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Department of Oncology and Immunology, Division of Surgery, John Hunter Hospital, Newcastle, New South Wales, Australia
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Abstract |
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 Top Abstract IntroductionMaterials and MethodsResultsDiscussionReferences |
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, and
CD40L. FasL also was not involved in CD4 T cell-mediated killing of
melanoma cells. In the present study, we have tested melanoma cells for
their susceptibility to apoptosis induced by human TNF-related
apoptosis-inducing ligand (TRAIL) and the ability of a mAb against
TRAIL to inhibit apoptosis and CD4 CTL-mediated killing of melanoma and
Jurkat target cells. The results show that TRAIL-induced apoptosis in
cells from 7 of 10 melanoma cell lines tested as well as in Jurkat T
cells. Susceptibility to apoptosis was increased in some of the cell
lines by treatment with cyclohexamide or actinomycin D. The melanoma
cells were resistant to apoptosis induced by FasL, TNF-, and CD40L.
mAb M180 against TRAIL inhibited apoptosis induced by TRAIL. It was
also found to inhibit CD4 CTL-mediated killing of Jurkat T cells as
well as autologous and allogeneic melanoma cells. The degree of
inhibition produced by the mAb varied between different clones of CTL
and according to the susceptibility of the target cells to
TRAIL-induced apoptosis. These results suggest that TRAIL is an
important mediator of cell death induced by CTL and may have an
important therapeutic role against human
melanoma. |
Introduction |
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TopAbstractIntroductionMaterials and MethodsResultsDiscussionReferences |
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(CD120a,b)
and Fas ligand (FasL)3
(CD95), as well as a more recently described protein referred
to as TNF-related apoptosis-inducing ligand or TRAIL (4, 5).
The latter was found to be more widely distributed in tissues than
FasL but was similar to FasL in its ability to induce apoptosis in a
number of cell lines, particularly of hemopoietic origin (4, 6, 7). At least three receptors have been described for TRAIL. R1 or death receptor 4 (DR4) was found to be expressed in most tissues, including activated T cells. It did not interact with the common adaptor molecule Fas-associated death domain (FADD), which binds to TNFR-1 and Fas (8). The second receptor, R2 (DR5), was also found to be widely distributed on tissues and, in contrast to R1, induced apoptosis by mechanisms that involved interaction with FADD (9). The third receptor, R3, differed mainly from R1 and R2 in not having a cytoplasmic domain and being linked to glycosyl phosphatidylinositol in the cell membrane. Interaction of TRAIL with R3 did not induce apoptosis (10). Expression of the latter was therefore postulated to protect cells against TRAIL-induced apoptosis (11, 12). This decoy role for R3 (or DcR1) was supported by its high expression on a variety of normal tissues but not on tumor cell lines (11). Similar findings were independently reported by a second group who referred to the receptors as TRID (13) (TRAIL receptor without an intracellular domain).
We have previously examined the role of the FasL/Fas pathway in the killing of melanoma target cells by CD4 CTL. This followed reports that the latter was the principal cytotoxic mechanism used for killing by CD4 T cells (14). Our results indicated, instead, that although the melanoma cells expressed Fas, they were resistant to killing by FasL and that mAb against FasL did not inhibit killing by the CD4 T cell clones (15). The CD4 T cells appeared to use different mechanisms against autologous and allogeneic melanoma cells. In the present study, we have investigated the susceptibility of melanoma cells to TRAIL-induced apoptosis and the role of TRAIL in the killing of melanoma and other target cells by CD4 T cells. We report that a high proportion of melanoma cells were susceptible to apoptosis induced by TRAIL and that the latter appears to mediate cytotoxic activity by CD4 T cells against Jurkat and melanoma target cells.
