkat cells." Cell and Tissue Biology 9, no. 5 (September 2015): 364–70. http://dx.doi.org/10.1134/s1990519x15050119.
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Andersen, Cecilie, Rolf Pettersen, Dina Aresvik, Marianne Wright, and Tore Abrahamsen. "Gliotoxin Mediated Apoptotic Cell Death in Jurkat cells." International Journal of Infectious Diseases 12 (June 2008): S47. http://dx.doi.org/10.1016/s1201-9712(08)60117-4.
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Anbarlou, Azadeh, Amir Atashi, Masoud Soleimani, Mahshid AkhavanRahnama, Mahbobeh Bohloli, and Majid Mossahebi-Mohammadi. "Differential characteristics of CD133+ and CD133− Jurkat cells." In Vitro Cellular & Developmental Biology - Animal 51, no. 6 (January 29, 2015): 556–61. http://dx.doi.org/10.1007/s11626-015-9869-z.
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Im, Do Jin, and Su-Nam Jeong. "Transfection of Jurkat T cells by droplet electroporation." Biochemical Engineering Journal 122 (June 2017): 133–40. http://dx.doi.org/10.1016/j.bej.2017.03.010.
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Okazaki, Masahiro, Genta Maeda, Tadashige Chiba, Takeshi Doi, and Kazushi Imai. "Identification of GATA3 binding sites in Jurkat cells." Gene 445, no. 1-2 (September 2009): 17–25. http://dx.doi.org/10.1016/j.gene.2009.06.010.
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Teixeira, J. E., and B. J. Mann. "Characterization ofEntamoeba histolytica-induced dephosphorylation in Jurkat cells." Journal of Biosciences 27, no. 6 (November 2002): 615–18. http://dx.doi.org/10.1007/bf02704856.
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Park, Sung-Joon, Sung-Hyuk Choi, Young-Duck Cho, Jung-Youn Kim, Han-Jin Cho, Kyung-Hwan Kim, and Won-Young Kim. "Protective effects of pentoxifylline on T-cell viability under inflammatory conditions." European Journal of Inflammation 20 (January 2022): 1721727X2211207. http://dx.doi.org/10.1177/1721727x221120753.
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Introduction: Pentoxifylline (PTX) reduces the levels of pro-inflammatory cytokines; however, its effects on immune system is not well understood. The aim of this study was to investigate the effect of PTX on T cells under inflammatory conditions in co-culture with THP-1-derived macrophages. Methods: Toll-like receptor 4 (TLR4) and macrophage migration inhibitory factor (MIF) levels were measured after addition of PTX to lipopolysaccharide (LPS)-stimulated differentiated THP-1 cells. T cell viability and MIF levels were measured after PTX was added to prostaglandin E2 (PGE2)-stimulated Jurkat T-cell leukemia line. Co-culture was conducted to determine the effect of LPS-stimulated differentiated THP-1 cells that are affected by PTX on Jurkat cells. To prevent the direct effects of LPS and PTX on Jurkat cells, LPS and PTX were washed from THP-1 cells before co-culture. T cell viability and interleukin-2 (IL-2) levels were determined in Jurkat cells. Results: Increase in the MIF concentration and TLR4 expression level in differentiated THP-1 cells stimulated with LPS were reversed after PTX addition. However, PTX did not improve T cell viability in PGE2–stimulated Jurkat cells. Co-culturing Jurkat cell and LPS-stimulated differentiated THP-1 cells resulted in a decreased viability of T cells. The addition of PTX restored T cell viability to normal control levels and IL-2 expression level in Jurkat cells. Conclusion: LPS-stimulated THP-1-derived macrophages reduced the T cell viability under inflammation. However, PTX restored T cells viability and IL-2 back to normal levels. Therefore, the immunomodulatory action of PTX may be mediated by macrophage-T cell interactions.
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Poenie, Martin F., Nicholas A. Maskalenko, and Shubhankar Nath. "The dynein-binding protein DISC1 plays important roles in relocating organelles to the immunological synapse during T cell activation." Journal of Immunology 200, no. 1_Supplement (May 1, 2018): 47.5. http://dx.doi.org/10.4049/jimmunol.200.supp.47.5.
