H-2 antigen expression: Loss in vitro, restoration in vivo, and correlation with cell-mediated cytotoxicity in a mouse lymphoma cell line

1978 ◽  
Vol 7 (1) ◽  
pp. 79-88 ◽  
Author(s):  
Olivera J. Finn ◽  
Miriam Lieberman ◽  
Henry S. Kaplan
Keyword(s):  
Cell Line ◽  
Antigen Expression ◽  
Lymphoma Cell ◽  
Lymphoma Cell Line ◽  
Mouse Lymphoma ◽  
Expression Loss

scholarly journals In vivo growth of a murine lymphoma cell line alters regulation of expression of HSP72.

1995 ◽  
Vol 15 (2) ◽  
pp. 1071-1078 ◽  
Author(s):  
S Davidson ◽  
P Høj ◽  
T Gabriele ◽  
R L Anderson
Keyword(s):  
Heat Shock ◽  
Cell Line ◽  
B Cell Lymphoma ◽  
Lymphoma Cell ◽  
Lymphoma Cell Line ◽  
Regulation Of Expression ◽  
Heat Shock Element ◽  
Stressed Cells

We have identified a murine B-cell lymphoma cell line, CH1, that has a much-diminished capacity to express increased levels of heat shock proteins in response to heat stress in vitro. In particular, these cells cannot synthesize the inducible 72-kDa heat shock protein (HSP72) which is normally expressed at high levels in stressed cells. We show here that CH1 fails to transcribe HSP72 mRNA after heat shock, even though the heat shock transcription factor, HSF, is activated correctly. After heat shock, HSF from CH1 is found in the nucleus and is phosphorylated, trimerized, and capable of binding the heat shock element. We propose that additional signals which CH1 cells are unable to transduce are normally required to activate hsp72 transcription in vitro. Surprisingly, we have found that when the CH1 cells are heated in situ in a mouse, they show normal expression of HSP72 mRNA and protein. Therefore, CH1 cells have a functional hsp72 gene which can be transcribed and translated when the cells are in an appropriate environment. A diffusible factor present in ascites fluid is capable of restoring normal HSP72 induction in CH1 cells. We conclude that as-yet-undefined factors are required for regulation of the hsp72 gene or, alternatively, that heat shock in vivo causes activation of hsp70 through a novel pathway which the defect in CH1 has exposed and which is distinct from that operating in vitro. This unique system offers an opportunity to study a physiologically relevant pathway of heat shock induction and to biochemically define effectors involved in the mammalian stress response.

Inhibition Effects of baicalin on Lymphoma Cell Line CA46 in Vitro and in Vivo

Blood ◽  
2008 ◽  
Vol 112 (11) ◽  
pp. 5053-5053
Author(s):  
Jian Da Hu ◽  
Yi Huang ◽  
Yingyu Chen ◽  
Tiannan Wei ◽  
Tingbo Liu ◽  
...  
Keyword(s):  
Cell Line ◽  
Biological Effects ◽  
Annexin V ◽  
Lymphoma Cell ◽  
Control Group ◽  
Dependent Manner ◽  
Lymphoma Cell Line ◽  
Proliferation Inhibition

Abstract Baicalin is a traditional Chinese medicine with multiple biological effects. Some researches showed baicalin has anti-tumor effects in solid tumor, such as prostate cancer. In order to investigate its effects on proliferation inhibition and apoptosis induction in human lymphoma cell, we treated Burkitt lymphoma cell line CA46 with baicalin in vitro and in vivo of CA46 xenograft. Baicalin remarkably inhibited the cell proliferation, with an IC50 value of 10μM. Apoptosis was remarkably induced by baicalin in a dose-dependent manner, which was detected by Annexin V FITC/PI double staining analysis, TUNEL labeling method and DNA fragmentation respectively. Furthermore, RT-PCR showed that the mRNA expressions of c-myc and bcl-2 in treated CA46 cell decreased in a time-dependent manner. Western-Blot showed that the protein expressions of c-myc, bcl-2, procaspase-3 and PARP(116KD) in baicalin treated CA46 cell were down-regulated, while the expression of PARP(85KD) increased. Based on the results in vitro, we investigated in vivo efficacy of baicalin, alone or in combination with cytotoxic drug VP16, for treatment in CA46 nude mice xenograft. Baicalin with the dosage of 40mg/kg/d and 80kg/mg/d could remarkably inhibit the growth of the tumor compared with control group. Combination of baicalin and VP16 had better anti-tumor effects. Histological examination of tumor samples showed more necrotic cells in treated groups. And obvious apoptosis could be observed by electron microscope. No adverse events were found in treated groups. From above we could conclude that baicalin could efficiently induce proliferation inhibition and apoptosis of CA46 cells in vitro and in vivo, which may be related with the down-regulation of c-myc and bcl-2 expressions, as well as the up-regulation of caspase-3 activity.