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Materials and Methods |
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TopAbstractIntroductionMaterials and MethodsResultsDiscussionReferences |
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The series of melanoma cells with the prefix Mel were isolated from patients attending the Newcastle and Sydney Melanoma Units. Mel-FH, Mel-RM, Mel-JS, Mel-FC, Mel-CV, and Mel-WB were isolated from lymph nodes. These cell lines had been in culture from 2 to 6 mo at the time of these studies. The MM200 cell line was kindly supplied by Drs. Pope and Parsons (Queensland Institute for Medical Research, Queensland, Australia) and were isolated from primary melanoma. ME1007, ME10538, and ME4405 were kind gifts from Dr. Parmiani (National Cancer Institute, Milan, Italy) and were established from primary melanoma. IgR3 was provided by Dr. Hope (Genetics Department, University of Adelaide, Adelaide, Australia); it was established from a primary melanoma and is described elsewhere (16). The Jurkat T cell leukemia line was obtained from Dr. Robert Gallo (National Cancer Institute, Bethesda, MD). Lymphoblastoid cell lines (LCL) were obtained by EBV transformation of blood lymphocytes by culture in supernatants from the B95-8 marmoset leukocyte line (ATCC CRL 1612). Melanoma cells and LCL were cultured in DMEM containing 5% FCS (Commonwealth Serum Laboratories, Melbourne, Victoria, Australia).
mAbs and recombinant proteins
Recombinant human TRAIL (lot 6321-19) prepared as described
elsewhere (4) and human CD40L (lot 5753-56) were supplied by
Immunex (Seattle, WA). Each preparation was supplied as a leucine
zipper fusion protein, which required no further cross-linking for
maximal activity. The mAb M3 (IgG1) (lot 5323-12.COA) against Fas (4),
which blocks Fas-mediated lysis, and mAb M180 (IgG1) against TRAIL (9)
were supplied by Immunex as purified mAb preparations. Recombinant
human FasL (huFasL), produced from isolated cDNA (GenBank accession No.
U08137) in vector pDC409 and transfected into COS cells, was kindly
supplied as sterile supernatants by Immunex. It produced 50% lysis of
Jurkat T cells at dilutions of 2 to 4 (17). rTNF- cytokines
and control mAb anti-trinitrophenyl (anti-TNP; IgG1)
were purchased from PharMingen (Bioclone, Marrickville, Australia).
Cytotoxic T cells
The generation and cytotoxic activity of the CD4 T cell clones
used in the study have been fully described elsewhere (15). In brief,
they were generated from the blood of patient FH (60-yr-old male,
HLA-2, B44, 62 DR-15, DR-51) 
2 yr after surgical removal of
metastatic melanoma in the right axillary lymph nodes. The cloned T
cells were maintained in DMEM + 10% AB serum + 25 IU IL-2 and were
restimulated every 14 days by adding mitomycin C-treated autologous
melanoma and autologous LCL (1:2), which had been previously incubated
together for 24 h and then irradiated (10,000 R). The generation
and specificity of the CD8 CTL clone CO is described elsewhere (16). It
is restricted by HLA-A1 and appears specific for melanoma.
Cytotoxic assays
The cytotoxic activity of cultured T cells was tested in triplicate or quadruplicate in 4- or 18-h 51Cr release assays. Target cells were labeled with 100 uCi of Na251Cr04 (NEN, Boston, MA) for 1.5 h at 37°C, washed three times, and resuspended in 10% FCS + 25 IU IL-2 (complete medium) at a concentration of 3 x 104/ml. A volume of 0.1 ml of target cells was added to 0.1 ml of T cells (6 x 105/ml) in a 96-well V-bottom plate (Medos, Lidcombe, Australia). The plates were centrifuged at 100 x g for 2 min and incubated in a humidified atmosphere of 5% CO2 at 37°C for 18 h. For each target system, spontaneous release as well as maximal 51Cr activity release was determined. After incubation, 100 µl of supernatant was harvested and counted in an automated gamma counter. Percent lysis was calculated as follows: % specific cytotoxicity = [experimental release (cpm) - spontaneous release (cpm)]/[maximal release (cpm) - spontaneous release (cpm)].
Inhibition of CTL activity with mAbs was performed likewise in a total volume of 200 µl. CTLs or target cells were preincubated with mAb for 30 min at 37°C at 20 µg/ml. Cultures were maintained for 18 h at 37°C in the continued presence of mAbs diluted four times. Inhibition induced by the mAb was calculated as the reduction in percent specific cytotoxicity/specific cytotoxicity x 100.
Apoptosis
Apoptotic cells were determined by the propidium iodide method
(18). In brief, melanoma cells were adhered overnight in a 24-well
plate (Falcon 3047; Becton Dickinson, Lane Cove, Australia) at a
concentration of 1 x 105/well in 10% FCS. Cells in
suspension were added on the day of the assay. Medium was removed, and
500 µl of fresh medium + 10% FCS containing the appropriate mAb was
added for 30 min at 37° before the addition of TRAIL, FasL, CD40L, or
TNF-. Cells were incubated for a further 24 h at 37°C, and
the medium removed and adherent and suspended cells washed 1 x
with PBS. The medium and PBS were placed in 12 x 75 mm Falcon
polystyrene tube and centrifuged at 200 x g. A
hypotonic buffer 1 ml (propidium iodide, 50 µg/ml, in 0.1% sodium
citrate plus 0.1% Triton X-100; Sigma, St. Louis, MO) was added
directly to the cell pellet of cells grown in suspension or to adhered
cells in the 24-well plate and gently pipetted off, then added to the
appropriate cell pellet in the Falcon tube. The tubes were placed at
4°C in the dark overnight before flow cytometric analyses. The
propidium iodide fluorescence of individual nucleic was measured in the
red fluorescene using a Facscan flow cytometer (Becton
Dickinson, Mountain View, CA) and the data registered in a logarithmic
scale. At least 104 cells of each sample were analyzed.
Apoptotic nuclei appeared as a broad hypodiploid DNA peak, which was
easily distinguished from the narrow hyperdiploid peak of nuclei in the
melanoma cells.
Cyclohexamide (10 µg/ml) and actinomycin D (3 µg/ml) were added to cells 2 h before adding apoptotic mediating reagents.
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Results |
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TopAbstractIntroductionMaterials and MethodsResultsDiscussionReferences |
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The susceptibility of melanoma cells and the Jurkat T cell line
was tested over a range of concentrations of TRAIL. As shown in Figure 1
, apoptosis of cells from two melanoma
lines was maximal at 100 ng/ml. Jurkat cells appeared more sensitive to
apoptosis induced by TRAIL than the melanoma cells. Studies on the
kinetics of induction of apoptosis by TRAIL shown in Figure 1B indicated that apoptosis was induced rapidly in Jurkat
and the Mel-RM cell line and was maximal at 6 h, whereas 18 h
was needed for maximal induction of apoptosis in the cells from the
MM200 line.
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We compared several TNF family members for their ability to induce
apoptosis in cells from the Jurkat and MM200 cell lines. As shown in
Figure 2, TNF-, FasL, and TRAIL, but
not CD40L, induced apoptosis in Jurkat cells, but only TRAIL induced
apoptosis in the MM200 melanoma cells. TRAIL was tested for its ability
to induce apoptosis in a range of melanoma cells that had previously
been shown (15) to be resistant to FasL- and TNF--induced apoptosis.
The results shown in Table I indicate
that cells from 4 of 10 melanoma lines (ME4405, MM200, Mel-CV, and
Mel-RM) were highly susceptible to TRAIL, and 3 were moderately
susceptible (Mel-WB, IgR3, and Mel-FH). Only 3 lines (ME1007, ME10538,
and Mel-JS) were resistant to apoptosis induced by TRAIL. Two each of
the three cell lines showing moderate or no sensitivity to induction of
apoptosis by TRAIL were treated with cyclohexamide or actinomycin D. As
illustrated in the table, both of the moderately sensitive lines (IgR3
and Mel-FH) had increased susceptibility to TRAIL-induced apoptosis in
the presence of actinomycin D or cyclohexamide. Cells from the
resistant line, Mel-JS, remained resistant to TRAIL-induced apoptosis,
but the ME10538 line became moderately sensitive. Similar results were
obtained in a repeat of the experiment.
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The specificity of the effects of TRAIL was examined using the mAb
M180 to inhibit TRAIL-induced apoptosis. As shown in Figure 3A, induction of apoptosis was
inhibited by the mAb at concentrations of 1 µg/ml and above. It is
noticeable that it was not possible to completely inhibit TRAIL-induced
apoptosis of melanoma cells from the MM200 line even at high
concentrations of the mAb. The data in Figure 3B also show
that the mAb at a concentration of 10 µg/ml had limited capacity to
neutralize TRAIL, and this was greater in assays against Jurkat
(
100 ng of TRAIL) than in assays against MM200 (11 ng of TRAIL).
Similar results were obtained in a repeat of the experiment.
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We have previously described the cytotoxic activity of four
CD4+ T cell clones against autologous and allogeneic
melanoma cells (15). In brief, the cytotoxic activity of clones A4C2,
C5C5, and 2C4 against autologous melanoma (Mel-FH) was mediated by
TCR-ß and were MHC class II restricted. The restricting HLA Ag was
not identified. The clone C5C4 was not MHC restricted and had different
kinetics against Mel-FH. Killing of the allogeneic melanoma Mel-RM was
not MHC restricted and was not associated with DNA fragmentation of the
nuclei.
These clones were tested for their cytotoxic activity against cells
from the autologous and two allogeneic melanoma cell lines and the
Jurkat target cell in the presence or absence of M180 mAb (5 µg/ml)
against TRAIL. As shown in Figure 4A, the killing of
Jurkat cells at 4 h by the clones C5C4, C5C5, and 2C4
was markedly inhibited (60–90%) by mAb to TRAIL, and killing by clone
A4C2 was inhibited by 37%. In contrast, mAb M3 against Fas at a
concentration of 5 µg/ml produced no (A4C2) or only low levels of
inhibition (C5C4, C5C5, and 2C4). When the assays were carried >16 h,
mAbs against TRAIL produced less inhibition of cytotoxicity and mAbs
against Fas relatively more inhibition (see Fig. 4B) of
cytotoxicity by the clones A4C2 and C5C5. This may indicate different
kinetics of expression of TRAIL and FasL on the T cells or different
kinetics of killing mediated by the ligands. We have shown previously
(15) that killing by the 2C4 clone at 16 h may be mediated by TNF,
which presumably accounts for the relatively low inhibition produced by
MAbs to TRAIL and Fas in the 16-h assay.
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show that
the CTL activity of A4C2 and C5C4 against the autologous melanoma
target cells was partially inhibited by mAb M180, whereas M3 against
Fas did not inhibit the CTL activity of any of the clones. The
cytotoxic activity of all four clones against the Mel-CV line was
partially inhibited by the mAb M180, but not by M3 mAb against Fas.
Neither mAb inhibited killing of the Mel-RM line. As shown in Table I
,
Mel-FH was only moderately sensitive to apoptosis induced by TRAIL,
whereas Mel-CV and Jurkat cells were sensitive. This may account for
the apparently greater involvement of TRAIL in killing of the Jurkat
and Mel-CV target cells by the CD4 clones. These results are
representative of two similar studies.
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, specific cytotoxicity at 16
h was 84%, and the percent inhibition produced by M180 was 15%; that
produced by the M3 mAb was 4%. Similar degrees of inhibition by the
mAbs were seen in a 4-h assay against Mel-CV. Specific cytotoxicity at
4 h was 37%, and inhibition by MAb M180 and M3 was 24 and 14%,
respectively.
We examined whether the sensitivity of the target cells to TRAIL
(shown in Table I) correlated with their susceptibility to killing by
the CD4 T cell clones. The data in Table III indicate that there was a close
correlation in that melanoma cells ME4405, Mel-CV, Mel-FH, and Mel-RM,
which were sensitive to TRAIL-induced apoptosis, were also sensitive to
lysis by the CD4 T cell clones, whereas ME1007 and JS were resistant to
killing by both TRAIL and the CD4 T cells. The exception appears to be
K562 target cells, which were susceptible to TRAIL (specific
cytotoxicity, 20% at 4 h) but were not killed by the CD4 T cells
(15).
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Discussion |
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TopAbstractIntroductionMaterials and MethodsResultsDiscussionReferences |
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, as
reported previously (15). It is not clear from the present studies why
melanoma cells should be sensitive to TRAIL but not FasL, as the
mechanisms involved in the induction of apoptosis by both ligands is
thought to be similar. Previous studies have shown that induction of
apoptosis by members of the TNF family requires aggregation of their
receptors and interaction of their death domains with signal
transduction components (3). Aggregation of TRAIL and CD40 in the
present studies was facilitated by use of TRAIL or CD40 as leucine
zipper fusion proteins. It is possible that TNF- and FasL were not
cross-linked to the same extent, which may account for their inability
to induce apoptosis in melanoma cells. However, in previous studies,
immobilization of FasL or TNF- on plastic surfaces did not increase
their ability to induce apoptosis of melanoma cells, and cross-linking
of mAb M3 against Fas did not induce apoptosis (unpublished data). The
membrane-bound rather than the soluble form of FasL was shown to be
active in induction of apoptosis of T cells (19), but in previous
studies, FasL-expressing CD4 T cells did not induce apoptosis in human
melanoma cells (15). It would therefore appear more likely that the difference in susceptibility of melanoma cells to TRAIL and FasL refects different signaling pathways for induction of apoptosis, e.g., one of the receptors (DR5 or R2) appears to engage the adaptor protein FADD (9) and thereby the protease FADD-like ICE (FLICE) (caspase 8), which is inhibited in many tissues by a protein referred to as FLICE-inhibitory protein (FLIP) (20, 21). This protein was reported as explaining the resistance of melanoma cells to FasL (21). In contrast, a second receptor for TRAIL, DR4 or R1, does not appear to mediate its effects through FADD. We hypothesize that melanoma cells may preferentially express R1, and signals from TRAIL may therefore not be inhibited by FLIP. Melanoma cells that are resistant to TRAIL may not express R1 or R2 receptors, or they may express one or both decoy receptors that do not express death domains. Our studies show that some of the melanoma cells that are resistant or partially resistant to TRAIL-induced apoptosis become susceptible after treatment with cyclohexamide or actinomycin D. It is possible these cells have a combination of R1 and R2 type receptors and that production of FLIP or similar proteins are inhibited by cyclohexamide or actinomycin D. Answering these questions is the subject of ongoing studies on the expression of different receptors for TRAIL on melanoma cells.
We have reported previously (15) that several clones of CD4 T cells did
not appear to kill melanoma target cells by FasL/Fas interactions, even
though previous reports suggested this mechanism appeared important
against other target cells (14). In view of the susceptibility of
melanoma cells to TRAIL, we examined whether TRAIL interactions might
be involved in the killing of target cells by CD4 T cells. These
studies were made possible by the availability of the M180 mAb, which
we and others (9) have shown to have the ability to partially block
TRAIL-induced apoptosis. The degree of inhibition produced by the mAbs
appeared to differ according to the target cell involved. In studies
against the Jurkat T cells, mAb M180 inhibited 80% of
TRAIL-induced apoptosis but <50% of the apoptosis induced in the
MM200 melanoma cells. These results may suggest that the receptors for
TRAIL on the two cell types have different affinities and that those on
the MM200 cells are able to compete more effectively with the mAbs for
TRAIL. If this interpretation is correct, the degree of inhibition of
CTL activity produced by mAbs against TRAIL may underestimate TRAIL
involvement in CTL activity against certain target cells such as the
MM200 melanoma cells.
Using the mAb M180 against TRAIL, we were able to show that killing of the Jurkat T cells by three of the CD4 T cell clones was mediated at 4 h almost entirely by TRAIL, with FasL contributing relatively little to the cytotoxicity. The degree of killing induced by FasL appeared to increase in assays conducted over a period of 16 h, which may indicate that TRAIL is expressed early after T cell activation and more transiently than FasL. Further studies are needed on this aspect. Killing of Jurkat T cells by one of the clones (A4C2) appeared to involve cytotoxic mechanisms other than FasL or TRAIL in that the mAb M180 against TRAIL and mAb M3 against Fas inhibited killing by <50%.
TRAIL also appeared to be involved in CD4 T cell-mediated killing of melanoma cells that were sensitive to TRAIL-induced apoptosis. This included cells from the autologous and an allogeneic melanoma cell line. In studies against the autologous melanoma, only two of the clones (A4C2 and C5C4) appeared to mediate their killing by TRAIL. Killing of the autologous melanoma by A4C2 was only partially inhibited by mAbs against TRAIL, which suggested that other cytotoxic mechanisms were involved. This is consistent with our previous studies (15) showing that killing of autologous melanoma cells by the A4C2 clone was partially calcium ion dependent, consistent with perforin granzyme cytotoxic mechanisms, whereas killing by C5C4 was calcium ion independent, consistent with killing by FasL or TRAIL. The mAb against TRAIL also produced only partial inhibition of the cytotoxic activity of the T cell clones against the allogeneic Mel-CV cells, which indicated that other cytotoxic mechanisms were also involved against this target cell.
A second allogeneic melanoma line (Mel-RM) was not killed by Fas or TRAIL. We have shown previously that the CD4 T cell-mediated killing of cells from this line was not MHC restricted and did not involve induction of apoptosis. The actual lytic mechanism remains unknown (15). It is clear from these studies that T cell clones use multiple lytic mechanisms against different target cells, consistent with findings by others (3, 22, 23). Killing of melanoma target cells by MHC class I-restricted CD8 T cells may also involve TRAIL in the early phase of killing in that cytotoxicity against melanoma cells (Mel-CV) by a HLA-A1 restricted clone (16) was partially inhibited after 4 h of culture, but to a lesser extent later in the culture. Further studies to assess the generality of these findings are required.
Further support for the involvement of TRAIL in the killing of target
cells by CD4 T cells came from our studies against a range of melanoma
target cells. These studies showed a correlation between the
susceptibility of the target cells to killing by TRAIL and by the
CD4+ T cell clones. Target cells that were resistant to
TRAIL-induced apoptosis were also resistant to killing by the CD4 T
cell clones. The exception to these findings was the absence of killing
of K562 target cells by the CD4 T cell clones even though K562 was
found to be sensitive to TRAIL-induced apoptosis (as also reported by
others (7)). These findings may indicate that T cell recognition is
needed to induce TRAIL expression and in the absence of TCR engagement
TRAIL is not expressed. These results are also consistent with the
failure to demonstrate TRAIL involvement in the killing of the
allogeneic Mel-RM melanoma cells, which did not involve ßTCR on
the CD4 T cell clones (15).
As far as we are aware this is the first study to show that TRAIL may be an important mediator of cell death induced by CD4 T cells. We have previously reported a preponderance of CD4 T cells infiltrating primary melanoma (24) and others have reported an association between infiltration by CD4 T cells and regression of primary melanoma (25). Our present results provide an attractive explanation for these findings and appear to have significance in regard to the therapeutic potential of TRAIL in treatment of patients with melanoma. If the results found here in vitro reflect similar sensitivity of melanoma cells to TRAIL in vivo, this agent may become a valuable additional treatment for control of melanoma.
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Acknowledgments |
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Footnotes |
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2 Address correspondence and reprint requests to Dr. Peter Hersey, Department of Oncology and Immunology, Division of Surgery, John Hunter Hospital, Room 443, David Maddison Clinical Sciences Building, King and Watt Streets, Newcastle, NSW 2300, Australia. E-mail address:
3 Abbreviations used in this paper: FasL, Fas ligand; CD40L, CD40 ligand; FADD, Fas-associated death domain; LCL, lymphoblastoid cell lines; FLICE, Fas-associated death domain-like ICE (caspase 8); FLIP, FLICE-inhibitory protein.
Received for publication January 27, 1998. Accepted for publication April 30, 1998.
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References |
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TopAbstractIntroductionMaterials and MethodsResultsDiscussionReferences |
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 T. J. Jang, H. J. Kang, J. R. Kim, and C. H. Yang Non-steroidal anti-inflammatory drug activated gene (NAG-1) expression is closely related to death receptor-4 and -5 induction, which may explain sulindac sulfide induced gastric cancer cell apoptosis Carcinogenesis, October 1, 2004; 25(10): 1853 - 1858. [Abstract] [Full Text] [PDF]
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M. Pennati, M. Binda, M. De Cesare, G. Pratesi, M. Folini, L. Citti, M. G. Daidone, F. Zunino, and N. Zaffaroni Ribozyme-mediated down-regulation of survivin expression sensitizes human melanoma cells to topotecan in vitro and in vivo Carcinogenesis, July 1, 2004; 25(7): 1129 - 1136. [Abstract] [Full Text] [PDF]
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 X. Y. Zhang, X. D. Zhang, J. M. Borrow, T. Nguyen, and P. Hersey Translational Control of Tumor Necrosis Factor-related Apoptosis-inducing Ligand Death Receptor Expression in Melanoma Cells J. Biol. Chem., March 12, 2004; 279(11): 10606 - 10614. [Abstract] [Full Text] [PDF]
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E. S. Schultz, B. Schuler-Thurner, V. Stroobant, L. Jenne, T. G. Berger, K. Thielemanns, P. van der Bruggen, and G. Schuler Functional Analysis of Tumor-Specific Th Cell Responses Detected in Melanoma Patients after Dendritic Cell-Based Immunotherapy J. Immunol., January 15, 2004; 172(2): 1304 - 1310. [Abstract] [Full Text] [PDF]
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A. Younes and M. E. Kadin Emerging Applications of the Tumor Necrosis Factor Family of Ligands and Receptors in Cancer Therapy J. Clin. Oncol., September 15, 2003; 21(18): 3526 - 3534. [Abstract] [Full Text] [PDF]
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S. Wang, Z. F. H. M. Boonman, H.-C. Li, Y. He, M. J. Jager, R. E. M. Toes, and J. Y. Niederkorn Role of TRAIL and IFN-{gamma} in CD4+ T Cell-Dependent Tumor Rejection in the Anterior Chamber of the Eye J. Immunol., September 15, 2003; 171(6): 2789 - 2796. [Abstract] [Full Text] [PDF]
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A. Kotelkin, E. A. Prikhod'ko, J. I. Cohen, P. L. Collins, and A. Bukreyev Respiratory Syncytial Virus Infection Sensitizes Cells to Apoptosis Mediated by Tumor Necrosis Factor-Related Apoptosis-Inducing Ligand J. Virol., September 1, 2003; 77(17): 9156 - 9172. [Abstract] [Full Text] [PDF]
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 S.-E. Lamhamedi-Cherradi, S. Zheng, R. M. Tisch, and Y. H. Chen Critical Roles of Tumor Necrosis Factor-Related Apoptosis-Inducing Ligand in Type 1 Diabetes Diabetes, September 1, 2003; 52(9): 2274 - 2278. [Abstract] [Full Text] [PDF]
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 T. J. Sayers, A. D. Brooks, C. Y. Koh, W. Ma, N. Seki, A. Raziuddin, B. R. Blazar, X. Zhang, P. J. Elliott, and W. J. Murphy The proteasome inhibitor PS-341 sensitizes neoplastic cells to TRAIL-mediated apoptosis by reducing levels of c-FLIP Blood, July 1, 2003; 102(1): 303 - 310. [Abstract] [Full Text] [PDF]
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K. Uno, T. Inukai, N. Kayagaki, K. Goi, H. Sato, A. Nemoto, K. Takahashi, K. Kagami, N. Yamaguchi, H. Yagita, et al. TNF-related apoptosis-inducing ligand (TRAIL) frequently induces apoptosis in Philadelphia chromosome-positive leukemia cells Blood, May 1, 2003; 101(9): 3658 - 3667. [Abstract] [Full Text] [PDF]
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 J.-P. Herbeuval, C. Lambert, O. Sabido, M. Cottier, P. Fournel, M. Dy, and C. Genin Macrophages From Cancer Patients: Analysis of TRAIL, TRAIL Receptors, and Colon Tumor Cell Apoptosis J Natl Cancer Inst, April 16, 2003; 95(8): 611 - 621. [Abstract] [Full Text] [PDF]
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J. A. Mahr, J. M. Boss, and L. R. Gooding The Adenovirus E3 Promoter Is Sensitive to Activation Signals in Human T Cells J. Virol., December 20, 2002; 77(2): 1112 - 1119. [Abstract] [Full Text] [PDF]
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T. S. Soderstrom, M. Poukkula, T. H. Holmstrom, K. M. Heiskanen, and J. E. Eriksson Mitogen-Activated Protein Kinase/Extracellular Signal-Regulated Kinase Signaling in Activated T Cells Abrogates TRAIL-Induced Apoptosis Upstream of the Mitochondrial Amplification Loop and Caspase-8 J. Immunol., September 15, 2002; 169(6): 2851 - 2860. [Abstract] [Full Text] [PDF]
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X. Tang, Y. J. Sun, E. Half, M. T. Kuo, and F. Sinicrope Cyclooxygenase-2 Overexpression Inhibits Death Receptor 5 Expression and Confers Resistance to Tumor Necrosis Factor-related Apoptosis-inducing Ligand-induced Apoptosis in Human Colon Cancer Cells Cancer Res., September 1, 2002; 62(17): 4903 - 4908. [Abstract] [Full Text] [PDF]
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G. Dorothee, I. Vergnon, J. Menez, H. Echchakir, D. Grunenwald, M. Kubin, S. Chouaib, and F. Mami-Chouaib Tumor-Infiltrating CD4+ T Lymphocytes Express APO2 Ligand (APO2L)/TRAIL upon Specific Stimulation with Autologous Lung Carcinoma Cells: Role of IFN-{alpha} on APO2L/TRAIL Expression and -Mediated Cytotoxicity J. Immunol., July 15, 2002; 169(2): 809 - 817. [Abstract] [Full Text] [PDF]
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M. Chawla-Sarkar, D. W. Leaman, B. S. