© The Rockefeller University Press, 0022-1007/1997/4/1511/ $5.00
The Journal of Experimental Medicine, Volume 185, Number 8, April 21, 1997 1511-1516
Differential Induction of Apoptosis by Fas–Fas Ligand Interactions in Human Monocytes and Macrophages
Peter A. Kiener*,
Patricia M. Davis*,
Gary C. Starling*,
Christopher Mehlin
,
Seymour J. Klebanoff
,
Jeffrey A. Ledbetter*, and
W. Conrad Liles
From the * Immunological Diseases, Bristol-Myers Squibb Pharmaceutical Research Institute, Seattle, Washington 98121; Department of Pathobiology and the Division of Infectious Diseases, Department of Medicine, University of Washington, Seattle, Washington 98195
 |
Abstract
|
|---|
Human monocytes undergo spontaneous apoptosis upon culture in vitro; removal of serum from the media dramatically increases the rate of this process. Monocyte apoptosis can be significantly abrogated by the addition of growth factors or proinflammatory mediators. We have evaluated the role of the endogenous Fas–Fas ligand (FasL) interaction in the induction of this spontaneous apoptosis and found that a Fas–immunoglobulin (Ig) fusion protein, an antagonistic anti-Fas monoclonal antibody and a rabbit anti-FasL antibody all greatly reduced the onset of apoptosis. The results indicate that spontaneous death of monocytes is mediated via an autocrine or paracrine pathway. Treatment of the cells with growth factors or cytokines that prevented spontaneous apoptosis had no major effects on the expression of Fas or FasL. Additionally, monocyte-derived macrophages were found to express both Fas and FasL but did not undergo spontaneous apoptosis and were not sensitive to stimulation by an agonistic anti-Fas IgM. These results indicate that protective mechanisms in these cells exist at a site downstream of the receptor–ligand interaction.
Address correspondence to Peter A. Kiener, Bristol-Myers Squibb Pharmaceutical Research Institute, 3005 First Avenue, Seattle, Washington 98121.
The Fas–Fas ligand (FasL) system is recognized as a major pathway for the induction of apoptosis (programmed cell death) in cells and tissues (for reviews see references 1, 2). Fas (CD95), a type I membrane protein of 
45 kD, is a member of the TNF-receptor (TNFR) family of proteins (3). FasL is a type II membrane protein of 37 kD, belonging to the TNF and CD40 ligand family of proteins (4, 5). Fas is widely expressed in many tissue types, either constitutively or following activation of the cells (6–11). In B and T cells, Fas is expressed at low levels on the surface of resting cells and expression is enhanced after lymphocyte activation (6, 11, 19). In contrast with Fas, the expression of FasL is reported to be much more restricted and often requires cell activation (7, 12–14). Cell surface expression of FasL is very low in resting lymphocytes but can be induced on both T and B cells after activation of the cells (13, 14, 20). The interaction of FasL with Fas on a target cell stimulates an intracellular cascade of events that leads to the induction of apoptosis. Because the expression of FasL appears to be regulated more strictly, the cell surface expression of FasL by the effector cells is thought to be the triggering event in the induction of programmed cell death. The Fas–FasL system has been shown to play a critical role in the development of the T and B cell repertoire (15, 16). Additionally, it has been proposed that target cell killing by CTLs is, in part, mediated through the interaction of FasL on the activated T cell with Fas on the target cell (17–19).
Human monocytes cultured in vitro undergo spontaneous apoptosis without requiring additional external stimuli (21–23). This process can be accelerated and enhanced by the removal of serum. Even in the presence of 20% serum, the majority of monocytes will undergo apoptosis over several days (23); surviving cells differentiate into macrophages. In culture, it is possible to prevent the rapid onset of apoptosis in monocytes by treatment with inflammatory mediators such as TNF, LPS, the ligand to CD40 (CD154), and growth factors and cytokines including GM-CSF and IFN-
(21–23). Monocytes and macrophages express low but detectable levels of Fas but the role of the endogenous Fas and FasL in the spontaneous apoptosis has not been established. Recent reports have shown that monocytes in medium containing serum can rapidly undergo apoptosis following the ligation of the Fas on the surface of the cells with an agonistic mAb to Fas (mAb CH-11) (9). However, no studies have been presented on the direct role of endogenous FasL in the spontaneous apoptosis of purified monocytes. Furthermore, the regulation of expression of FasL and its role in monocyte and macrophage function has not been explored.
In this report, we show that peripheral monocytes isolated by elutriation express both Fas and FasL and that the onset of apoptosis of human peripheral monocytes in culture is prevented by the addition of a nonstimulatory antiFas mAb, an antagonistic rabbit anti-FasL Ab, or a soluble Fas–Ig fusion protein, all of which block the interaction between Fas and FasL. Therefore, monocytes are able to undergo apoptosis via an autocrine or paracrine mechanism that is dependent on the expression of both Fas and FasL but is independent of another source of FasL, such as activated T cells. In contrast, monocyte-derived macrophages cultured for 7 d in vitro developed resistance to Fas-induced apoptosis despite expressing significant levels of Fas and FasL on the cell surface.
|
Materials and Methods
|
|---|
Cells.
Peripheral monocytes were prepared from healthy donors as described previously (23) in RPMI containing 2.5 mM EDTA, 10 µg/ml polymyxin B, 100 U/ml penicillin, and 100 µg/ml streptomycin. In brief, the PBMC were separated on Ficoll and the T cells were depleted from the PBMC fraction by rosetting with SRBC. The monocytes were then separated from the remaining PBMC by centrifugal elutriation. After elutriation, the monocytes were collected from the appropriate fractions by centrifugation and then resuspended in RPMI-1640 media with additions as noted in the figure legends. The monocytes isolated by this procedure were >90% pure as measured by staining the cells to determine expression of CD14, CD16, CD19, and CD3. Staining of monocytes for FACS® analysis was performed immediately after isolation. Monocyte-derived macrophages were prepared from peripheral monocytes by culturing the cells in RPMI containing 20% FBS, penicillin (100 U/ml) and streptomycin (100 µg/ml), in Teflon beakers at 37°C for 7 d; half the media was changed after 4 d. Before analysis, dead cells were removed by centrifugation over Histopaque (Sigma Chem. Co., St. Louis, MO).
Reagents and Antibodies.
