Establishment of a novel MALT lymphoma cell line, ma-1, from a patient with t(14;18)(q32;q21)-positive Helicobacter Pylori-Independent Gastric MALT Lymphoma

2011 ◽  
Vol 50 (11) ◽  
pp. 908-921 ◽  
Author(s):  
Sung-Hsin Kuo ◽  
Wen-Hui Weng ◽  
Zi-Hua Chen ◽  
Ping-Ning Hsu ◽  
Ming-Shiang Wu ◽  
...  
2020 ◽  
Vol 59 (9) ◽  
pp. 517-524
Author(s):  
Kiyotaka Izumi ◽  
Momoko Nishikori ◽  
Hepei Yuan ◽  
Yasuyuki Otsuka ◽  
Kensuke Nakao ◽  
...  

2013 ◽  
Vol 52 (10) ◽  
pp. 986-988 ◽  
Author(s):  
Amanda Capes-Davis ◽  
Christine Alston-Roberts ◽  
Liz Kerrigan ◽  
Yvonne A. Reid ◽  
Tanya Barrett ◽  
...  

2001 ◽  
Vol 120 (5) ◽  
pp. A746-A746
Author(s):  
S KONTUREK ◽  
P KONTUREK ◽  
T STARZYNSKA ◽  
K MARLICZ ◽  
P PIERZCHALSKI ◽  
...  

2021 ◽  
Vol 32 ◽  
pp. S331
Author(s):  
Mario Sutanto ◽  
Kinley Dhinata ◽  
Audrey Hamdoyo ◽  
Felix Wijovi ◽  
Andree Kurniawan

FEBS Letters ◽  
1999 ◽  
Vol 455 (3) ◽  
pp. 276-280 ◽  
Author(s):  
Jong-Seo Lee ◽  
Akinori Ishimoto ◽  
Tasuku Honjo ◽  
Shin-ichi Yanagawa

1995 ◽  
Vol 15 (2) ◽  
pp. 1071-1078 ◽  
Author(s):  
S Davidson ◽  
P Høj ◽  
T Gabriele ◽  
R L Anderson

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.


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

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