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Abstract DISC1 (Disrupted in Schizophrenia-1) is a dynein-binding scaffold protein that interacts with many other proteins. In neurons, DISC1 is important for proliferation, migration, and signaling. We found that DISC1 is expressed in Jurkat cells and human NK cells and that it coimmunoprecipitates with dynein in Jurkat cells. Immunostaining for DISC1 in unstimulated Jurkat cells showed that it was generally located around the MTOC. When Jurkat cells were stimulated with SEE-coated Raji cells, depending on the antibody used, we found DISC1 either clustered around mitochondria or colocalized with dynein and NDE1 at the immunological synapse (IS). Biochemical studies showed that after Jurkat cells are activated (SEE-coated Raji cells or PMA), DISC1 coimmunoprecipitates with talin and paxillin. Sequence analysis of cloned DISC1 cDNAs from Jurkat cells revealed that at least two isoforms (L and Lv) are expressed. When GFP-DISC1 isoforms were individually expressed in Jurkat cells, we found that the Lv isoform concentrated around mitochondria whereas the L isoform colocalized with dynein at the synapse as seen in the immunostaining data. While RNAi was relatively ineffective at reducing DISC1 expression, we could abolish expression by using a DISC1-targeted CAS9/CRISPR construct. In these DISC1-disrupted cells, we found that mitochondria failed to accumulate at the immunological synapse and the MTOC did not appear to move all the way to the contact site (perhaps suggesting a defect in docking). When GFP-DISC1 Lv was expressed in the DISC1 CAS9/CRISPR cells mitochondria accumulation at the IS was restored. Similarly, expression of the GFP-DISC1 L restored the normal positioning of the MTOC upon T cell activation.
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Hagner, Patrick, Krystyna Mazan-Mamczarz, Sharon Corl, and Ron B. Gartenhaus. "Dominant-Negative Inhibition of MCT-1 Oncogene Attenuates a Malignant Phenotype through Translational Repression." Blood 110, no. 11 (November 16, 2007): 4168. http://dx.doi.org/10.1182/blood.v110.11.4168.4168.
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Abstract Background: Gene expression is controlled at multiple levels. Translation initiation is a critical checkpoint for regulating levels of protein synthesis. The MCT-1 (Multiple copies in T-cell lymphoma 1) oncogene product has been shown to bind to the cap complex through its PUA domain and recruit DENR, a SUI1 motif containing protein that can increase translation initiation of target mRNAs by scanning and recognition of the initiation codon. An important function of MCT-1 is its modulation of a subset of cancer related mRNAs in human tumors. Levels of MCT-1 protein are increased in a number of non-Hodgkin’s lymphoma cell lines and diffuse large B-cell lymphoma. The abnormal regulation of protein synthesis in lymphoma cells has the potential to be exploited for cancer therapy. We have shown that an MCT-1 deletion mutant, containing only the PUA domain interacts with the cap-complex but does not promote translation. We hypothesized that a PUA-domain mutant acting as dominant-negative would interfere with MCT-1 function through translational repression and modify the malignant phenotype. Method: Using a retroviral vector we established stable Jurkat cell lines expressing either PUA (Jurkat-PUA) or empty vector (Jurkat-V) in order to investigate the feasibility of targeting MCT-1 using a dominant-negative approach and its impact on the transformed phenotype. Multiple clones were plated in soft agar to determine anchorage-independent growth capacity. We also examined growth under reduced serum conditions to evaluate growth kinetics under stress conditions. Jurkat cell lines expressing either PUA or empty vector were exposed to either doxorubicin or gamma-irradiation and cell viability was assessed using both trypan blue exclusion and TUNEL assay. Effects on translation were assayed employing a combination of Western blotting and in-vivo translation assays. Results: There was a greater than three-fold difference in colony formation comparing Jurkat-V with Jurkat-PUA cells. Under serum deprivation conditions Jurkat-PUA grew much slower than Jurkat-V, and cell cycle analysis demonstrated Jurkat-PUA clones progressing through the cell cycle significantly slower than Jurkat-V clones. Sensitivity to both doxorubicin and gamma-radiation was increased at least 2-fold in cells expressing the PUA deletion mutant. Quantitative real-time PCR performed in Jurkat-V and Jurkat-PUA cells demonstrated equivalent levels of selected target mRNAs including Dp-1 and Cyclin D1 however, there were lower protein levels in the Jurkat-PUA clones. Finally, Jurkat-PUA cells displayed reduced in-vivo translation. Conclusion: We have shown that Jurkat cells retrovirally transduced with a dominant-negative MCT-1 mutant can interfere with protein synthesis and modify the malignant phenotype of a highly aggressive lymphoma. As proof of principle, we have established the utility of targeting MCT-1 and the translation initiation complex in lymphoma cells as a potentially useful therapeutic approach.