The Fas–Ig and B7–Ig fusion proteins were constructed essentially as described previously (8, 23, 24), based on published sequences of the extracellular domains (3, 25) together with the constant region of human IgG1. Modified pCDM8 vectors containing the fusion genes were transiently expressed in COS cells for 6 d. The cell supernatants were harvested, clarified by centrifugation, and the fusion proteins then purified on protein A. Soluble recombinant FasL (CD8–FasL) was expressed as a fusion protein consisting of the extracellular domain of murine CD8 fused to the entire extracellular domain of human FasL. CD8–FasL was produced by transient transfection of COS cells and purified on immobilized anti-murine CD8 as described for sCD154 (23). Human GM-CSF, IFN-, IL-4, TNF-
, and FITC-labeled annexin V were obtained from R & D Systems (Minneapolis, MN). LPS (Escherichia coli 055:B5) was from Whittaker Bioproducts (Walkersville, MD). The mouse monoclonal anti-Fas IgM and anti-Fas IgG1 were obtained from Immunotech (Westbrook, ME); rabbit anti-FasL polyclonal antibodies (C20 and N20) were obtained from Santa Cruz Labs (Santa Cruz, CA); anti-FasL mAb was from Transduction Laboratories (Lexington, KY); FITC-labeled anti-rabbit and anti-mouse antibodies were from Jackson ImmunoResearch Labs., Inc. (West Grove, PA) or Tago (Burlingame, CA). Human IgG and all other reagents were from Sigma.
Analysis of Cell Surface Antigen Expression.
After the appropriate incubations, the cells were harvested, washed once in 2% FBS– RPMI (staining media) at 4°C, resuspended in 200 µl 2% FBS– RPMI containing 1 mg/ml BSA, and 250 µg/ml human IgG for 20 min. The cells were pelleted and resuspended in PBS containing 2% FBS, before the addition of the primary antibodies (at 10 µg/ml). The cells were incubated for 30 min at 4°C, washed once with staining media, and then incubated with FITC-labeled antimurine IgG or anti-rabbit IgG (1:50 dilution) in staining media for an additional 30 min at 4°C. For single color analysis, the samples were washed twice in PBS and fixed in 2% formaldehyde. In most analyses, the cells were stained both for the uptake of propidium iodide and for specific antigen expression. For this two-color staining, the cells were not fixed; instead, after staining cells with Ab and washing them in PBS, propidium iodide (PI) (5 µg/ml) was added immediately before analysis on a FACScan® analyzer (Becton Dickinson and Co., Mountain View, CA). In the measurement of cell surface antigen expression, the gates of the analyzer were set to exclude PI-positive cells. The FACS® data are reported as mean fluorescence ratios. This represents the mean fluorescence determined using the Fas or FasL Ab divided by the mean fluorescence of the control Ab for each treatment of the monocytes.
Assay of Apoptosis and DNA Fragmentation.
Monocytes were isolated by elutriation and cultured at 1 x 106/ml in RPMI containing 500 ng/ml polymyxin B together with no further additions, or with the agents as indicated in the text. After these incubations, the cells were harvested by centrifugation and then either permeabilized with buffer containing sodium citrate (0.3%), Triton X-100 (0.01%), and PI (50 µg/ml) for FACS® analysis or assayed for cell viability by measuring the exclusion of Trypan blue. Alternatively, the binding of FITC–annexin V was used to follow the expression of phosphatidylserine on early apoptotic cells (8, 26). The staining was carried out essentially according to the manufacturer's instructions. After the appropriate incubations cells, 5 x 105/500 µl, were incubated with saturating concentrations of FITC– annexin V for 30 min at room temperature; the cells were then immediately analyzed by FACS®.
|
Results
|
|---|
Expression of Cell Surface Fas and FasL on Human Monocytes and Macrophages.
To evaluate the expression of Fas and FasL on the cell surface, monocytes were isolated by elutriation and analyzed immediately; human macrophages were derived from peripheral monocytes by culturing the cells for 7 d in Teflon culture dishes. The different cells were then analyzed, without fixation, by FACS®. The results showed that freshly isolated monocytes and cultured monocyte-derived macrophages expressed both Fas and FasL on the cell surface (Fig. 1), although the levels of both Fas and FasL were slightly lower in the macrophages (Fig. 1, C and D). In the analysis of cells from seven different donors the ratio of specific mean fluorescence of Ab to Fas relative to the control Ab was 8.4 ± 0.7 and 5.5 ± 1.7 in monocytes and macrophages, respectively. For FasL, the ratio of specific mean fluorescence to the control was 5.7 ± 0.5 and 4.7 ± 1.0 in monocytes and macrophages, respectively.
View larger version (21K):
[in this window]
[in a new window]
[Download PPT slide]
|
Figure 1 Cell surface staining of Fas and FasL on monocytes and monocyte-derived macrophages. Dotted line, control antibodies; solid line, Fas or FasL Abs as indicated. Peripheral monocytes were isolated by elutriation and then stained immediately (A and B), or cultured for 7 d in Teflon dishes (C and D) and then stained for cell surface expression of FasL (A and C, using anti-FasL polyclonal Ab, C20) and Fas (B and D, using anti-Fas, murine IgG1) as described in Material and Methods. Staining with control antibodies was carried out using mouse IgG1 or rabbit IgG as appropriate. The histograms are from a single experiment representative of seven experiments with cells from different donors.
| |
Role of Endogenous FasL in the Spontaneous Apoptosis of Human Monocytes.
In the absence of serum, freshly isolated human monocytes rapidly undergo programmed cell death (21, 22); even in the presence of serum a significant proportion of the cells die (23). Studies were undertaken to determine the role of FasL in this spontaneous death of the cells. Peripheral monocytes were isolated and then immediately placed into culture for 18 h in serum-free RPMI alone, with the soluble fusion protein Fas–Ig, or with blocking anti-Fas or anti-FasL antibodies. The spontaneous apoptosis was markedly reduced by culturing the monocytes with Fas–Ig but not by the control fusion protein B7– Ig (Fig. 2 A). An antagonistic mouse anti-Fas mAb (IgG1) also protected the cells to a similar extent, whereas control mouse IgG1 gave rise to only marginal protection. The polyclonal anti-FasL antibody (C20) was the most effective at inhibiting the spontaneous apoptosis of the peripheral monocytes; normal rabbit IgG yielded little protection (Fig. 2 A).
