CD44 ligation induces caspase-independent cell death via a novel calpain/AIF pathway in human erythroleukemia cells

Artus, Cédric; Maquarre, Eliane; Moubarak, Rana S.; Delettre, Cécile; Jasmin, C; Susin, Santos A.; Robert-Lézénès, J

doi:10.1038/sj.onc.1209581

Cited by 46 publications

(48 citation statements)

References 62 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In contrast, no cytochrome c release was detected (Figure 6a and Supplementary Figure 4c). These results are consistent with the recent published data, which suggest specific independent pathways for AIF and cytochrome c release from mitochondria (Artus et al, 2006).…”

Section: Knockdown Of Junb Protein Increases C-jun Levels and The Prosupporting

confidence: 83%

Targeting c-Jun and JunB proteins as potential anticancer cell therapy

et al. 2007

View full text Add to dashboard Cite

The activating protein-1 transcription factor, in particular the Jun proteins play critical roles in the regulation of cell proliferation and tumor progression. To study the potential clinical relevance of interfering with JunB expression, we generated retroviruses expressing short hairpin RNA. Reduction of JunB levels causes increased proliferation and tumorigenicity in wild-type murine fibroblasts, whereas in c-Jun knockout cells p53-independent cell cycle arrest and apoptosis are induced. Using melanoma-derived B16-F10 cancer cells the combination of JunB knockdown and c-Jun/JNK inactivation leads to cell cycle arrest and apoptosis-inducing factor-dependent apoptosis. Furthermore, the combined treatment extends survival of mice inoculated with the tumor cells. These results indicate that in the absence of c-Jun, JunB can act as a tumor promoter and inactivation of both, c-Jun and JunB, could provide a valuable strategy for antitumor intervention.

show abstract

Section: Knockdown Of Junb Protein Increases C-jun Levels and The Prosupporting

confidence: 83%

Targeting c-Jun and JunB proteins as potential anticancer cell therapy

et al. 2007

View full text Add to dashboard Cite

show abstract

“…Chemical inhibitors of calpains, calpain knockdown or CAPN4 genetic ablation, preclude mitochondrial AIFrelease and DNA damage-induced programmed necrosis. 21 Similar findings have been demonstrated in other caspaseindependent pathological models, such as retinitis pigmentosa, 37 myeloid leukemia, 38 or ischemic neuronal injury.…”

supporting

confidence: 69%

Histone H2AX: The missing link in AIF-mediated caspase-independent programmed necrosis

Fick

Belsham²

2010

Cell Cycle

View full text Add to dashboard Cite

C aspase-independent programmed necrosis is a highly regulated cellular demise that displays morphological and biochemical necrotic hallmarks, such as an earlier permeability of the plasma membrane and lactate dehydrogenase (LDH) leakiness. This form of programmed cell death (PCD) is regulated by AIF, a FAD-dependent oxidoreductase, which is released from the mitochondria to the nucleus where it induces chromatin tcondensation and DNA fragmentation. Some years ago, it was established that the sequential activation of poly(ADP-ribose) polymerase-1 (PARP-1), calpains and Bax regulates the mitochondrial AIF release associated to programmed necrosis. But, what happens when AIF is in the nucleus? How does this protein induce chromatinolysis and programmed necrosis? Recently, we have unraveled some of the mechanisms underlying the nuclear action of AIF in this type of caspase-independent cell death. Indeed, AIF plays a key role in programmed necrosis by its ability to organize a DNA-degrading complex with H2AX and Cyclophiline A (CypA). The AIF/H2AX link is indeed a critical event and explains the nuclear AIF apoptogenic action. In the present article, we outline the current knowledge on cell death by programmed necrosis and discuss the relevance of the AIF/H2AX/CypA DNAdegrading complex in the regulation of this original form of cell death.

show abstract

“…Caspase-independent death has been previously described in an erythroleukemia cell line following treatment with an anti-CD44 mAb (49). In this case, death was linked to release of apoptosisinducing factor and activation of calpain.…”

Section: Discussionmentioning

confidence: 95%

Hyaluronan Induces Cell Death in Activated T Cells through CD44

Ruffell

Johnson

2008

The Journal of Immunology

View full text Add to dashboard Cite

In the immune system, leukocyte activation induces CD44 to bind hyaluronan, a component of the extracellular matrix. Here we used gain and loss of hyaluronan-binding mutants of CD44 to examine the consequence of hyaluronan binding in T cells. Jurkat T cells transfected with CD44 mutated at S180, which prevented the addition of chondroitin sulfate, displayed constitutively high levels of hyaluronan binding. These cells were more susceptible to activation-induced cell death, whereas cells expressing a CD44 mutant unable to bind hyaluronan (R41A) were resistant to cell death. In TCR or PMA activated Jurkat T cells, hyaluronan induced rapid cell death. This depended on the level of hyaluronan binding by the cell, and the amount and size of hyaluronan. High molecular mass hyaluronan had the greatest effect and cell death occurred independently of Fas and caspase activation. In splenic T cells, high hyaluronan binding occurred in a subpopulation of cells undergoing activation-induced cell death. In addition, hyaluronan induced cell death in ∼10% of reactivated splenic T cells when Fas-dependent apoptosis was prevented by Ab blocking or in Fas negative MRL/lpr T cells. This demonstrates that hyaluronan can induce cell death in activated, high hyaluronan binding T cells via a Fas-independent mechanism.

show abstract

CD44 ligation induces caspase-independent cell death via a novel calpain/AIF pathway in human erythroleukemia cells

Cited by 46 publications

References 62 publications

Targeting c-Jun and JunB proteins as potential anticancer cell therapy

Targeting c-Jun and JunB proteins as potential anticancer cell therapy

Histone H2AX: The missing link in AIF-mediated caspase-independent programmed necrosis

Hyaluronan Induces Cell Death in Activated T Cells through CD44

Contact Info

Product

Resources

About