Basiliolides, a Class of Tetracyclic C19 Dilactones from Thapsia garganica, Release Ca2+ from the Endoplasmic Reticulum and Regulate the Activity of the Transcription Factors Nuclear Factor of Activated T Cells, Nuclear Factor-κB, and Activator Protein 1 in T Lymphocytes

2006 ◽  
Vol 319 (1) ◽  
pp. 422-430 ◽  
Author(s):  
Carmen Navarrete ◽  
Rocío Sancho ◽  
Francisco J. Caballero ◽  
Federica Pollastro ◽  
Bernd L. Fiebich ◽  
...  
Keyword(s):  
T Cells ◽  
Endoplasmic Reticulum ◽  
Transcription Factors ◽  
T Lymphocytes ◽  
Nuclear Factor Κb ◽  
Nuclear Factor ◽  
Activator Protein 1 ◽  
Activated T Cells ◽  
Activator Protein ◽  
Thapsia Garganica

Activation of transcription factors activator protein-1 and nuclear factor-κB by 2,3,7,8-Tetrachlorodibenzo-p-dioxin

2000 ◽  
Vol 59 (8) ◽  
pp. 997-1005 ◽  
Author(s):  
Alvaro Puga ◽  
Sonya J Barnes ◽  
Ching-yi Chang ◽  
Huan Zhu ◽  
Kenneth P Nephew ◽  
...  
Keyword(s):  
Transcription Factors ◽  
Nuclear Factor Κb ◽  
Nuclear Factor ◽  
Activator Protein 1 ◽  
Activator Protein ◽  
Activation Of Transcription ◽  
Tetrachlorodibenzo P Dioxin

B-cell antigen receptor activates transcription factors NFAT (nuclear factor of activated T-cells) and NF-κB (nuclear factor κB) via a mechanism that involves diacylglycerol

2004 ◽  
Vol 32 (1) ◽  
pp. 113-115 ◽  
Author(s):  
P. Antony ◽  
J.B. Petro ◽  
G. Carlesso ◽  
N.P. Shinners ◽  
J. Lowe ◽  
...  
Keyword(s):  
T Cells ◽  
Transcription Factors ◽  
B Cell ◽  
Antigen Receptor ◽  
Nuclear Factor Κb ◽  
B Cell Antigen Receptor ◽  
Nuclear Factor ◽  
Activated T Cells ◽  
Cell Antigen Receptor ◽  
Cell Antigen

Engagement of the B-cell antigen receptor (BCR) induces the activation of various transcription factors, including NFAT (nuclear factor of activated T-cells) and NF-κB (nuclear factor κB), which participate in long-term biological responses such as proliferation, survival and differentiation of B-lymphocytes. We addressed the biochemical basis of this process using the DT40 chicken B-cell lymphoma. We discovered that Bruton's tyrosine kinase (BTK) and phospholipase C-γ2 (PLC-γ2) are required to activate NFAT and NF-κB, and to produce the lipid second messenger diacylglycerol in response to BCR cross-linking. Therefore the functional integrity of the BTK/PLC-γ2/diacylglycerol signalling axis is crucial for BCR-directed activation of both transcription factors NFAT and NF-κB.

scholarly journals Antisense-mediated loss of calcium homoeostasis endoplasmic reticulum protein (CHERP; ERPROT213-21) impairs Ca2+ mobilization, nuclear factor of activated T-cells (NFAT) activation and cell proliferation in Jurkat T-lymphocytes

2003 ◽  
Vol 373 (1) ◽  
pp. 133-143 ◽  
Author(s):  
Flavia A. O'ROURKE ◽  
Janice M. LaPLANTE ◽  
Maurice B. FEINSTEIN
Keyword(s):  
Cell Cycle ◽  
Cell Proliferation ◽  
T Cells ◽  
Endoplasmic Reticulum ◽  
T Lymphocytes ◽  
Nuclear Factor ◽  
Activated T Cells ◽  
Endoplasmic Reticulum Protein ◽  
Hel Cells ◽  
Er Membrane

We recently discovered a novel gene on chromosome 19p13.1 and its product, an integral endoplasmic reticulum (ER) membrane protein, termed CHERP (calcium homoeostasis endoplasmic reticulum protein). A monoclonal antibody against its C-terminal domain inhibits Ins(1,4,5)P3-induced Ca2+ release from ER membrane vesicles of many cell types, and an antisense-mediated knockdown of CHERP in human erythroleukemia (HEL) cells greatly impaired Ca2+ mobilization by thrombin. In the present paper, we explore further CHERP's function in Jurkat T-lymphocytes. Confocal laser immunofluorescence microscopy showed that CHERP was co-localized with the Ins(1,4,5)P3 receptor throughout the cytoplasmic and perinuclear region, as previously found in HEL cells. Transfection of Jurkat cells with a lacI-regulated mammalian expression vector containing CHERP antisense cDNA caused a knockdown of CHERP and impaired the rise of cytoplasmic Ca2+ (measured by fura-2 acetoxymethyl ester fluorescence) caused by phytohaemagglutinin (PHA) and thrombin. A 50% fall of CHERP decreased the PHA-induced rise of the cytoplasmic free Ca2+ concentration ([Ca2+]i), but Ca2+ influx was unaffected. Greater depletion of CHERP (>70%) did not affect the concentration of Ins(1,4,5)P3 receptors, but diminished the rise of [Ca2+]i in response to PHA to ≤30% of that in control cells, decreased Ca2+ influx and slowed the initial rate of [Ca2+]i rise caused by thapsigargin, an inhibitor of the sarcoplasmic/endoplasmic-reticulum Ca2+-ATPase, suggesting there was also some deficit in ER Ca2+ stores. In CHERP-depleted cells the Ca2+-dependent activation and translocation of the key transcription factor NFAT (nuclear factor of activated T-cells) from cytoplasm to nucleus was suppressed. Furthermore, cell proliferation was greatly slowed (as in HEL cells) along with a 60% decrease in cyclin D1, a key regulator of progression through the G1 phase of the cell cycle. These findings provide further evidence that CHERP is an important component of the ER Ca2+-mobilizing system in cells, and its loss impairs Ca2+-dependent biochemical pathways and progression through the cell cycle.

Repression of T-Cell Function by Thionamides Is Mediated by Inhibition of the Activator Protein-1/Nuclear Factor of Activated T-Cells Pathway and Is Associated with a Common Structure

2007 ◽  
Vol 72 (6) ◽  
pp. 1647-1656 ◽  
Author(s):  
Matjaz Humar ◽  
Hannah Dohrmann ◽  
Philipp Stein ◽  
Nikolaos Andriopoulos ◽  
Ulrich Goebel ◽  
...  
Keyword(s):  
T Cells ◽  
T Cell ◽  
Cell Function ◽  
Nuclear Factor ◽  
Activator Protein 1 ◽  
Activated T Cells ◽  
Activator Protein ◽  
Common Structure ◽  
T Cell Function
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