View larger version (18K):
[in this window]
[in a new window]
[Download PPT slide]
|
Figure 2 Effect of fusion proteins and antibodies on spontaneous apoptosis of peripheral monocytes. (A) Staining of nuclei with PI. (B) Staining of the cell surface with annexin V. Elutriated peripheral monocytes were cultured at 1 x 106/ml in polypropylene tubes in RPMI media containing 1 µg/ml polymyxin B together with no additions, 50 µg/ml Fas–Ig, 50 µg/ml B7.1–Ig, 10 µg/ml anti-Fas IgG, 10 µg/ml muIgG1, 10 µg/ml rabbit anti-FasL (C20) or 10 µg/ml rabbit IgG. For PI staining, the cells were harvested by centrifugation after 18 h at 37°C ; they were then analyzed for apoptotic nuclei with PI as described in Materials and Methods. n, the number of different donors in each treatment set. For staining with annexin V the cells were harvested after 8 h in culture, washed, and then stained for 30 min with FITC–annexin V. The bars represent the mean ± SEM of the number (n) of different donors.
| |
One of the early changes in cells undergoing apoptosis is the exposure of phosphatidyl serine on the surface of the cells, which can be detected by the ability of the phospholipid to bind annexin V (8, 26). FACS® analysis of changes in the phospholipids in the plasma membrane of the monocytes using FITC–annexin V confirmed the onset of apoptotic responses observed in Fig. 2 A. After 8 h in culture, 50–60% of the peripheral monocytes bound annexin V, whereas culture of the cells in Fas–Ig or anti-FasL reduced the number of positive staining cells to less than 20% (Fig. 2 B). These results indicate that the autocrine or paracrine interaction of Fas and FasL is largely responsible for the spontaneous induction of programmed cell death that occurs upon culture of peripheral monocytes in serum-free media.
Effect of Cytokines on Apoptosis and Fas and FasL Expression.
It has previously been shown that different cytokines, growth factors, and LPS can prevent the onset of apoptosis in human monocytes (9, 21, 22). In agreement with these earlier findings, we found that IFN-, TNF-, GM-CSF, and LPS all effectively reduced the degree of apoptosis of monocytes when added at the initiation of the cell culture (Fig. 3 A). In addition, IL-4 alone appeared to provide slight protection from apoptosis (Fig. 3 A), but, as reported previously (21, 22), it was able to abrogate most of the rescue of the cells mediated by TNF (data not shown). Over the time course of these incubations (18 h), no major changes in the level of cell surface expression of Fas or FasL (Fig. 3, B and C) were observed. However, TNF and LPS did appear to induce a small decrease in the level of expression of FasL, and IL-4 induced a small increase in the expression of FasL. These results suggest that while the Fas– FasL interaction is essential for the spontaneous induction of programmed cell death in monocytes, the effect of cytokines, growth factors, and LPS on the apoptotic process is at a site downstream of the cell surface receptors.
View larger version (37K):
[in this window]
[in a new window]
[Download PPT slide]
|
Figure 3 Effect of IFN-, IL-4, GM-CSF, TNF-, and LPS on the Fas apoptotic pathway in peripheral monocytes. (A) Apoptosis. Elutriated peripheral monocytes were cultured at 1 x 106/ml in polypropylene tubes in RPMI media containing 1 µg/ml polymyxin B together with no additions, 10 ng/ ml TNF-, 500 U/ml IL-4, 500 U/ml IFN-, 5 µg/ml LPS or 10 ng/ml GM-CSF. After 18 h at 37°C, the cells were harvested by centrifugation and analyzed for apoptotic nuclei as described in Materials and Methods. (B and C) Cell surface expression of Fas (B) and FasL (C). Elutriated peripheral monocytes were cultured at 1 x 106/ml in polypropylene tubes in RPMI media containing 1 µg/ml polymyxin B together with no additions, 500 U/ml IFN-, 10 ng/ml GM-CSF, 500 U/ml IL-4, 5 µg/ml LPS or 10 ng/ml TNF-. After 18 h, the cells were harvested and stained for cell surface expression of Fas (anti-Fas, murine IgG1) and FasL (anti-FasL, polyclonal Ab, C20) as described in Materials and Methods. Staining with control antibodies was carried out using mouse IgG1 or rabbit IgG as appropriate. The data are expressed as ratio of the mean fluorescence intensity (mfi) of Ab against the specific antigen, relative to the mfi of control Abs for each treatment. The data represent mean ± SEM of four independent experiments.
| |
Anti-Fas–induced Apoptosis in Monocytes and Monocytederived Macrophages.
Spontaneous apoptosis was evident in peripheral monocytes, even when the cells were cultured in the presence of 20% FBS (Fig. 4). As shown here (Fig. 4) and reported previously (9), monocyte apoptosis in either the absence or presence of serum significantly increased after the addition of a stimulatory anti-Fas mAb to the cells. In contrast, human monocyte-derived macrophages were completely resistant to anti-Fas (Fig. 4) or sFasL-induced (data not shown) apoptosis. Thus, despite expressing significant levels of Fas and FasL on the cell surface (see Fig. 1), monocyte-derived macrophages were resistant to both spontaneous and anti-Fas–induced apoptosis.
View larger version (29K):
[in this window]
[in a new window]
[Download PPT slide]
|
Figure 4 Induction of apoptosis in peripheral monocytes and monocyte-derived macrophages. Elutriated peripheral monocytes were cultured for 18 h alone or with 20% FBS, in the absence or presence of 200 ng/ml anti-Fas mAb (CH-11). Monocyte-derived macrophages were cultured for 7 d in RPMI containing 20% FBS and then harvested, washed once, and then resuspended in RPMI containing 20% FBS. The cells were then cultured for an additional 18 h in the presence of 200 ng/ml anti-Fas mAb. No spontaneous apoptosis of these cells was observed over the final 18 h. Cells were harvested by centrifugation and analyzed for apoptotic nuclei with PI. The bars represent the mean ± SEM of eight (monocytes) or six (macrophages) experiments with different donors.
| |
|
Discussion
|
|---|
While the function of the Fas–FasL system in the regulation of apoptosis in lymphocytes is well established (7, 11, 14), its role in other leukocytes is less well established, though recent reports suggest that here too it may play a crucial function (8, 27, 28). Fas is constitutively expressed on other phagocytes (8–10, 28) and stimulation of Fas with an agonistic mAb induces apoptosis in neutrophils and eosinophils (8, 28). Additionally, it has been shown that the neutrophils, like activated T cells, can release biologically active soluble FasL (7, 8). Furthermore, upon isolation and culture in vitro, neutrophils undergo programmed cell death (8) mediated by interactions of Fas and FasL on the cells. It has been proposed that this apoptotic response of leukocytes in vitro reflects one of the normal mechanisms for the elimination of the cells in vivo. During an inflammatory response the eosinophils or neutrophils are recruited into the tissue. Later, the subsequent resolution of the inflammation requires that the leukocytes are removed from the site and this may be mediated by apoptosis.