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Yellin, M. J., J. J. Lee, L. Chess, and S. Lederman. "A human CD4- T cell leukemia subclone with contact-dependent helper function." Journal of Immunology 147, no. 10 (November 15, 1991): 3389–95. http://dx.doi.org/10.4049/jimmunol.147.10.3389.
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Abstract Helper T lymphocytes provide a contact dependent signal to resting B cells that is required for optimal differentiation into Ig-secreting cells. The surface structure(s) on T cells that mediate helper function have not been identified but are known to be induced by T cell activation. A CD4- subclone of the Jurkat leukemic T cell line (D1.1) was isolated and found to be distinct from CD4+ Jurkat clones and a variety of other T and non-T cell leukemic lines in that coculture of D1.1 with resting B cells induced B cells to specifically express surface CD23 molecules, a marker of B cell activation. Furthermore, Jurkat D1.1 induced B cell proliferation and terminal B cell differentiation into IgG-secreting cells in the presence of T cell-dependent B cell mitogens. Similar to the helper effector function of activated T cells, the effects of Jurkat D1.1 were neither Ag nor MHC restricted. Paraformaldehyde fixed Jurkat D1.1 cells remained competent to activate B cells while D1.1 supernatants and diffusible factors were inactive. The effect of Jurkat D1.1 on B cell activation was distinct from that of rIL-4 and was not inhibited by antibodies to IL-4. Together these observations suggested that surface structures on D1.1 and not secreted factors, mediated contact-dependent helper effector function.
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Sabran, Affidah, Endang Kumolosasi, and Ibrahim Jantan. "Effects of annexin A1 on apoptosis and cell cycle arrest in human leukemic cell lines." Acta Pharmaceutica 69, no. 1 (March 1, 2019): 75–86. http://dx.doi.org/10.2478/acph-2019-0005.
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Abstract Recent studies suggest that annexin A1 (ANXA1) promotes apoptosis in cancerous cells. This study aims to investigate the effects of ANXA1 on apoptosis and cell cycle arrest in K562, Jurkat and U937 cells and peripheral blood mononu-clear cells (PBMC). Cells were treated with ANXA1 and cyclophosphamide prior to flow cytometry analysis for apoptosis and cell cycle arrest induction. At 2.5µM, ANXA1 induced significant apoptosis in K562 (p ≤ 0.001) and U937 (p ≤ 0.05) cells, with EC50 values of 3.6 and 3.8 µM, respectively. In Jurkat cells, induction was not significant (EC50, 17.0 µM). No significant apoptosis induction was observed in PBMC. ANXA1 caused cycle arrest in the G0/G1 phase in K562 and U937 cells with p ≤ 0.001 for both, and (p ≤ 0.01) for Jurkat cells. ANXA1 induced apoptosis and cycle arrest in the G0/G1 phase in K562 and U937 cells, causing only cell cycle arrest in Jurkat cells.
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Yang, Tianhang, Ji Peng, Zhiquan Shu, Praveen K. Sekar, Songjing Li, and Dayong Gao. "Determination of the Membrane Transport Properties of Jurkat Cells with a Microfluidic Device." Micromachines 10, no. 12 (November 29, 2019): 832. http://dx.doi.org/10.3390/mi10120832.
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The Jurkat cell is an immortalized line of human acute lymphocyte leukemia cells that is widely used in the study of adoptive cell therapy, a novel treatment of several advanced forms of cancer. The ability to transport water and solutes across the cell membrane under different temperatures is an important factor for deciding the specific protocol for cryopreservation of the Jurkat cell. In this study we propose a comprehensive process for determination of membrane transport properties of Jurkat cell. using a novel microfluidic controlled single cell-trapping system. The osmotic behavior of an individual Jurkat cell to water and dimethyl sulfoxide (DMSO), a commonly used cryoprotective agent (CPA), under constant temperature, was recorded under a microscope utilizing the modified microfluidic system. The images of the Jurkat cell under osmotic change were processed to obtain a relationship between cell volume change and time. The experimental results were fitted using a two-parameter transport numeric model to calculate the Jurkat cell membrane permeability to water and DMSO at room temperature (22 °C). This model and the calculated parameters can help scientists optimize the cryopreservation protocol for any cell type with optimal cryoprotective agents and cooling rate for future experiments.