Intracellular superoxide dismutase activity defines invasiveness of the murine T-lymphoma cell line L5187Y-ML25 in vitro and in vivo

2013 ◽  
Vol 37 (1) ◽  
pp. 89-92 ◽  
Author(s):  
Maki Tanaka ◽  
Kageaki Kuribayashi ◽  
Kastuhisa Kogawa ◽  
Kiminori Nakamura ◽  
Naoki Watanabe
Keyword(s):  
Superoxide Dismutase ◽  
Cell Line ◽  
Lymphoma Cell ◽  
Superoxide Dismutase Activity ◽  
Lymphoma Cell Line ◽  
T Lymphoma

Isolation and Characterization of Apoptosis-Resistant Mutants from a Radiosensitive Mouse Lymphoma Cell Line

1998 ◽  
Vol 149 (1) ◽  
pp. 41 ◽  
Author(s):  
Hidehiko Kawai ◽  
Yukika Kitamura ◽  
Osamu Nikaido ◽  
Masaaki Tatsuka ◽  
Hiroko Hama-Inaba ◽  
...  
Keyword(s):  
Cell Line ◽  
Lymphoma Cell ◽  
Lymphoma Cell Line ◽  
Isolation And Characterization ◽  
Resistant Mutants ◽  
Mouse Lymphoma

Establishment of a Primary Effusion Lymphoma Cell Line (RM-P1) and In Vivo Growth System Using SCID Mice

2002 ◽  
Vol 76 (2) ◽  
pp. 165-172 ◽  
Author(s):  
Jun-ichi Miyagi ◽  
Masato Masuda ◽  
Nobuyuki Takasu ◽  
Akitoshi Nagasaki ◽  
Tetsuharu Shinjyo ◽  
...  
Keyword(s):  
Cell Line ◽  
Primary Effusion Lymphoma ◽  
Scid Mice ◽  
Lymphoma Cell ◽  
Lymphoma Cell Line ◽  
Primary Effusion Lymphoma Cell ◽  
Growth System ◽  
In Vivo Growth

scholarly journals The lymphocyte-specific protein LSP1 binds to F-actin and to the cytoskeleton through its COOH-terminal basic domain.

1992 ◽  
Vol 118 (6) ◽  
pp. 1443-1453 ◽  
Author(s):  
J Jongstra-Bilen ◽  
P A Janmey ◽  
J H Hartwig ◽  
S Galea ◽  
J Jongstra
Keyword(s):  
Amino Acids ◽  
Cell Line ◽  
Fusion Proteins ◽  
Specific Protein ◽  
Lymphoma Cell ◽  
Actin Binding ◽  
Lymphoma Cell Line ◽  
Basic Domain ◽  
Acidic Domain

The lymphocyte-specific phosphoprotein LSP1 associates with the cytoplasmic face of the plasma membrane and with the cytoskeleton. Mouse LSP1 protein contains 330 amino acids and contains an NH2-terminal acidic domain of approximately 177 amino acids. The COOH-terminal half of the LSP1 protein is rich in basic residues. In this paper we show that LSP1 protein which is immunoprecipitated with anti-LSP1 antibodies from NP-40-soluble lysates of the mouse B-lymphoma cell line BAL17 is associated with actin. In vitro binding experiments using recombinant LSP1 (rLSP1) protein and rabbit skeletal muscle actin show that LSP1 binds along the sides of F-actin but does not bind to G-actin. rLSP1 does not alter the initial polymerization kinetics of actin. The highly conserved COOH-terminal basic domains of mouse and human LSP1 share a significant homology with the 20-kD COOH-terminal F-actin binding fragment of caldesmon. A truncated rLSP1 protein containing the entire COOH-terminal basic domain from residue 179 to 330, but not the NH2-terminal acidic domain binds to F-actin at least as well as rLSP1. When LSP1/CAT fusion proteins are expressed in a LSP1-negative T-lymphoma cell line, only fusion proteins containing the basic COOH-terminal domain associate with the NP-40-insoluble cytoskeleton. These data show that LSP1 binds F-actin through its COOH-terminal basic domain and strongly suggest that LSP1 interacts with the cytoskeleton by direct binding to F-actin. We propose that LSP1 plays a role in mediating cytoskeleton driven responses in lymphocytes such as receptor capping, cell motility, or cell-cell interactions.