Monocytes undergo spontaneous apoptosis (9, 21–23). This cell death can be inhibited by treatment of the monocytes with LPS, TNF-, GM-CSF, IFN-, and sCD154 (21–23). Monocytes express Fas, but the reports vary considerably on the extent to which the cells are sensitive to apoptosis induced by the anti-Fas mAb (9, 10, 29). In addition, treatment of monocytes with inflammatory mediators such as TNF- and IL-1β partially protects the cells from anti-Fas–induced apoptosis whereas LPS pretreatment fully protects the cells (9, 21, 22). These treatments are reported not to alter the level of Fas (9). Thus, both growth and proinflammatory factors enhance the survival of monocytes. The role of FasL in the spontaneous apoptosis of monocytes has not been explored. Furthermore, the effect of inflammatory mediators and growth factors on FasL expression is not known.
In the work reported here, we show that resting monocytes constitutively express FasL on the cell surface. This expression was not readily detected in an earlier study using the fusion protein Fas–Ig to detect FasL (9) due to the lower affinity of the reagent and due to high background binding of the Ig protein to the Fc receptors. In addition, our results indicate that spontaneous apoptosis of monocytes in vitro is mediated by the interaction of Fas and FasL on the cell surface, because apoptosis could be suppressed by reagents that block the interaction of Fas and FasL. These agents included a Fas–Ig soluble fusion protein and antagonistic antibodies to Fas or FasL. Because of the inability of any of these agents to provide complete protection from death, we cannot rule out that other mechanisms may also contribute to the induction of spontaneous apoptosis.
However, it is clear that other factors beyond the expression of Fas and FasL on the cell surface also ultimately contribute to the sensitivity of monocytes to the apoptotic pathway (27–29). We found that treatment of peripheral monocytes with TNF-, IFN-, GM-CSF, or LPS, agents that protect the cells from spontaneous apoptosis, did not markedly alter the expression of either Fas or FasL. In addition, despite the expression of both Fas and FasL on the surface, monocyte-derived macrophages were able to survive 7 d in culture and were also resistant to direct stimulation of Fas with the agonistic anti-Fas mAb. This is in contrast with a report where differentiation of monocytes by adherence to plastic enhanced their sensitivity to the mAb (29). The pathways that give rise to protection of these cells are currently being explored.
The presence of FasL on the cell surface of both monocytes and macrophages suggests that the ligand may play a role, other than regulating self-apoptosis, in the effector functions of the cell. This has also recently been proposed for neutrophils that were found to both express FasL on the cell surface and also release biologically active sFasL in the cell supernatants (8). In preliminary experiments, we have found that it is possible to stimulate monocytic cells to release biologically active sFasL (data not shown). Together, these results indicate that it is very likely that FasL plays a very important role in mediating some of the physiological functions of monocytes and macrophages.
Submitted: 9 January 1997
Revised: 24 February 1997
W.C. Liles is a Pfizer Postdoctoral fellow.
|
References
|
|---|
1 Nagata S. Fas and Fas ligand: a death factor and its receptor, Adv Immunol, 1996, 57, 129–144.
2 Nagata S & Golstein P. The Fas death factor, Science (Wash DC), 1995, 267, 1449–1456.[Abstract/Free Full Text]
3 Itoh N, Yonehara S, Ishii A, Yonehara M, Mizushima SI, Sameshima M, Hase A, Seto Y & Nagata S. The polypeptide encoded by the cDNA for human cell surface antigen Fas can mediate apoptosis, Cell, 1991, 66, 233–243.[Medline]
4 Takahashi T, Tanaka M, Inazawa J, Abe T, Suda T & Nagata S. Human Fas ligand: gene structure, chromosomal location and species specificity, Int Immunol, 1994, 6, 1567–1574.[Abstract/Free Full Text]
5 Suda T & Nagata S. Purification and characterization of the Fas-ligand that induces apoptosis, J Exp Med, 1994, 179, 873–879.[Abstract/Free Full Text]
6 Miyawaki T, Uehara T, Nibu R, Tsuji T, Yachie A, Yonehara S & Taniguchi N. Differential expression of apoptosis-related Fas antigen on lymphocyte subpopulations in human peripheral blood, J Immunol, 1992, 149, 3753–3758.[Abstract]
7 Tanaka M, Suda T, Takahashi T & Nagata S. Expression of the functional soluble form of human Fas ligand in activated lymphocytes, EMBO (Eur Mol Biol Organ) J, 1995, 14, 1129–1135.[Medline]
8 Liles WC, Kiener PA, Ledbetter JA, Aruffo A & Klebanoff SJ. Differential expression of Fas (CD95) and Fas ligand on normal human phagocytes: implications for the regulation of apoptosis in neutrophils, J Exp Med, 1996, 184, 429–440.[Abstract/Free Full Text]
9 Um H-D, Orenstein JM & Wahl SM. Fas mediates apoptosis in human monocytes by a reactive oxygen intermediate dependent pathway, J Immunol, 1996, 156, 3469–3477.[Abstract]
10 Iwai K, Miyawaki T, Takizawa T, Konno A, Ohta K, Yachie A, Seki H & Taniguchi N. Differential expression of bcl-2 and susceptibility to anti-Fas–mediated cell death in peripheral blood lymphocytes, monocytes, and neutrophils, Blood, 1994, 84, 1201–1208.[Abstract/Free Full Text]
11 Schattner E & Friedman SM. Fas expression and apoptosis in human B cells, Immunol Res, 1996, 15, 246–257.[Medline]
