IFN-γ Upregulates Anti-Apoptotic Gene Expression and Inhibits Apoptosis in IL-3-Dependent Hematopoietic Cells

Sekiya, Masuo; Adachi, Masaaki; Takayama, Shinichi; Reed, John C.; Imai, Kohzoh

doi:10.1006/bbrc.1997.7478

Cited by 20 publications

(9 citation statements)

References 21 publications

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“…Therefore, consistent with what has been seen for BAG-1, BAG-3 inhibits IL-3 withdrawal-induced apoptosis. However, the antiapoptotic effects of BAG-3 appear to be considerably weaker than those reported for BAG-1 in the Ba/F3 and BAF-B03 cell lines (17,18). In summary, our data show that, like BAG-1, other members of the BAG protein family, namely BAG-3 and BAG-4/SODD, are able to bind to the Bcl-2 oncoprotein.…”

Section: Sequence and Structural Comparisons Of The Bag-3 And Bag-4/scontrasting

confidence: 55%

“…The ability of BAG-3 and BAG-4/SODD to bind to Bcl-2 led us to ask whether these proteins also may influence cellular susceptibility to apoptosis. BAG-1 protein has been shown to strongly inhibit apoptosis induced by IL-3 withdrawal in murine Ba/F3 and BAF-B03 hematopoietic progenitor cells (17,18). In Fig.…”

Section: Sequence and Structural Comparisons Of The Bag-3 And Bag-4/smentioning

confidence: 87%

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Isolation of Bcl-2 Binding Proteins That Exhibit Homology with BAG-1 and Suppressor of Death Domains Protein

Antoku

Maser

Scully

et al. 2001

Biochemical and Biophysical Research Communications

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Section: Sequence and Structural Comparisons Of The Bag-3 And Bag-4/scontrasting

confidence: 55%

Section: Sequence and Structural Comparisons Of The Bag-3 And Bag-4/smentioning

confidence: 87%

Isolation of Bcl-2 Binding Proteins That Exhibit Homology with BAG-1 and Suppressor of Death Domains Protein

Antoku

Maser

Scully

et al. 2001

Biochemical and Biophysical Research Communications

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“…Our hypothesis is that the changes in myeloma cell-derived MVs in the early stage of SD may reflect the adapted phenotype of the myeloma cells, which could be targeted by therapy. Because the proapoptotic effect of long hours of SD was obvious for RPMI 8226 cells [16] , 24 h was chosen as the time point for MV collection. Dead cells were kept below 5% for both groups, which ensured that SD MVs were predominantly caused by stimulation and not cell death.…”

Section: Resultsmentioning

confidence: 99%

Serum deprivation elevates the levels of microvesicles with different size distributions and selectively enriched proteins in human myeloma cells in vitro

et al. 2013

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Aim: To investigate the effects of serum deprivation (SD) on microvesicles (MVs) secreted from human myeloma cells and the implications for disease progression. Methods: RPMI 8226, U266, and KM3 human myeloma cells were incubated in medium containing 10% (non-SD) or 1% fetal bovine serum (SD) and MVs were isolated. The levels and size distribution of MVs were analyzed with flow cytometry. The protein profiles of MVs were studied using 2D SDS-PAGE, MALDI-TOF-MS, and Western blotting. NF-κB activation was analyzed using EMSA. Angiogenesis was examined in Eahy926 endothelial cells. Results: Exposure of RPMI 8226 cells to SD for 24 h did not alter the number of apoptotic cells. However, SD increased the number of MVs from RPMI 8226, U266, and KM3 cells to 2.5-, 4.3-, and 3.8-fold, respectively. The size distribution of SD MVs was also significantly different from that of non-SD MVs. Three proteins ZNF224, SARM, and COBL in SD MVs were found to be up-regulated, which were involved in cell cycle regulation, signal transduction and metabolism, respectively. Co-culture of SD MVs and RPMI 8226 cells increased NF-κB activation in the target RPMI 8226 cells. Furthermore, SD MVs from RPMI 8226 cells significantly increased the microtubule formation capacity of Eahy926 endothelial cells compared with non-SD MVs. Conclusion: SD elevates the levels of microvesicles with different size distribution and selectively enriched proteins in human myeloma cells in vitro. The selectively enriched proteins, especially ZNF224, may play key roles in regulation of myeloma cells, allowing better adaptation to SD.

