scholarly journals Immunophenotypic and Immunotypic Evalua-tions of Human Myeloma Cell Lines KMM-1, JJN3, LP1, L363, KMS-12BM and RPMI-8226 for Cell-Line Authentication

2019 ◽  
Vol 22 (5) ◽  
pp. 278-295
Author(s):  
Nader Vazifeh shiran ◽  
Saeid Abroun ◽  
◽  
Keyword(s):  
Cell Line ◽  
Cell Lines ◽  
Myeloma Cell ◽  
Cell Line Authentication ◽  
Rpmi 8226 ◽  
Human Myeloma Cell

Wogonin induces apoptosis in RPMI 8226, a human myeloma cell line, by downregulating phospho-Akt and overexpressing Bax

Life Sciences ◽  
2013 ◽  
Vol 92 (1) ◽  
pp. 55-62 ◽  
Author(s):  
Meng Zhang ◽  
Li-Ping Liu ◽  
Yuling Chen ◽  
Xiao-ying Tian ◽  
Jian Qin ◽  
...  
Keyword(s):  
Cell Line ◽  
Myeloma Cell ◽  
Myeloma Cell Line ◽  
Human Myeloma Cell Line ◽  
Rpmi 8226 ◽  
Human Myeloma Cell

scholarly journals Evidence for the Involvement of Both Retinoic Acid Receptor- and Retinoic X Receptor-Dependent Signaling Pathways in the Induction of Tissue Transglutaminase and Apoptosis in the Human Myeloma Cell Line RPMI 8226

Blood ◽  
1998 ◽  
Vol 91 (7) ◽  
pp. 2423-2432 ◽  
Author(s):  
Bertrand Joseph ◽  
Olga Lefebvre ◽  
Claude Méreau-Richard ◽  
Pierre-Marie Danzé ◽  
Marie-Thérèse Belin-Plancot ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Retinoic Acid ◽  
Cell Line ◽  
Retinoic Acid Receptor ◽  
Tissue Transglutaminase ◽  
Myeloma Cell ◽  
Myeloma Cell Line ◽  
Human Myeloma Cell Line ◽  
Rpmi 8226 ◽  
Human Myeloma Cell

In this study, we show that both all-trans-retinoic acid (atRA) and 9-cis-retinoic acid (9-cis-RA) are potent inducers of tissue transglutaminase (TGase II), an enzyme involved in apoptosis, at the level of both enzyme activity and mRNA in the human myeloma cell line RPMI 8226. RPMI 8226 cells were shown to express mRNAs for all the retinoid receptors subtypes, ie, RARα, RARβ, RARγ, RXRα, RXRβ, and RXRγ. To identify which of these receptors are involved in regulating TGase II expression, several receptor-selective synthetic retinoids were used. Neither CD367, a very potent retinoid that selectively binds and activates receptors of the RAR family, nor CD2425, an RXR-selective agonist, induced TGase II when used alone. However, combination of CD367 and CD2425 resulted in nearly full induction of the enzyme. Moreover, when used in combination with atRA, CD367 partially inhibited the atRA-dependent induction of TGase II, whereas CD2425 enhanced it. The effects of Am 580, CD417, and CD437, three synthetic retinoids selective for the RARs subtypes RARα, RARβ, and RARγ, respectively, were also investigated. None of these compounds was able to induce TGase II when used alone; however, the combination of each of them with CD2425 resulted in strong induction of the enzyme activity, reaching 30% to 50% of the values obtained in the presence of retinoic acid and suggesting functional redundancy between the RAR subtypes. Finally, treatment with atRA or the combination of CD367 and CD2425, but not with CD367 or CD2425 alone, was also shown to trigger apoptosis in RPMI 8226 cells, with prominent accumulation of TGase II immunoreactivity in apoptotic cells. Taken together these data suggest that the induction of TGase II expression and apoptosis in the RPMI 8226 myeloma cell line required ligand-dependent activation of both the RAR and RXR receptors.