12 Suda T, Takahashi T, Golstein P & Nagata S. Molecular cloning and expression of the Fas ligand, a novel member of the tumor necrosis factor family, Cell, 1993, 75, 1169–1178.[Medline]
13 Hahne M, Renno T, Schroeter M, Irmler M, French L, Bornand T, MacDonald HR & Tschopp J. Activated B cells express functional Fas ligand, Eur J Immunol, 1996, 26, 721–724.[Medline]
14 Suda T, Okazaki T, Naito Y, Yokota T, Arai N, Ozaki S, Nakao K & Nagata S. Expression of the Fas ligand in cells of T cell lineage, J Immunol, 1995, 154, 3806–3813.[Abstract]
15 Ramsdell F, Seaman MS, Miller RE, Tough TW, Alderson MR & Lynch DH. gld/gldmice are unable to express a functional ligand for Fas, Eur J Immunol, 1994, 24, 928–933.[Medline]
16 Takahashi T, Tanaka M, Brannan CI, Jenkins NA, Copeland NG, Suda T & Nagata S. Generalized lymphoproliferative disease in mice, caused by a point mutation in the Fas ligand, Cell, 1994, 76, 969–976.[Medline]
17 Kagi D, Vignaux F, Ledermann B, Burki K, Depraetere V, Nagata S, Hengartner H & Golstein P. Fas and perforin pathways as major mechanisms of T-cell mediated cytotoxicity, Science (Wash DC), 1994, 265, 528–530.[Abstract/Free Full Text]
18 Lowin B, Hahne M, Mattmann C & Tschopp J. Cytolytic T-cell cytotoxicity is mediated through perforin and Fas lytic pathways, Nature (Lond), 1994, 370, 650–652.[Medline]
19 Anel A, Simon AK, Auphan N, Buferne M, Boyer C, Golstein P & Schmitt-Verhulst AM. Two signaling pathways can lead to Fas ligand expression in CD8+cytotoxic T lymphocyte clones, Eur J Immunol, 1995, 25, 3381–3387.[Medline]
20 Nishimura Y, Ishii A, Kobayashi Y, Yamasaki Y & Yonehara S. Expression and function of mouse Fas antigen on immature and mature T cells, J Immunol, 1995, 154, 4395–4403.[Abstract]
21 Managan DF, Welch GR & Wahl SM. Lipopolysaccharide, tumor necrosis factor-, and IL-1β prevent programmed cell death (apoptosis) in human peripheral blood monocytes, J Immunol, 1991, 146, 1541–1546.[Abstract]
22 Managan DF & Wahl SM. Differential regulation of human monocyte programmed cell death (apoptosis) by chemotactic factors and pro-inflammatory cytokines, J Immunol, 1991, 147, 3408–3412.[Abstract]
23 Kiener PA, Moran-Davis P, Rankin BM, Wahl AF, Aruffo A & Hollenbaugh D. Stimulation of CD40 with purified soluble gp39 induces proinflammatory responses in human monocytes, J Immunol, 1995, 155, 4917–4925.[Abstract]
24 Hollenbaugh D & Aruffo A. Construction of immunoglobulin fusion proteins, Curr Prot Immunol, 1994, 2, 10–19.
25 Freeman GJ, Freedman AS, Segil JM, Lee G, Whitman JF & Nadler LM. B7, a new member of the Ig superfamily with unique expression on activated and neoplastic B cells, J Immunol, 1989, 143, 2714–2722.[Abstract]
26 Martin SJ, Reutelingsperger CPM, McGahon AJ, Rader JA, van Schie RCAA, LaFace DM & Green DR. Early redistribution of plasma membrane phosphatidylserine is a general feature of apoptosis regardless of the initiating stimulus: inhibition by overexpression of Bcl-2 and Abl, J Exp Med, 1995, 182, 1545–1556.[Abstract/Free Full Text]
27 Squier MKT, Sehnert AJ & Cohen JJ. Apoptosis in leukocytes, J Leukoc Biol, 1995, 57, 2–10.[Abstract]
28 Matsumoto K, Schleimer RP, Saito H, Likura Y & Bochner BS. Induction of apoptosis in human eosinophils by anti-Fas antibody treatment in vitro, Blood, 1995, 86, 1437–1443.[Abstract/Free Full Text]
29 Richardson BC, Lalwani ND, Johnson KJ & Marks RM. Fas ligation triggers apoptosis in macrophages but not endothelial cells, Eur J Immunol, 1994, 24, 2640–2645.[Medline]
CiteULike 
Complore 
Connotea 
Del.icio.us 
Digg 
Facebook 
Reddit 
Technorati 
Twitter What's this?
This article has been cited by other articles:
-
Roca, H., Varsos, Z. S., Sud, S., Craig, M. J., Ying, C., Pienta, K. J.
(2009). CCL2 and Interleukin-6 Promote Survival of Human CD11b+ Peripheral Blood Mononuclear Cells and Induce M2-type Macrophage Polarization. J. Biol. Chem.
284: 34342-34354
[Abstract]
[Full Text]
-
Kubota, Y., Kinoshita, K., Suetomi, K., Fujimori, A., Takahashi, S.
(2007). Mcl-1 Depletion in Apoptosis Elicited by Ionizing Radiation in Peritoneal Resident Macrophages of C3H Mice. J. Immunol.
178: 2923-2931
[Abstract]
[Full Text]
-
Ji, J., Chen, J. J-Y., Braciale, V. L., Cloyd, M. W.
(2007). Apoptosis induced in HIV-1-exposed, resting CD4+ T cells subsequent to signaling through homing receptors is Fas/Fas ligand-mediated. J. Leukoc. Biol.
81: 297-305
[Abstract]
[Full Text]
-
Yu, Q., Chow, E. M. C., Wong, H., Gu, J., Mandelboim, O., Gray-Owen, S. D., Ostrowski, M. A.
(2006). CEACAM1 (CD66a) Promotes Human Monocyte Survival via a Phosphatidylinositol 3-Kinase- and AKT-dependent Pathway. J. Biol. Chem.
281: 39179-39193
[Abstract]
[Full Text]
-
Venet, F., Pachot, A., Debard, A.-L., Bohe, J., Bienvenu, J., Lepape, A., Powell, W. S., Monneret, G.
(2006). Human CD4+CD25+ Regulatory T Lymphocytes Inhibit Lipopolysaccharide-Induced Monocyte Survival through a Fas/Fas Ligand-Dependent Mechanism. J. Immunol.
177: 6540-6547
[Abstract]
[Full Text]
-
Lemarie, A., Morzadec, C., Merino, D., Micheau, O., Fardel, O., Vernhet, L.
(2006). Arsenic Trioxide Induces Apoptosis of Human Monocytes during Macrophagic Differentiation through Nuclear Factor-{kappa}B-Related Survival Pathway Down-Regulation. J. Pharmacol. Exp. Ther.
316: 304-314
[Abstract]
[Full Text]
-
Ma, Y., Temkin, V., Liu, H., Pope, R. M.