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Shiau, Jeng-Yuan, Shu-Yi Yin, Shu-Lin Chang, Yi-Jou Hsu, Kai-Wei Chen, Tien-Fen Kuo, Ching-Shan Feng, et al. "Mechanistic Study of the Phytocompound, 2-β-D-Glucopyranosyloxy-1-hydroxytrideca-5,7,9,11-tetrayne in Human T-Cell Acute Lymphocytic Leukemia Cells by Using Combined Differential Proteomics and Bioinformatics Approaches." Evidence-Based Complementary and Alternative Medicine 2015 (2015): 1–10. http://dx.doi.org/10.1155/2015/475610.
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Bidens pilosa, a medicinal herb worldwide, is rich in bioactive polyynes. In this study, by using high resolution 2-dimensional gel electrophoresis coupled with mass spectrometry analysis, as many as 2000 protein spots could be detected and those whose expression was specifically up- or downregulated in Jurkat T cells responsive to the treatment with 2-β-D-glucopyranosyloxy-1-hydroxytrideca-5,7,9,11-tetrayne (GHTT) can be identified. GHTT treatment can upregulate thirteen proteins involved in signal transduction, detoxification, metabolism, energy pathways, and channel transport in Jurkat cells. Nine proteins, that is, thioredoxin-like proteins, BH3 interacting domain death agonist (BID protein involving apoptosis), methylcrotonoyl-CoA carboxylase beta chain, and NADH-ubiquinone oxidoreductase, were downregulated in GHTT-treated Jurkat cells. Further, bioinformatics tool, Ingenuity software, was used to predict signaling pathways based on the data obtained from the differential proteomics approach. Two matched pathways, relevant to mitochondrial dysfunction and apoptosis, in Jurkat cells were inferred from the proteomics data. Biochemical analysis further verified both pathways involving GHTT in Jurkat cells. These findings do not merely prove the feasibility of combining proteomics and bioinformatics methods to identify cellular proteins as key players in response to the phytocompound in Jurkat cells but also establish the pathways of the proteins as the potential therapeutic targets of leukemia.
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Guse, A. H., E. Roth, and F. Emmrich. "Intracellular Ca2+ pools in Jurkat T-lymphocytes." Biochemical Journal 291, no. 2 (April 15, 1993): 447–51. http://dx.doi.org/10.1042/bj2910447.
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Jurkat T-lymphocytes comprise at least four intracellular Ca2+ pools. Pool I was agonist-sensitive and contained 23 +/- 8% (n = 18) of the total Ca(2+)-storage capacity, as shown in intact cells in the presence of EGTA. The time courses of the agonist-induced formation of Ins(1,4,5)P3 and of the Ca2+ release from pool I were nearly superimposable, indicating that the agonist-sensitive pool I is emptied by Ins(1,4,5)P3. Likewise, in permeabilized cells, the size of the Ins(1,4,5)P3-sensitive Ca2+ pool I was 27 +/- 11% (n = 14). Pool II contained 26 +/- 5% (n = 9) of intracellularly stored Ca2+ and was liberated by thapsigargin, an inhibitor of the endoplasmic-reticulum (ER) Ca(2+)-ATPase. Addition of thapsigargin before addition of agonist abolished the agonist-induced Ca2+ release in both intact and permeabilized cells, indicating that pool I is a subcompartment of the ER Ca2+ pool. The content of this ER Ca2+ pool (pools I and II) amounted to 51 +/- 15% (n = 9) in intact cells and 49 +/- 16% (n = 16) in permeabilized cells. Caffeine released Ca2+ even when the ER pool (pools I and II) was emptied by previous addition of thapsigargin, indicating the presence of a third pool independent of pools I and II. Pool III contained 23 +/- 6% (n = 8) in intact cells, but 41 +/- 8% (n = 5) in permeabilized cells. The remaining intracellularly stored Ca2+ was released by addition of the Ca2+ ionophore ionomycin. This fourth pool contained 27 +/- 8% (n = 9) in intact cells, but less than 10% in permeabilized cells. The size of pool III was increased when pools I and II were emptied before addition of caffeine, whereas the size of pool IV was decreased under such conditions. In conclusion, this first comprehensive description of intracellular Ca2+ pools in Jurkat T-lymphocytes demonstrates the presence of four different Ca2+ pools, provides estimates of their sizes and describes relationships between each other. Release of Ca2+ from pool I [Ins(1,4,5)P3-sensitive] has previously been shown to play a major role in T-cell activation, whereas the physiological role of pools II-IV remains to be established.