scholarly journals Calcium-Carbonate Nanocapsules Improve the Efficacy of BEZ235 in Lymphoma a Cell Line: A Promising New Technology of Drug Delivery

Blood ◽  
2015 ◽  
Vol 126 (23) ◽  
pp. 4851-4851
Author(s):  
Monica Civallero ◽  
Viviana Vergaro ◽  
Cinzia Citti ◽  
Maria Cosenza ◽  
Giuseppe Cannazza ◽  
...  
Keyword(s):  
Drug Delivery ◽  
Cell Line ◽  
Cell Lines ◽  
Free Drug ◽  
Lymphoma Cell ◽  
Intracellular Concentration ◽  
Solid Cancer ◽  
Lymphoma Cell Line ◽  
Biological Studies

Abstract Nanotechnology is a promising branch of the medical field, directed to improve diagnostic and therapeutics strategies, applying nanovectors as drug delivery systems. Efficient encapsulation of anticancer drugs in nanocolloids and microcapsules was recently developed by G. Ciccarella research group (1). Based on our collaboration with the Nantional Nanotechnology Laboratory of the University of Salento and our previous experience with target therapies, we encapsulated BEZ235, a phosphatidylinositol 3-kinase (PI3K)/Akt/mammalian target of rapamycin inhibitor (mTOR). BEZ235 efficiently blocks the dysfunctional activation of the PI3K/mTOR pathway in cellular and in vivo settings, thus inhibiting the growth and proliferation of various cancer cells, and phase I/II clinical trials were open in solid cancer. However the scarse solubility limited further development of this promising compound. In order to overcome the solubility issue BEZ235-loaded nanocapsules were generated by the stepwise adsorption of oppositely charged polyelectrolytes into biocompatible CaCO3 cores. First nanocapsules were tested for biocompatibility. The exposition of lymphoma cell lines to empty nanocapsules up to 48 hours, did not induce any cititoxicity, confirming their biocompatibility. Second, encapsulated BEZ235 was compared with free-drug to test the cytotoxicity in a T lymphoma cell line (HUT78) by MTT assay (Fig. 1). The results suggested that nanoencapsulated-BEZ235 was extremely efficient compared with free-BEZ235, reaching IC50 just after 5 hours of exposure compared with an IC65% at 48 hours with the free drug. A validated LC-MS/MS method was developed in order to quantify intracellular concentration of BEZ235 over time. Intracellular concentration of BEZ235 in the lymphoma cell line was consistent with biological results since the internalization kinetic and efficiency was increased by the coating. In order to confirm that the encapsuled-BEZ235 was still effective on cell apoptosis, we tested free BEZ and encapsulated BEZ235 at a concentration of 1µM in T cell lymphoma cell lines. Encapsulated-BEZ235 induced apoptosis evidenced by the cleavage of caspase 8, 9 and 3 at an earlier time point compared with free BEZ235 and at significantly lower concentration. We also confirmed that the encapsulated-BEZ235 maintained its effect on the target mTOR/AKT pathway: p-AKT was dephosphorylated at 5h while the free BEZ235 operates at least after 24 hours at concentrations 100 times higher, as previously demonstrated (2). Keeping in mind a future clinical application of these polymeric particles/capsules, our data can be regarded as a promising new nanotechnology-based strategy to improve the efficacy and bioavailability of old and new drugs. Functional biological studies of BEZ235-encapsulated carrier and its mechanism of internalization are already under way, and animal in vivo studies to evaluated toxicity and distribution of the nanocapsuled compound are ongoing. 1 F. Baldassare et al., Macromolecular Bioscience, Volume 12, Issue 5, pages 656-665, 2012 2 Civallero M, Cosenza M, Marcheselli L, Pozzi S, Sacchi S. Expert Opin Investig Drugs. 2012 Nov;21(11):1597-606. Disclosures No relevant conflicts of interest to declare.

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