(2005). NF-{kappa}B Protects Macrophages from Lipopolysaccharide-induced Cell Death: THE ROLE OF CASPASE 8 AND RECEPTOR-INTERACTING PROTEIN. J. Biol. Chem.
280: 41827-41834
[Abstract]
[Full Text]
-
Valerie Pasqualetto, , Florence Vasseur, , Flora Zavala, , Elke Schneider, , Sophie Ezine,
(2005). Fas receptor signaling is requisite for B cell differentiation. J. Leukoc. Biol.
78: 1106-1117
[Abstract]
[Full Text]
-
Sergejeva, S., Ivanov, S., Lotvall, J., Linden, A.
(2005). Interleukin-17 as a Recruitment and Survival Factor for Airway Macrophages in Allergic Airway Inflammation. Am. J. Respir. Cell Mol. Bio.
33: 248-253
[Abstract]
[Full Text]
-
Brown, N. J., Hutcheson, J., Bickel, E., Scatizzi, J. C., Albee, L. D., Haines, G. K. III, Eslick, J., Bradley, K., Taricone, E., Perlman, H.
(2004). Fas Death Receptor Signaling Represses Monocyte Numbers and Macrophage Activation In Vivo. J. Immunol.
173: 7584-7593
[Abstract]
[Full Text]
-
Kokkonen, T. S., Augustin, M. T., Makinen, J. M., Kokkonen, J., Karttunen, T. J.
(2004). High Endothelial Venules of the Lymph Nodes Express Fas Ligand. J. Histochem. Cytochem.
52: 693-700
[Abstract]
[Full Text]
-
Jiang, N., Pisetsky, D. S.
(2004). The Effect of Dexamethasone on the Generation of Plasma DNA from Dead and Dying Cells. Am. J. Pathol.
164: 1751-1759
[Abstract]
[Full Text]
-
Gockel, H. R., Lugering, A., Heidemann, J., Schmidt, M., Domschke, W., Kucharzik, T., Lugering, N.
(2004). Thalidomide Induces Apoptosis in Human Monocytes by Using a Cytochrome c-Dependent Pathway. J. Immunol.
172: 5103-5109
[Abstract]
[Full Text]
-
Canbay, A., Feldstein, A., Baskin-Bey, E., Bronk, S. F., Gores, G. J.
(2004). The Caspase Inhibitor IDN-6556 Attenuates Hepatic Injury and Fibrosis in the Bile Duct Ligated Mouse. J. Pharmacol. Exp. Ther.
308: 1191-1196
[Abstract]
[Full Text]
-
Liu, H., Ma, Y., Pagliari, L. J., Perlman, H., Yu, C., Lin, A., Pope, R. M.
(2004). TNF-{alpha}-Induced Apoptosis of Macrophages Following Inhibition of NF-{kappa}B: A Central Role for Disruption of Mitochondria. J. Immunol.
172: 1907-1915
[Abstract]
[Full Text]
-
Schaub, F. J., Liles, W. C., Ferri, N., Sayson, K., Seifert, R. A., Bowen-Pope, D. F.
(2003). Fas and Fas-Associated Death Domain Protein Regulate Monocyte Chemoattractant Protein-1 Expression by Human Smooth Muscle Cells Through Caspase- and Calpain-Dependent Release of Interleukin-1{alpha}. Circ. Res.
93: 515-522
[Abstract]
[Full Text]
-
Chung, C.-S., Song, G. Y., Lomas, J., Simms, H. H., Chaudry, I. H., Ayala, A.
(2003). Inhibition of Fas/Fas ligand signaling improves septic survival: differential effects on macrophage apoptotic and functional capacity. J. Leukoc. Biol.
74: 344-351
[Abstract]
[Full Text]
-
Doseff, A. I., Baker, J. H. Jr., Bourgeois, T. A., Wewers, M. D.
(2003). Interleukin-4-Induced Apoptosis Entails Caspase Activation and Suppression of Extracellular Signal-Regulated Kinase Phosphorylation. Am. J. Respir. Cell Mol. Bio.
29: 367-374
[Abstract]
[Full Text]
-
Dayyani, F., Belge, K.-U., Frankenberger, M., Mack, M., Berki, T., Ziegler-Heitbrock, L.
(2003). Mechanism of glucocorticoid-induced depletion of human CD14+CD16+ monocytes. J. Leukoc. Biol.
74: 33-39
[Abstract]
[Full Text]
-
Nhan, T. Q., Liles, W. C., Chait, A., Fallon, J. T., Schwartz, S. M.
(2003). The p17 Cleaved Form of Caspase-3 Is Present Within Viable Macrophages In Vitro and in Atherosclerotic Plaque. Arterioscler. Thromb. Vasc. Bio.
23: 1276-1282
[Abstract]
[Full Text]
-
Perez-Cruz, I., Carcamo, J. M., Golde, D. W.
(2003). Vitamin C inhibits FAS-induced apoptosis in monocytes and U937 cells. Blood
102: 336-343
[Abstract]
[Full Text]
-
Kimura, F., Suzu, S., Nakamura, Y., Nakata, Y., Yamada, M., Kuwada, N., Matsumura, T., Yamashita, T., Ikeda, T., Sato, K., Motoyoshi, K.
(2003). Cloning and Characterization of a Novel RING-B-box-Coiled-coil Protein with Apoptotic Function. J. Biol. Chem.
278: 25046-25054
[Abstract]
[Full Text]
-
Park, D. R., Thomsen, A. R., Frevert, C. W., Pham, U., Skerrett, S. J., Kiener, P. A., Liles, W. C.
(2003). Fas (CD95) Induces Proinflammatory Cytokine Responses by Human Monocytes and Monocyte-Derived Macrophages. J. Immunol.
170: 6209-6216
[Abstract]
[Full Text]
-
Mor, G., Sapi, E., Abrahams, V. M., Rutherford, T., Song, J., Hao, X.-Y., Muzaffar, S., Kohen, F.
(2003). Interaction of the Estrogen Receptors with the Fas Ligand Promoter in Human Monocytes. J. Immunol.
170: 114-122
[Abstract]
[Full Text]
-
Castaigne, J.-G., Guo, W., Leveille, C., Charron, D., Al-Daccak, R.
(2002). A CD18-dependent protein kinase C {beta}-mediated alternative cell death pathway of activated monocytes. Int Immunol
14: 1003-1014
[Abstract]
[Full Text]
-
Baker, P. K., Pettitt, A. R., Slupsky, J. R., Chen, H. J., Glenn, M. A., Zuzel, M., Cawley, J. C.
