CMP-N-acetylneuraminic acid hydroxylase activity determines the wheat germ agglutinin-binding phenotype in two mutants of the lymphoma cell line MDAY-D2

1991 ◽  
Vol 8 (5) ◽  
pp. 434-441 ◽  
Author(s):  
Lee Shaw ◽  
Shida Yousefi ◽  
James W. Dennis ◽  
Roland Schauer
Keyword(s):  
Cell Line ◽  
Wheat Germ Agglutinin ◽  
Wheat Germ ◽  
Lymphoma Cell ◽  
Lymphoma Cell Line ◽  
Hydroxylase Activity ◽  
Acetylneuraminic Acid

Murine leukemia provirus-mediated activation of theNotch1gene leads to induction ofHES-1in a mouse T lymphoma cell line, DL-3

FEBS Letters ◽  
1999 ◽  
Vol 455 (3) ◽  
pp. 276-280 ◽  
Author(s):  
Jong-Seo Lee ◽  
Akinori Ishimoto ◽  
Tasuku Honjo ◽  
Shin-ichi Yanagawa
Keyword(s):  
Cell Line ◽  
Lymphoma Cell ◽  
Lymphoma Cell Line ◽  
T Lymphoma ◽  
Murine Leukemia

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.

Induction of apoptosis in a human lymphoma cell line by hydrophobic peptide fraction separated from anchovy sauce

BioFactors ◽  
2004 ◽  
Vol 21 (1-4) ◽  
pp. 63-67 ◽  
Author(s):  
Young Gon Lee ◽  
Ki Won Lee ◽  
Ji Yeon Kim ◽  
Kyoung Heon Kim ◽  
Hyong Joo Lee
Keyword(s):  
Cell Line ◽  
Lymphoma Cell ◽  
Lymphoma Cell Line ◽  
Peptide Fraction ◽  
Hydrophobic Peptide ◽  
Human Lymphoma ◽  
Anchovy Sauce ◽  
Induction Of Apoptosis

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

scholarly journals Peripheral T-cell lymphoma cell line T8ML-1 highlights conspicuous targeting of PVRL2 by t(14;19)(q11.2;q13.3)

Haematologica ◽  
2017 ◽  
Vol 102 (9) ◽  
pp. e356-e359
Author(s):  
Stefan Ehrentraut ◽  
Stefan Nagel ◽  
Claudia Pommerenke ◽  
Wilhelm G. Dirks ◽  
Hilmar Quentmeier ◽  
...  
Keyword(s):  
T Cell ◽  
Cell Line ◽  
Cell Lymphoma ◽  
T Cell Lymphoma ◽  
Lymphoma Cell ◽  
Lymphoma Cell Line ◽  
Peripheral T Cell Lymphoma

scholarly journals Receptor-mediated gonadotropin action in the ovary. Inhibitory actions of concanavalin A and wheat-germ agglutinin on gonadotropin-stimulated cyclic AMP and progesterone responses in ovarian cells

1981 ◽  
Vol 200 (1) ◽  
pp. 153-159 ◽  
Author(s):  
S Azhar ◽  
K M Menon
Keyword(s):  
Cyclic Amp ◽  
Concanavalin A ◽  
Wheat Germ Agglutinin ◽  
Wheat Germ ◽  
Carbohydrate Chain ◽  
Inhibitory Effect ◽  
Dolichos Biflorus ◽  
Acetylneuraminic Acid ◽  
Ovarian Cells ◽  
Proline Incorporation

Pretreatment of ovarian cells with concanavalin A and wheat-germ agglutinin blocked the gonadotropin-induced cyclic AMP and progesterone responses and this effect was time- and concentration-dependent. Basal production of either cyclic AMP or progesterone, however, was not affected by treatment of cells with lectin. The effect of concanavalin A on gonadotropin-mediated cyclic AMP and progesterone responses was blocked by alpha-methyl D-mannoside and alpha-methyl d-glucoside. Similarly the inhibitory effect of wheat-germ agglutinin was reversed by N-acetyl-D-glucosamine. Pretreatment of ovarian cells with concanavalin A or wheat-germ agglutinin had no effect on protein synthesis in the ovary as monitored by [3H]proline incorporation studies. Concanavalin A and wheat-germ agglutinin did not affect steroid production in response to dibutyryl cyclic AMP and 8-bromo cyclic AMP, indicating that the inhibitory action of lectin was occurring at a step before cyclic AMP formation. Lectins specific for L-fucose, D-galactose and N-acetyl-D-galactosamine, gorse seed agglutinin, peanut agglutinin and Dolichos biflorus agglutinin respectively, did not interfere with gonadotropin-induced cyclic AMP and progesterone responses. The present studies suggest that gonadotropin receptors may be glycoprotein in nature or closely associated with glycoprotein structures with the carbohydrate chain containing N-acetyl-D-glucosamine, mannose and possibly N-acetylneuraminic acid.

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