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Moyo, Batanai, and Stanley Mukanganyama. "Antiproliferative Activity ofT. welwitschiiExtract on Jurkat T CellsIn Vitro." BioMed Research International 2015 (2015): 1–10. http://dx.doi.org/10.1155/2015/817624.
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Triumfetta welwitschiiis a plant used traditionally for the treatment of fever and diarrhoea. Previous work has shown thatT. welwitschiihas antibacterial activity. The purpose of this study was to investigateT. welwitschiiextract for anticancer activity against Jurkat T cells. The Jurkat T cell line is used to study acute T cell leukaemia. An antiproliferation assay, determination of induction of apoptosis, the determination of the effect of the combination of the extract and GSH, and effects of the extract on DNA leakage were conducted.T. welwitschiiwas found to decrease cell viability in a dose- and time-dependent manner.T. welwitschiicaused apoptosis in the Jurkat T cells as shown by DNA fragmentation. WhenT. welwitschiiwas combined with reduced GSH, it was found that the growth of the Jurkat T cells was significantly reduced compared to untreated cells after 72 h of treatment. This was unexpected, as cancer cells have elevated levels of GSH compared to normal cells. The results of this study show thatT. welwitschiiis a potential source of compounds that may serve as leads for anticancer compounds.
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Litvinova, L. S., K. A. Yurova, V. V. Shchupletsova, N. D. Gazatova, O. G. Khaziakhmatova, V. V. Malashchenko, E. O. Shunkin, et al. "Significance of nutrient media choice for the long-term cultures of leukemic T-lymphoblasts." Medical Immunology (Russia) 23, no. 3 (June 22, 2021): 593–604. http://dx.doi.org/10.15789/1563-0625-son-2142.
Full textAbstract:
Correct choice of nutrient media for culturing different types of cells in various applications is one of the most important aspects of modern biotechnology, since chemical composition of the culture media largely contains the necessary metabolites to support certain cells’ growth lines outside the body. Jurkat line of human leukemic T-lymphoblast-like cells (hereinafter Jurkat T-cells) is actively used for in vitro modeling of intracellular signaling and activation of normal blood T-lymphocytes mediated by the T-cell receptor/CD3/ CD4 complex in toxicological studies of immune and secretory responses, to test medicinal substances and ions. Also, Jurkat T-cells are widely used for ex vivo testing in immunology, oncology, toxicology, orthopedics, and traumatology. The existing standards and numerous studies are mainly based on short-term in vitro cultivation of Jurkat T-cells in RPMI 1640 nutrient medium. Meanwhile, the issues of long-term maintenance of the growth of Jurkat T-cells culture are poorly presented in the research literature. This study aimed for studying the activity of Jurkat T-cells over 7 to 14 days of in vitro culture and comparing the relative value of RPMI 1640 and αMEM media for the behavior of immunocompetent tumor cells. Using flow cytometry, multiplex analysis, and phase contrast Cell-IQ microscopy, the proportions of living cells and those dying by apoptosis and necrosis, secretion of cytokines and chemokines, and the dynamics of cell biomass propagation were studied. It was found that the αMEM medium in the complete nutrient medium, as compared with RPMI 1640, is more appropriate to in vitro promotion of cell viability (increased proportion of viable cells by 13.5% at the day 14), their secretory ability for 23 из 27 tested biomolecules, shortened adaptation time (на 32%) in culture before growth initiation, 5-fold increase of the Jurkat Т-cell cellularity by the day 7. Potential significance of the chemical components of nutrient media and secreted biomolecules for these results is discussed. As based on the results obtained, we concluded on superior properties of αMEM medium for long-term in vitro cultures of Jurkat T-cells. Consequently, the in vitro testing of medical devices intended for long-term contact with the body, including those for cancer patients, using Jurkat T-cell leukemia line in RPMI 1640 medium, may lead to wrong predictions on their biocompatibility and potential antitumor activity.
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Rahman, Heshu Sulaiman, Abdullah Rasedee, Max Stanley Chartrand, Hemn Hassan Othman, Swee Keong Yeap, and Farideh Namvar. "Zerumbone Induces G2/M Cell Cycle Arrest and Apoptosis via Mitochondrial Pathway in Jurkat cell Line." Natural Product Communications 9, no. 9 (September 2014): 1934578X1400900. http://dx.doi.org/10.1177/1934578x1400900904.