(2002). Response of hairy cells to IFN-alpha involves induction of apoptosis through autocrine TNF-alpha and protection by adhesion. Blood
100: 647-653
[Abstract]
[Full Text]
-
Terada, S., Takizawa, M., Yamamoto, S., Ezaki, O., Itakura, H., Akagawa, K. S.
(2002). Eicosapentaenoic acid inhibits CSF-induced human monocyte survival and maturation into macrophage through the stimulation of H2O2 production. J. Leukoc. Biol.
71: 981-986
[Abstract]
[Full Text]
-
Bae, Y.-S., Kim, Y., Park, J. C., Suh, P.-G., Ryu, S. H.
(2002). The synthetic chemoattractant peptide, Trp-Lys-Tyr-Met-Val-D-Met, enhances monocyte survival via PKC-dependent Akt activation. J. Leukoc. Biol.
71: 329-338
[Abstract]
[Full Text]
-
Joashi, U., Tibby, S. M., Turner, C., Mayer, A., Austin, C., Anderson, D., Durward, A., Murdoch, I. A.
(2002). Soluble Fas may be a proinflammatory marker after cardiopulmonary bypass in children. J. Thorac. Cardiovasc. Surg.
123: 137-144
[Abstract]
[Full Text]
-
Hohlbaum, A. M., Gregory, M. S., Ju, S.-T., Marshak-Rothstein, A.
(2001). Fas Ligand Engagement of Resident Peritoneal Macrophages In Vivo Induces Apoptosis and the Production of Neutrophil Chemotactic Factors. J. Immunol.
167: 6217-6224
[Abstract]
[Full Text]
-
Shoshan, Y., Shapira, I., Toubi, E., Frolkis, I., Yaron, M., Mevorach, D.
(2001). Accelerated Fas-Mediated Apoptosis of Monocytes and Maturing Macrophages from Patients with Systemic Lupus Erythematosus: Relevance to In Vitro Impairment of Interaction with iC3b-Opsonized Apoptotic Cells. J. Immunol.
167: 5963-5969
[Abstract]
[Full Text]
-
Boyle, J. J., Bowyer, D. E., Weissberg, P. L., Bennett, M. R.
(2001). Human Blood-Derived Macrophages Induce Apoptosis in Human Plaque-Derived Vascular Smooth Muscle Cells by Fas-Ligand/Fas Interactions. Arterioscler. Thromb. Vasc. Bio.
21: 1402-1407
[Abstract]
[Full Text]
-
Liles, W. C., Thomsen, A. R., O'Mahony, D. S., Klebanoff, S. J.
(2001). Stimulation of human neutrophils and monocytes by staphylococcal phenol-soluble modulin. J. Leukoc. Biol.
70: 96-102
[Abstract]
[Full Text]
-
Nwakoby, I. E., Reddy, K., Patel, P., Shah, N., Sharma, S., Bhaskaran, M., Gibbons, N., Kapasi, A. A., Singhal, P. C.
(2001). Fas-Mediated Apoptosis of Neutrophils in Sera of Patients with Infection. Infect. Immun.
69: 3343-3349
[Abstract]
[Full Text]
-
Baran, J., Weglarczyk, K., Mysiak, M., Guzik, K., Ernst, M., Flad, H.-D., Pryjma, J.
(2001). Fas (CD95)-Fas Ligand Interactions Are Responsible for Monocyte Apoptosis Occurring as a Result of Phagocytosis and Killing of Staphylococcus aureus. Infect. Immun.
69: 1287-1297
[Abstract]
[Full Text]
-
Flo, T. H., Halaas, O., Torp, S., Ryan, L., Lien, E., Dybdahl, B., Sundan, A., Espevik, T.
(2001). Differential expression of Toll-like receptor 2 in human cells. J. Leukoc. Biol.
69: 474-481
[Abstract]
[Full Text]
-
Sandri, M., Sandri, C., Brun, B., Giurisato, E., Cantini, M., Rossini, K., Destro, C., Arslan, P., Carraro, U.
(2001). Inhibition of FasL sustains phagocytic cells and delays myogenesis in regenerating muscle fibers. J. Leukoc. Biol.
69: 482-489
[Abstract]
[Full Text]
-
Hu, C.-L., Cowan, R. G., Harman, R. M., Porter, D. A., Quirk, S. M.
(2001). Apoptosis of Bovine Granulosa Cells After Serum Withdrawal Is Mediated by Fas Antigen (CD95) and Fas Ligand. Biol. Reprod.
64: 518-526
[Abstract]
[Full Text]
-
Schmidt, M., Lugering, N., Lugering, A., Pauels, H.-G., Schulze-Osthoff, K., Domschke, W., Kucharzik, T.
(2001). Role of the CD95/CD95 Ligand System in Glucocorticoid-Induced Monocyte Apoptosis. J. Immunol.
166: 1344-1351
[Abstract]
[Full Text]
-
Pagliari, L. J., Perlman, H., Liu, H., Pope, R. M.
(2000). Macrophages Require Constitutive NF-kappa B Activation To Maintain A1 Expression and Mitochondrial Homeostasis. Mol. Cell. Biol.
20: 8855-8865
[Abstract]
[Full Text]
-
Lang, D., Hubrich, A., Dohle, F., Terstesse, M., Saleh, H., Schmidt, M., Pauels, H.-G., Heidenreich, S.
(2000). Differential expression of heat shock protein 70 (hsp70) in human monocytes rendered apoptotic by IL-4 or serum deprivation. J. Leukoc. Biol.
68: 729-736
[Abstract]
[Full Text]
-
Walsh, K., Smith, R. C., Kim, H.-S.
(2000). Vascular Cell Apoptosis in Remodeling, Restenosis, and Plaque Rupture. Circ. Res.
87: 184-188
[Full Text]
-
Niinobu, T., Fukuo, K., Yasuda, O., Tsubakimoto, M., Mogi, M., Nishimaki, H., Morimoto, S., Ogihara, T.
(2000). Negative feedback regulation of activated macrophages via Fas-mediated apoptosis. Am. J. Physiol. Cell Physiol.
279: C504-C509
[Abstract]
[Full Text]
-
Fernandez-Prada, C. M., Hoover, D. L., Tall, B. D., Hartman, A. B., Kopelowitz, J., Venkatesan, M. M.