PRL-3 Regulates Myeloma Cell Survival, Proliferation, Adhesion and Migration

Blood ◽  
2012 ◽  
Vol 120 (21) ◽  
pp. 1321-1321
Author(s):  
Tobias Schmidt Slordahl ◽  
Kristine Misund ◽  
Torstein Baade Ro ◽  
Magne Borset
Keyword(s):  
Growth Factor ◽  
Cell Survival ◽  
Cell Line ◽  
Cell Lines ◽  
Western Blotting ◽  
Plasma Cells ◽  
Myeloma Cell ◽  
Retroviral Transduction ◽  
And Migration ◽  
Rpmi 8226

Abstract Abstract 1321 Introduction: Multiple myeloma (MM) is a neoplastic monoclonal proliferation of bone marrow plasma cells. Despite advances in treatment in recent years, MM is still a fatal disease. Phosphatase of regenerating liver-3 (PRL-3) is a protein expressed in primary MM cells and MM cell lines, but not in normal plasma cells. A recent study showed that siRNA against PRL-3 suppresses MM-cell migration (Fagerli et al, 2008) and another study has identified PRL-3 as a marker gene for a subgroup of patients with MM (Broyl et al, 2010). Methods: The human myeloma cell lines INA-6, ANBL-6, IH-1, OH-2 and RPMI-8226 were used in this study. Apoptosis was measured by Annexin V-FITC binding by flow cytometry, proliferation was measured by methyl-3H-thymidine incorporation, migration against a stromal cell derived factor-1α (SDF-1α) gradient was studied in a Transwell two-chamber assay and adhesion was measured as percentage adhered cells to fibronectin after stimulation with the pro-adhesive cytokines hepatocyte growth factor (HGF), insulin like growth factor-1 (IGF-1) and SDF-1α. RT-PCR and Western blotting were used to measure expression of pro- and anti-apoptotic proteins. Western blotting was used to map intracellular signaling pathways. INA-6 cells stably expressing exogenous PRL-3 were generated using retroviral transduction. The small molecular inhibitor PRL-3 Inhibitor I was used for PRL-3 inhibition. Results: PRL-3 inhibitor I reduced survival of the myeloma cell lines INA-6, ANBL-6, IH-1, OH-2 and RPMI-8226. IC50 was between 15 and 50 μM depending on cell line. Treatment with the inhibitor down-regulated the anti-apoptotic protein Mcl-1 and led to activation of the intrinsic apoptotic pathway. Inhibition of PRL-3 reduced interleukin (IL)-6-induced phosphorylation of STAT-3. Treatment with 10 μM of PRL-3 inhibitor I also significantly reduced migration against a SDF-1α gradient and HGF-, IGF-1- and SDF-1α -mediated adhesion of the cell line INA-6. By retroviral transduction we made PRL-3-overexpressing INA-6 cells. INA-6 cells are dependent on IL-6 to grow, but overexpression of PRL-3 led to a major increase in cell proliferation even in the absence of IL-6 as well as increased survival at suboptimal concentrations of IL-6. Conclusion: PRL-3 is expressed in MM cells but not in normal plasma cells and can represent a cancer-specific target. Overexpression of PRL-3 in the IL-6-dependent human myeloma cell line INA-6 renders the cells less dependent of IL-6 and increases survival and proliferation. On the other hand, the use of an inhibitor against PRL-3 significantly decreases survival of five MM-cell lines and reduces adhesion and migration of the cell line INA-6. IL-6-STAT3 signaling is important in MM cell survival and proliferation and we here show that PRL-3 possibly influences cell survival as a positive regulator of this signaling pathway. This study indicates that PRL-3 could be important in the pathogenesis of MM and a potential target in the treatment of MM. Disclosures: No relevant conflicts of interest to declare.

scholarly journals Evidence for the Involvement of Both Retinoic Acid Receptor- and Retinoic X Receptor-Dependent Signaling Pathways in the Induction of Tissue Transglutaminase and Apoptosis in the Human Myeloma Cell Line RPMI 8226

Blood ◽  
1998 ◽  
Vol 91 (7) ◽  
pp. 2423-2432 ◽  
Author(s):  
Bertrand Joseph ◽  
Olga Lefebvre ◽  
Claude Méreau-Richard ◽  
Pierre-Marie Danzé ◽  
Marie-Thérèse Belin-Plancot ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Retinoic Acid ◽  
Cell Line ◽  
Retinoic Acid Receptor ◽  
Tissue Transglutaminase ◽  
Myeloma Cell ◽  
Myeloma Cell Line ◽  
Human Myeloma Cell Line ◽  
Rpmi 8226 ◽  
Human Myeloma Cell