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“…The prototype and bestcharacterized member of the BAG protein family is BAG-1. BAG-1 inhibits the chaperone activity of the Hsp/Hsc70 system (4,38,40) and, when overexpressed, confers enhanced resistance to apoptosis (9,37,41). The latter effect may depend on the capacity of BAG-1 to bind to the Hsp/Hsc70 system and/or to the antiapoptotic protein Bcl-2 (41).…”

mentioning

confidence: 99%

Apparently Normal Tumor Necrosis Factor Receptor 1 Signaling in the Absence of the Silencer of Death Domains

Endres

Häcker

Brosch

et al. 2003

Molecular and Cellular Biology

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The silencer of death domains (SODD) has been proposed to prevent constitutive signaling of tumor necrosis factor receptor 1 (TNFR1) in the absence of ligand. Besides TNFR1, death receptor 3 (DR3), Hsp70/Hsc70, and Bcl-2 have been characterized as binding partners of SODD. In order to investigate the in vivo role of SODD, we generated mice congenitally deficient in expression of the sodd gene. No spontaneous inflammatory infiltrations were observed in any organ of these mice. Consistent with this finding, in the absence of SODD no alteration in the activation patterns of nuclear factor B (NF-B), stress kinases, or ERK1 or -2 was observed after stimulation with tumor necrosis factor (TNF). Activation of NF-B by DR3 was also unchanged. The extents of DR3-and TNF-induced apoptosis were comparable in gene-deficient and wild-type cells. Protection of cells against heat shock as mediated by the Hsp70 system and against staurosporine-induced apoptosis was independent of SODD. Furthermore, resistance to high-dose lipopolysaccharide (LPS) injections, LPS-D-GalN injections, and infection with listeriae was similar in wild-type and gene-deficient mice. In conclusion, our data do not support the concept of a unique, nonredundant role of SODD for the functions of TNFR1, Hsp70, and DR3.In a yeast-two-hybrid screen, the silencer of death domains (SODD) was isolated as the binding partner of death receptor 3 (DR3), a member of the tumor necrosis factor receptor (TNFR) family which has been described as playing a role in negative selection during thymocyte development (20, 47). The cytoplasmic death domain of DR3 was identified as the domain interacting with SODD. The death domain of DR3 shares a high degree of homology with its counterpart in TNFR1, and not surprisingly, SODD was also found to bind to the death domain of TNFR1, although it did not bind to the death domains of other death receptor family members such as Fas, DR4, and DR5. Likewise, SODD was unable to interact with TNFR2 (20). SODD is a 457-amino-acid (aa) cytosolic protein that lacks death domains. Overexpression of SODD and RNA antisense experiments suggested a role for SODD in preventing ligand-independent TNFR1 signaling (20). According to the proposed model, SODD associates with TNFR1 in the absence of tumor necrosis factor (TNF) and thereby keeps the receptor molecules in a conformation that inhibits spontaneous signaling. In the presence of TNF, SODD dissociates, and the receptor-triggered signaling cascades can be initiated by binding of TRADD and other downstream signaling proteins, leading to activation of NF-B and stress kinases or to apoptosis. In vivo, uncontrolled signaling of TNFR1 can lead to hyperinflammation or to cell death by apoptosis (23,24). Recently, it has been shown that (i) TNFR1 is present in aggregates in ATP-depleted cells, (ii) SODD is able to disassemble TNFR1 aggregates only in the presence of ATP, and (iii)

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IFN-γ Upregulates Anti-Apoptotic Gene Expression and Inhibits Apoptosis in IL-3-Dependent Hematopoietic Cells

Cited by 20 publications

References 21 publications

Isolation of Bcl-2 Binding Proteins That Exhibit Homology with BAG-1 and Suppressor of Death Domains Protein

Isolation of Bcl-2 Binding Proteins That Exhibit Homology with BAG-1 and Suppressor of Death Domains Protein

Serum deprivation elevates the levels of microvesicles with different size distributions and selectively enriched proteins in human myeloma cells in vitro

Apparently Normal Tumor Necrosis Factor Receptor 1 Signaling in the Absence of the Silencer of Death Domains

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