(2000). Shigella flexneri IpaH7.8 Facilitates Escape of Virulent Bacteria from the Endocytic Vacuoles of Mouse and Human Macrophages. Infect. Immun.
68: 3608-3619
[Abstract]
[Full Text]
-
Josephs, M. D., Bahjat, F. R., Fukuzuka, K., Ksontini, R., Solorzano, C. C., Edwards, C. K. III, Tannahill, C. L., MacKay, S. L. D., Copeland, E. M. III, Moldawer, L. L.
(2000). Lipopolysaccharide and D-galactosamine-induced hepatic injury is mediated by TNF-alpha and not by Fas ligand. Am. J. Physiol. Regul. Integr. Comp. Physiol.
278: R1196-R1201
[Abstract]
[Full Text]
-
Ohishi, K., Varnum-Finney, B., Flowers, D., Anasetti, C., Myerson, D., Bernstein, I. D.
(2000). Monocytes express high amounts of Notch and undergo cytokine specific apoptosis following interaction with the Notch ligand, Delta-1. Blood
95: 2847-2854
[Abstract]
[Full Text]
-
Scheuerer, B., Ernst, M., Durrbaum-Landmann, I., Fleischer, J., Grage-Griebenow, E., Brandt, E., Flad, H.-D., Petersen, F.
(2000). The CXC-chemokine platelet factor 4 promotes monocyte survival and induces monocyte differentiation into macrophages. Blood
95: 1158-1166
[Abstract]
[Full Text]
-
Walsh, K., Isner, J. M.
(2000). Apoptosis in inflammatory-fibroproliferative disorders of the vessel wall. Cardiovasc Res
45: 756-765
[Abstract]
[Full Text]
-
van den Brink, M. R. M., Moore, E., Horndasch, K. J., Crawford, J. M., Hoffman, J., Murphy, G. F., Burakoff, S. J.
(2000). Fas-Deficient lpr Mice Are More Susceptible to Graft-Versus-Host Disease. J. Immunol.
164: 469-480
[Abstract]
[Full Text]
-
Perlman, H., Pagliari, L. J., Georganas, C., Mano, T., Walsh, K., Pope, R. M.
(1999). Flice-Inhibitory Protein Expression during Macrophage Differentiation Confers Resistance to FAS-Mediated Apoptosis. JEM
190: 1679-1688
[Abstract]
[Full Text]
-
Cohen, S. S., Li, C., Ding, L., Cao, Y., Pardee, A. B., Shevach, E. M., Cohen, D. I.
(1999). Pronounced acute immunosuppression in vivo mediated by HIV Tat challenge. Proc. Natl. Acad. Sci. USA
96: 10842-10847
[Abstract]
[Full Text]
-
Matute-Bello, G., Liles, W. C., Steinberg, K. P., Kiener, P. A., Mongovin, S., Chi, E. Y., Jonas, M., Martin, T. R.
(1999). Soluble Fas Ligand Induces Epithelial Cell Apoptosis in Humans with Acute Lung Injury (ARDS). J. Immunol.
163: 2217-2225
[Abstract]
[Full Text]
-
Arnold, R., Seifert, M., Asadullah, K., Volk, H. D.
(1999). Crosstalk Between Keratinocytes and T Lymphocytes via Fas/Fas Ligand Interaction: Modulation by Cytokines. J. Immunol.
162: 7140-7147
[Abstract]
[Full Text]
-
Matsue, H., Edelbaum, D., Hartmann, A. C., Morita, A., Bergstresser, P. R., Yagita, H., Okumura, K., Takashima, A.
(1999). Dendritic Cells Undergo Rapid Apoptosis In Vitro During Antigen-Specific Interaction with CD4+ T Cells. J. Immunol.
162: 5287-5298
[Abstract]
[Full Text]
-
Morelli, A., Larregina, A., Smith-Arica, J, Dewey, R., Southgate, T., Ambar, B, Fontana, A, Castro, M., Lowenstein, P.
(1999). Neuronal and glial cell type-specific promoters within adenovirus recombinants restrict the expression of the apoptosis-inducing molecule Fas ligand to predetermined brain cell types, and abolish peripheral liver toxicity. J. Gen. Virol.
80: 571-583
[Abstract]
-
Pentikainen, V., Erkkila, K., Dunkel, L.
(1999). Fas regulates germ cell apoptosis in the human testis in vitro. Am. J. Physiol. Endocrinol. Metab.
276: E310-E316
[Abstract]
[Full Text]
-
Brown, S. B., Savill, J.
(1999). Phagocytosis Triggers Macrophage Release of Fas Ligand and Induces Apoptosis of Bystander Leukocytes. J. Immunol.
162: 480-485
[Abstract]
[Full Text]
-
Hamilton, J. A., Chan, J., Byrne, R. J., Bischof, R. J., Jaworowski, A., Kanagasundaram, V.
(1998). MRL/lpr and MRL+/+ Macrophage DNA Synthesis in the Absence and the Presence of Colony-Stimulating Factor-1 and Granulocyte-Macrophage Colony-Stimulating Factor. J. Immunol.
161: 6802-6811
[Abstract]
[Full Text]
-
Perera, L. P., Waldmann, T. A.
(1998). Activation of human monocytes induces differential resistance to apoptosis with rapid down regulation of caspase-8/FLICE. Proc. Natl. Acad. Sci. USA
95: 14308-14313
[Abstract]
[Full Text]
-
Smith, D., Sieg, S., Kaplan, D.
(1998). Technical Note: Aberrant Detection of Cell Surface Fas Ligand with Anti-Peptide Antibodies. J. Immunol.
160: 4159-4160
[Abstract]
[Full Text]
-
Halaas, O., Vik, R., Espevik, T.
(1998). Induction of Fas Ligand in Murine Bone Marrow NK Cells by Bacterial Polysaccharides. J. Immunol.
160: 4330-4336
[Abstract]
[Full Text]
-
Algeciras, A., Dockrell, D. H., Lynch, D. H., Paya, C. V.
(1998). CD4 Regulates Susceptibility to Fas ligand- and Tumor Necrosis Factor-mediated Apoptosis. JEM
187: 711-720
[Abstract]
[Full Text]
-
Yao, P. M., Tabas, I.
(2000). Free Cholesterol Loading of Macrophages Induces Apoptosis Involving the Fas Pathway. J. Biol. Chem.
275: 23807-23813
[Abstract]
[Full Text]
Top
Abstract
Materials and Methods