AbstractIn this study, we show that both all-trans-retinoic acid (atRA) and 9-cis-retinoic acid (9-cis-RA) are potent inducers of tissue transglutaminase (TGase II), an enzyme involved in apoptosis, at the level of both enzyme activity and mRNA in the human myeloma cell line RPMI 8226. RPMI 8226 cells were shown to express mRNAs for all the retinoid receptors subtypes, ie, RARα, RARβ, RARγ, RXRα, RXRβ, and RXRγ. To identify which of these receptors are involved in regulating TGase II expression, several receptor-selective synthetic retinoids were used. Neither CD367, a very potent retinoid that selectively binds and activates receptors of the RAR family, nor CD2425, an RXR-selective agonist, induced TGase II when used alone. However, combination of CD367 and CD2425 resulted in nearly full induction of the enzyme. Moreover, when used in combination with atRA, CD367 partially inhibited the atRA-dependent induction of TGase II, whereas CD2425 enhanced it. The effects of Am 580, CD417, and CD437, three synthetic retinoids selective for the RARs subtypes RARα, RARβ, and RARγ, respectively, were also investigated. None of these compounds was able to induce TGase II when used alone; however, the combination of each of them with CD2425 resulted in strong induction of the enzyme activity, reaching 30% to 50% of the values obtained in the presence of retinoic acid and suggesting functional redundancy between the RAR subtypes. Finally, treatment with atRA or the combination of CD367 and CD2425, but not with CD367 or CD2425 alone, was also shown to trigger apoptosis in RPMI 8226 cells, with prominent accumulation of TGase II immunoreactivity in apoptotic cells. Taken together these data suggest that the induction of TGase II expression and apoptosis in the RPMI 8226 myeloma cell line required ligand-dependent activation of both the RAR and RXR receptors.

Induction of mitochondrial changes in myeloma cells by imexon

Blood ◽  
2001 ◽  
Vol 97 (11) ◽  
pp. 3544-3551 ◽  
Author(s):  
Katerina Dvorakova ◽  
Caroline N. Waltmire ◽  
Claire M. Payne ◽  
Margaret E. Tome ◽  
Margaret M. Briehl ◽  
...  
Keyword(s):  
Cell Line ◽  
Acute Promyelocytic Leukemia ◽  
Cell Lines ◽  
Nuclear Dna ◽  
Leukemia Cell ◽  
Myeloma Cell ◽  
Promyelocytic Leukemia ◽  
Leukemia Cell Line ◽  
Myeloma Cells ◽  
Rpmi 8226

Imexon is a cyanoaziridine derivative that has antitumor activity in multiple myeloma. Previous studies have shown that imexon induces oxidative stress and apoptosis in the RPMI 8226 myeloma cell line. This study reports that imexon has cytotoxic activity in other malignant cell lines including NCI-H929 myeloma cells and NB-4 acute promyelocytic leukemia cells, whereas normal lymphocytes and U266 myeloma cells are substantially less sensitive. Flow cytometric experiments have shown that imexon treatment is associated with the formation of reactive oxygen species (ROS) and the loss of mitochondrial membrane potential (Δψm) in imexon-sensitive myeloma cell lines and NB-4 cells. In contrast, reduction of Δψm and increased levels of ROS were not observed in imexon-resistant U266 cells. Treatment of imexon-sensitive RPMI 8226 cells with the antioxidant N-acetyl-l-cysteine (NAC) protects cells against these effects of imexon. Mitochondrial swelling was observed by electron microscopy in RPMI 8226 myeloma cells treated with 180 μM imexon as early as 4 hours. Damage to mitochondrial DNA was detected by a semiquantitative polymerase chain reaction assay in imexon-treated RPMI 8226 cells; however, nuclear DNA was not affected. Finally, partial protection of RPMI 8226 cells against the imexon effects was achieved by treatment with theonyltrifluoroacetone, an inhibitor of superoxide production at mitochondrial complex II. These changes are consistent with mitochondrial oxidation and apoptotic signaling as mediators of the growth inhibitory effects of imexon. Interestingly, oxidative damage and decrease of Δψm induced by imexon highly correlates with sensitivity to imexon in several myeloma cell lines and an acute promyelocytic leukemia cell line.