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This investigation determined the anticancer properties of zerumbone (ZER) on the human T-cell (Jurkat) line using the MTT assay, microscopic evaluations, flow cytometric analyses, and caspase activity estimations. The results showed that ZER is selectively cytotoxic to Jurkat cells in a dose and time-dependent manner with IC50 of 11.9 ± 0.2, 8.6 ± 0.5 and 5.4 ± 0.4 μg/mL at 24, 48 and 72 hours of treatment, respectively. ZER did not produce an adverse effect on normal human peripheral blood mononuclear cells (PBMC). ZER is not as cytotoxic as doxorubicin, which imposed an inhibitory effect on Jurkat cells with IC50 of 2.1 ± 0.2, 1.8 ± 0.15, 1.5 ± 0.07 μg/mL after 24, 48 and 72 hours treatment, respectively. ZER significantly (P<0.05 ) arrested Jurkat cells at the G2/M phase of the cell cycle. The antiproliferative effect of ZER on Jurkat cells was through the apoptotic intrinsic pathway via the activation of caspase-3 and -9. The results showed that ZER can be further developed into a safe chemotherapeutic compound for the treatment of cancers, especially leukemia.
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Poiroux, Guillaume, Annick Barre, Mathias Simplicien, Sandrine Pelofy, Bruno Segui, Els J. M. Van Damme, Pierre Rougé, and Hervé Benoist. "Morniga-G, a T/Tn-Specific Lectin, Induces Leukemic Cell Death via Caspase and DR5 Receptor-Dependent Pathways." International Journal of Molecular Sciences 20, no. 1 (January 8, 2019): 230. http://dx.doi.org/10.3390/ijms20010230.
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Morniga-G, the Gal-specific black mulberry (Morus nigra) lectin, displays high affinity for T (CD176) and Tn (CD175) antigens, frequently expressed at the cancer cell surface. The effects of Morniga-G were investigated on a Tn-positive leukemic Jurkat cell line. The lectin, used in a concentration range between 5–20 μg/mL, induced cell death in leukemic Jurkat cells. Microscopic and cytofluorometric analyses indicated that Jurkat cell death was essentially apoptotic, associated with an increase in the ceramide content and a depolarization of the mitochondrial transmembrane potential. This lectin-mediated cell death was inhibited by the pan caspase-inhibitor zVAD. In addition, cleavage of caspases 8, 9, and 3 was observed in Morniga-G-treated Jurkat cells whereas Jurkat cell lines that are deficient in caspase 8–10, caspase 9, or FADD, survived to the lectin-mediated toxicity. Furthermore, in the presence of TRAIL- or DR5-blocking mononoclonal antibodies, Jurkat cells became resistant to Morniga-G, suggesting that the lectin triggers cell death via the TRAIL/DR5 pathway. In silico computer simulations suggest that Morniga-G might facilitate both the DR5 dimerization and the building of TRAIL/DR5 complexes. Finally, upon treatment of Jurkat cells with benzyl-GalNAc, an O-glycosylation inhibitor, a decrease in Tn antigen expression associating with a reduced Morniga-G toxicity, was observed. Taken together, these results suggest that Morniga-G induces the cell death of Tn-positive leukemic cells via concomitant O-glycosylation-, caspase-, and TRAIL/DR5-dependent pathways.
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Lee, Gun-Hwi, Kyung-A. Hwang, and Kyung-Chul Choi. "Effects of Fludioxonil on the Cell Growth and Apoptosis in T and B Lymphocytes." Biomolecules 9, no. 9 (September 18, 2019): 500. http://dx.doi.org/10.3390/biom9090500.
