Cytokine production by macrophages in association with phagocytosis of etoposide-treated P388 cells in vitro and in vivo

Kawagishi, Chizuru; Kurosaka, Kahori; Watanabe, Naoko; Kobayashi, Yoshiro

doi:10.1016/s0167-4889(01)00158-6

Cited by 54 publications

(60 citation statements)

References 19 publications

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“…Chemotherapy and radiotherapy are prescribed to cancer patients in the hope that dying cells will be safely scavenged by phagocytic cells, such as macrophages. However, in vitro and in vivo studies showed that phagocytosis of VP-16-treated P388 cells by macrophages was associated with the release of IL-8 and other cytokines, such as MIF and MIP-2 (Kawagishi et al, 2001). In addition, VP-16 and the chemotherapeutic agent mitomycin were also found to induce IL-8 and TNF-a production by a human epithelial carcinoma cell line (KB cells) that expressed platelet-activating factor receptor (Darst et al, 2004).…”

Section: Discussionmentioning

confidence: 99%

“…Several studies have indicated that in addition to their known cytotoxic effects, many chemotherapeutic agents, including VP-16, are also prooxidative stressors (Kagan et al, 2001) and trigger cytokine production in a variety of cell types in vitro (Kawagishi et al, 2001;Darst et al, 2004). These findings were supported by reports of significant levels of proinflammatory cytokines in patients undergoing chemotherapy for a variety of tumours (Villani et al, 2002).…”

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confidence: 96%

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Moxifloxacin enhances antiproliferative and apoptotic effects of etoposide but inhibits its proinflammatory effects in THP-1 and Jurkat cells

et al. 2006

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Etoposide (VP-16) is a topoisomerase II (topo II) inhibitor chemotherapeutic agent. Studies indicate that VP-16 enhances proinflammatory cytokines secretion from tumour cells, including IL-8, a chemokine associated with proangiogenic effects. Fluoroquinolones inhibit topo II activity in eukaryotic cells by a mechanism different from that of VP-16. The fluoroquinolone moxifloxacin (MXF) has pronounced anti-inflammatory effects in vitro and in vivo. We studied the effects of MXF and VP-16 on purified human topo II activity and further analysed their combined activity on proliferation, apoptosis and caspase-3 activity in THP-1 and Jurkat cells. Moxifloxacin alone slightly inhibited the activity of human topo II; however, in combination with VP-16 it led to a 73% reduction in enzyme activity. VP-16 inhibited cell proliferation in a time and dose-dependent manner. The addition of moxifloxacin for 72 h to low-dose VP-16 doubled its cytotoxic effect in THP-1 and Jurkat cells (1.8-and 2.6-fold decrease in cell proliferation, respectively) (Po0.004). Moxifloxacin given alone did not induce apoptosis but enhanced VP-16-induced apoptosis in THP-1 and Jurkat cells (1.8-and two-fold increase in annexin V positive cells and caspase-3 activity, respectively) (Po0.04). VP-16 induced the release of IL-8 in a time and dose-dependent manner from THP-1 cells. Moxifloxacin completely blocked the enhanced release of IL-8 induced by 0.5 and 1 mg ml À1 VP-16, and decreased IL-8 release from cells incubated for 72 h with 3 mg ml À1 VP-16 (Po0.001). VP-16 enhanced the release of IL-1b and TNF-a from THP-1 cells, whereas the addition of MXF prevented the enhanced cytokine secretion (Po0.001). We conclude that MXF significantly enhances VP-16 cytotoxicity in tumour-derived cells while preventing VP-16-induced proinflammatory cytokine release. This unique combination may have clinical benefits and cytotoxic drug 'sparing effect' and should be further studied in vivo.

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Section: Discussionmentioning

confidence: 99%

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confidence: 96%

Moxifloxacin enhances antiproliferative and apoptotic effects of etoposide but inhibits its proinflammatory effects in THP-1 and Jurkat cells

et al. 2006

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“…However, we reported previously that the expression of a proinflammatory chemokine, IL-8 or MIP-2, but not TNF-␤, was upregulated on coculturing of macrophages with apoptotic cells at the mRNA and protein levels (6 -8). In addition, we reported that injection of late apoptotic cells into the mouse peritoneal cavity caused the production of MIP-2 and infiltration of neutrophils, and that the macrophages ingesting and/or binding to apoptotic cells, which were isolated with a cell sorter, produced a similar amount of MIP-2 as in the case of coculturing of peritoneal exudate cells (PEC) 3 with apoptotic cells (9,10). Moreover, we recently showed that anti-MIP-2 and anti-CXCR2 Abs significantly suppressed the neutrophil infiltration caused by injection of apoptotic cells into the peritoneal cavity, suggesting that the neutrophil infiltration is mainly caused by MIP-2 (11).…”

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confidence: 99%

Neutrophils Accelerate Macrophage-Mediated Digestion of Apoptotic Cells In Vivo as Well as In Vitro