Bortezomib could down-regulate the expression of RANKL, inhibit cell proliferation and induce cell apoptosis in the human myeloma cell line RPMI 8226 by activating casepase-3

2017 ◽  
Vol 20 (2) ◽  
pp. 217-224 ◽  
Author(s):  
Li Lin ◽  
Dong Chen ◽  
Zhen-Fei Xiang ◽  
Ren-Zhi Pei ◽  
Pi-Sheng Zhang ◽  
...  
Keyword(s):  
Cell Proliferation ◽  
Cell Line ◽  
Cell Apoptosis ◽  
Myeloma Cell ◽  
Myeloma Cell Line ◽  
Human Myeloma Cell Line ◽  
Induce Cell Apoptosis ◽  
Rpmi 8226 ◽  
Inhibit Cell Proliferation ◽  
Human Myeloma Cell

A Novel Role for Histone Deacetylase 11 (HDAC11) in B Cell Lymphopoiesis and Plasma Cell Survival in Multiple Myeloma

Blood ◽  
2014 ◽  
Vol 124 (21) ◽  
pp. 4715-4715
Author(s):  
Jason B. Brayer ◽  
Eva Sahakian ◽  
John Powers ◽  
Mark B Meads ◽  
Susan Deng ◽  
...  
Keyword(s):  
Multiple Myeloma ◽  
Cell Lines ◽  
Plasma Cell ◽  
Plasma Cells ◽  
Proteasome Inhibitors ◽  
Myeloma Cell ◽  
Resistant Cell ◽  
Rpmi 8226 ◽  
Human Myeloma Cell

Abstract While multiple myeloma (MM) remains incurable presently, expanded therapeutic options over the past decade have improved patient survival markedly. Proteasome inhibitors have redefined the treatment paradigm for myeloma, often serving as the backbone of front-line treatment. Histone deacetylase (HDAC) inhibitors (HDI), although only marginally active as single agent therapy in hematological malignancies, have demonstrated an ability to salvage bortezomib responsiveness in refractory patients, prompting heightened interest in this class of targeted therapeutics in myeloma. HDAC’s represent a family of enzymes, currently with 11 known members in the classical HDAC family, and subdivided into 4 sub-classes. HDAC11 is currently the only member of the sub-class IV and, as the newest member of the HDAC family, its impact on B cell lymphopoiesis and myeloma development is only starting to be unveiled. Intriguingly, we show that mice with germ-line silencing of HDAC11 (HDAC11KO mice) exhibit a 50% decrease in plasma cells in both the bone marrow and peripheral blood plasma cell compartments relative to wild-type mice. Consistent with this, Tg-HDAC11-eGFP mice, a transgenic strain engineered to express GFP under control of the HDAC11 promoter (Heinz, N Nat. Rev. Neuroscience 2001) reveals that HDAC11 expression is increased in the plasma cell population and to a lesser extent B1 B cells, as compared to earlier lineage stages. Similar observations based on measurements of HDAC11 mRNA were seen in normal human plasma cells. Significant increases in HDAC11 mRNA expression were observed in 7 of 11 primary human multiple myeloma samples and 11 of 12 human myeloma cell lines as compared to normal plasma cells, further emphasizing the potential relevance of HDAC11 to the underlying pathologic processes driving myeloma development and/or survival. Targeted silencing of HDAC11 in RPMI-8226 cells lines using siRNA results in a modest decrease in cell viability as measured by Annexin/PI staining and detection of activated caspase-3. Quisinostat, a second generation pan-HDI, has previously demonstrated activity against human myeloma cell lines in vitro (Stuhmer, Brit J Haematol, 2010), and suppressed bone destruction in an in vivo murine myeloma model (Deleu, Cancer Res, 2009). We similarly observe dose-dependent survival impairment in 10 human myeloma cell lines when cultured in the presence of quisinostat, with EC50’s consistently in the 1-10nM range. Importantly, quisinostat acts synergistically with proteasome inhibitiors (bortezomib and carfilzomib) in RPMI-8226 cells; more importantly, the degree of synergism is amplified in the RPMI-6226-B25 bortezomib-resistant cell line. Although a clear mechanism of action remains to be elucidated, preliminary data suggests that RPMI-8226 cells exposed to quisinostat appear to exhibit a decrease nuclear, but not cytosolic HDAC11. Collectively, these data illustrate a previously unknown role for HDAC11 in plasma cell differentiation and survival. Increased HDAC11 expression seen in myeloma patient specimens and primary myeloma cell lines highlights the potential of HDAC11 as a therapeutic target. Furthermore, we show that quisinostat, a pan-HDI with selectivity towards HDAC11 at lower dosing, acts synergistically with proteasome inhibitors in vitro in proteasome inhibitor sensitive and resistant cell lines. Future work will focus on further elucidating the role of HDAC11 in myeloma survival and drug response, with particular emphasis on proteasome inhibitors. Disclosures No relevant conflicts of interest to declare.