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Fludioxonil is fungicide used in agriculture, which is present in fruits and vegetables. In this study, the effects of fludioxonil on human immune cell viability, apoptosis, cell cycle arrest, and mitochondrial membrane potential were examined in human immune cells, such as Jurkat T cells and Ramos B cells. To examine the cell viability, Jurkat T cells and Ramos B cells were treated with fludioxonil (10−9–10−5 M) for 24 h and 48 h. Water soluble tetrazolium salt assay showed that fludioxonil decreased Jurkat T cell and Ramos B cell viability. Jurkat T cell viability decreased at 24 and 48 h, but Ramos B cell viability decreased only at 48 h. JC-1 dye revealed decreased mitochondrial membrane potential in fludioxonil-treated Jurkat T cells and Ramos B cells. To evaluate apoptosis, annexin-V conjugated FITC, AF488, and propidium iodide (PI) were used and to evaluate cell cycle arrest PI was used. Apoptosis and cell cycle arrest were induced by fludioxonil (10−7–10−5 M) in the Jurkat T cells at 24 and 48 h and Ramos B cells at 48 h. Moreover, the protein levels of pro-apoptotic proteins, such as p53, BAX, and cleaved caspase 3, were increased and anti-apoptotic protein Bcl-2 was decreased by fludioxonil. Expression of the Fas receptor related to the extrinsic apoptosis pathway was increased by fludioxonil. Additionally, cyclin D1 and cyclin E1 were decreased by fludioxonil. In the present study, fludioxonil induced immunotoxicity in human T cells and B cells through apoptosis and cell cycle arrest. Therefore, the present study suggests that fludioxonil induces the cellular toxicity in immune cells.
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Dosiou, C., A. E. Hamilton, Y. Pang, M. T. Overgaard, S. Tulac, J. Dong, P. Thomas, and L. C. Giudice. "Expression of membrane progesterone receptors on human T lymphocytes and Jurkat cells and activation of G-proteins by progesterone." Journal of Endocrinology 196, no. 1 (October 5, 2007): 67–77. http://dx.doi.org/10.1677/joe-07-0317.
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Although there is significant evidence for progesterone's role as an immunomodulator, nuclear progesterone receptors have not been consistently identified in immune cells. Recently, three new putative membrane progesterone receptors (mPRs), mPRα, mPRβ, and mPRγ have been described. The objective of this study was to examine whether mPRs are expressed in peripheral blood leukocytes (PBLs) in women of reproductive age, and to further characterize them in T lymphocytes and immortalized T cells (Jurkat cells). Transcripts for mPRα and mPRβ but not mPRγ, were detected by RT-PCR in PBLs, T lymphocytes, and Jurkat cells. Western blot analysis showed the presence of the mPRα and mPRβ proteins on cell membranes of T lymphocytes and Jurkat cells. Expression of the mPRα mRNA was upregulated in the luteal phase of the menstrual cycle in cluster of differentiation (CD)8+, but not in CD4+, T lymphocytes. Radioreceptor assays revealed specific [3H]progesterone binding to T- and Jurkat cell membranes (Kd 4.25 nM) characteristic of steroid membrane receptors. Progesterone activated an inhibitory G-protein (Gi), suggesting that mPRs are coupled to Gi in Jurkat cells. These results suggest a potential novel mechanism for progesterone's immunoregulatory function through activation of mPRs.
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Aune, T. M., K. A. Kelley, G. E. Ranges, and M. P. Bombara. "Serotonin-activated signal transduction via serotonin receptors on Jurkat cells." Journal of Immunology 145, no. 6 (September 15, 1990): 1826–31. http://dx.doi.org/10.4049/jimmunol.145.6.1826.
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Abstract Serotonin (5-hydroxytryptamine) (5HT) a neurotransmitter and vasoactive amine, is a major storage product of platelets that are released at sites of inflammation. Several different subtypes of serotonin receptors have been defined. 5HT receptors have been divided into three major families based on molecular, biochemical, and pharmacologic properties. Binding of serotonin to the 5HT1 family results in inhibition of adenylate cyclase whereas binding to the 5HT2 family results in stimulation of phosphatidylinositol turnover and mobilization of intracellular Ca2+. 5HT has been shown to have effects on lymphoid cells. The question of whether human T lymphocytes express receptors for 5HT and transduce signals through 5HT receptors has not been adequately addressed. As a model system, Jurkat cells (a transformed human T lymphocyte line) were examined to determine if they expressed 5HT receptors and whether 5HT stimulated an increase in inositol phosphates or affected adenylate cyclase activity. The results show that Jurkat cells bind 5HT with an average dissociation constant of 90 nM and that 5HT stimulates an increase in inositol phosphate and intracellular Ca2+ levels. These results link the 5HT receptor on Jurkat cells to the 5HT2 family; however, studies with 5HT receptor agonists and antagonists failed to clearly classify the 5HT receptor on Jurkat cells as a known member of the 5HT2 family.