Iyoda

Nagata

Akashi³

et al. 2005

The Journal of Immunology

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It is generally believed that the clearance of apoptotic cells does not lead to inflammation. In contrast, we previously found that injection of apoptotic cells into the peritoneal cavity induced the expression of an inflammatory chemokine, MIP-2, and infiltration of neutrophils, and that anti-MIP-2 Abs suppressed the infiltration significantly. Because our previous study showed that whole-body x-irradiation caused neutrophil infiltration into the thymus along with T cell apoptosis, we examined the role of neutrophils in apoptotic cell clearance. Neutrophil infiltration reached a peak 12 h after irradiation with 1 Gy of x-rays. Immunohistological analysis revealed that apoptotic cells disappeared dramatically from 10.5 to 12 h after x-irradiation. As neutrophils moved from an inner area of the cortex to the periphery, apoptotic cells disappeared concomitantly. Either anti-MIP-2 or anti-CXCR2 Abs suppressed neutrophil infiltration significantly, and the suppression of neutrophil infiltration by anti-MIP-2 Abs delayed the disappearance of apoptotic cells. Moreover, macrophage-mediated digestion of apoptotic thymocytes was accelerated in vitro on coculturing with neutrophils, even if neutrophils were separated from macrophages. These results suggest that neutrophils are recruited to the thymus mainly by MIP-2 after whole-body x-irradiation and that such neutrophils may not induce inflammation but rather accelerate complete digestion of apoptotic cells by macrophages.

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“…1A), no loss of membrane intactness was seen in the trypan blue dye-exclusion assay (data not shown). 34) These results suggest that treatment with SAL accelerates incorporation of PI by living Raji cells.…”

Section: Sal Causes Ps Externalization Followed By Cellmentioning

confidence: 82%

Catfish Egg Lectin Causes Rapid Activation of Multidrug Resistance 1 P-Glycoprotein as a Lipid Translocase

Sugawara

Hosono

Ogawa

et al. 2005

Biological & Pharmaceutical Bulletin

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Apoptotic cells are characterized based on biologic and morphologic features, such as externalization of phosphatidylserine (PS), activation of caspase, fragmentation of chromosomal DNA, cell shrinkage, plasma membrane blebbing, and nuclear condensation. [1][2][3][4][5] Plasma membrane phospholipids are normally asymmetrically distributed, with phosphatidylcholine (PC) and sphingomyelin located in the outer leaflet, and PS and phosphatidylethanolamine (PE) restricted to the inner leaflet.6) It is well known that a rapid bidirectional movement of plasma membrane phospholipids between the two leaflets is catalyzed by phospholipid scramblase (PLS), aminophospholipid translocase (APTL), and ATP-binding cassette (ABC) transporter multidrug resistance (MDR) 1 P-glycoprotein (MDR1 P-gp).7-9) Treatment of cells with various apoptosis inducers causes transbilayer movement of phospholipids, resulting in the externalization of PS and PE on the cell surface. [10][11][12] Cytotoxic galactose (Gal)-binding lectins such as ricin, abrin, and misletoe lectin ultimately cause apoptosis through PS externalization and other apoptotic events. [13][14][15] On the other hand, human dimeric galectin-1 (dGal-1) induces PS externalization but not apoptosis.16) The molecular mechanisms of PS externalization induced by these lectins are still unclear and appear to be different.In our previous studies, we demonstrated that: 1) catfish (Silurus asotus) lectin (SAL) is a 32-kDa protein and consists of three tandem repeat domains of 95 amino acid residues 17); 2) SAL has potent affinity for L-rhamnose and melibiose (Gala1-6Glc) and belongs to the rhamnose-binding lectin family 18) ; 3) SAL recognizes Gal a-linked carbohydrate chains of glycoproteins as well as those of glycosphingolipids (GSLs) such as globotriaosylceramide (Gb3) (Hosono M., Sugawara S., Ogawa Y., Hikita T., Ambo A., Sasaki Y., Takayanagi M., Hakomori S., Nitta K., unpublished observation); and 4) SAL agglutinates Gb3-expressing Burkitt's lymphoma cells, such as Raji and Daudi cells. [19][20][21] In this study, we used Gb3-expressing Raji cells to investigate whether: 1) SAL causes an increase in annexin V binding as reflected by PS externalization and a decrease in cell volume; 2) SAL leads to activation of MDR1 P-gp, causing translocation of PS from inner to outer leaflets; and 3) Gb3 and MDR1 P-gp are colocalized in the GSL-enriched microdomain (GEM). MATERIALS AND METHODSMaterials SAL was isolated in sequential chromatography on a DE23 (Whatman) anion-exchange column and Dgalactose-Sepharose 6B column as described previously. 18)Antiserum against SAL was prepared in rabbits (Japanese white) with Freund's incomplete adjuvant, as described previously. 17)Cell Culture The Burkitt's lymphoma Raji cell line was obtained from the Cell Resource Center of the Biomedical Research, Institute of Development, Ageing and Cancer, Tohoku University (Sendai, Japan). Human erythroleukemia K562 cells were obtained from the Japanese Cancer Research Resources Bank (Tokyo, Japan). Doxorubicin-...

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Cytokine production by macrophages in association with phagocytosis of etoposide-treated P388 cells in vitro and in vivo

Cited by 54 publications

References 19 publications

Moxifloxacin enhances antiproliferative and apoptotic effects of etoposide but inhibits its proinflammatory effects in THP-1 and Jurkat cells

Moxifloxacin enhances antiproliferative and apoptotic effects of etoposide but inhibits its proinflammatory effects in THP-1 and Jurkat cells

Neutrophils Accelerate Macrophage-Mediated Digestion of Apoptotic Cells In Vivo as Well as In Vitro

Catfish Egg Lectin Causes Rapid Activation of Multidrug Resistance 1 P-Glycoprotein as a Lipid Translocase

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