Cell Line-Dependent Synergy Between the PARP Inhibitor Veliparib and the Proteasome Inhibitor Bortezomib in the Killing of Myeloma Cells

Blood ◽  
2015 ◽  
Vol 126 (23) ◽  
pp. 5556-5556 ◽  
Author(s):  
Alex Xu ◽  
Amitabha Mazumder ◽  
James A. Borowiec
Keyword(s):  
Dna Repair ◽  
Cell Line ◽  
Cell Lines ◽  
Synthetic Lethality ◽  
Parp Inhibitor ◽  
Lethal Dose ◽  
Myeloma Cell ◽  
Chemotherapeutic Agents ◽  
Molecular Heterogeneity ◽  
Rpmi 8226

Abstract One hallmark of multiple myeloma is its genetic instability, leading to extensive molecular heterogeneity. This has led to the hypothesis that a high level of DNA repair is needed to counterbalance the continual genotoxic stress seen in these cells. One important DNA repair pathway involves PARP (poly-ADP ribose polymerase 1 and 2). With the goal of developing improved therapies against myeloma, we examined for potential synergy between the PARP inhibitor veliparib and agents currently used to treat myeloma. In these pre-clinical studies, various myeloma cell lines including OPM2.2 and RPMI 8226 are being tested. Cells in triplicate are exposed to myeloma therapeutics (e.g., bortezomib, doxorubicin, cyclophosphamide) in the presence and absence of a sub-lethal dose of veliparib. Cells are incubated for 48 h and viability then assayed by luminescence using CellTiter-Glo (Promega). Dependent on the cell line, we found that veliparib can be synthetically lethal with other agents. For example, testing OPM2.2 cells, we found that 50 µM veliparib caused a ~7-fold decrease in the bortezomib LC50 from 7.1 nM (bortezomib alone) to 1.0 nM (bortezomib and veliparib; see Figure). We note that the concentration of veliparib employed was significantly below the LC50 of veliparib (410 µM) for these same OPM2.2 cells. In contrast, RPMI 8226 cells did not show a significant synergy between bortezomib and veliparib, even though the LC50 of each agent alone was similar to that found for OPM2.2 cells. We are currently examining the synergy between veliparib and other chemotherapeutic agents and additional myeloma cell lines. These studies will determine the generality of a potential synthetic lethality between these agents, and reveal whether use of a PARP inhibitor has the potential to provide improved treatment options against myeloma. Disclosures No relevant conflicts of interest to declare.

scholarly journals Abnormal behavior of protein kinase C in the human myeloma cell line, RPMI 8226

FEBS Letters ◽  
1990 ◽  
Vol 269 (2) ◽  
pp. 331-335 ◽  
Author(s):  
Marc R. Parant ◽  
Bernard Klein ◽  
Henri Vial
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Cell Line ◽  
Myeloma Cell ◽  
Abnormal Behavior ◽  
Myeloma Cell Line ◽  
Kinase C ◽  
Human Myeloma Cell Line ◽  
Rpmi 8226 ◽  
Human Myeloma Cell

Cell cycle arrest and DNA damage after melphalan treatment of the human myeloma cell line RPMI 8226

2009 ◽  
Vol 47 (3) ◽  
pp. 161-167 ◽  
Author(s):  
Jan-Olof Fernberg ◽  
Rolf Lewensohn ◽  
Sven Skog
Keyword(s):  
Cell Cycle ◽  
Dna Damage ◽  
Cell Cycle Arrest ◽  
Cell Line ◽  
Myeloma Cell ◽  
Myeloma Cell Line ◽  
Cycle Arrest ◽  
Human Myeloma Cell Line ◽  
Rpmi 8226 ◽  
Human Myeloma Cell
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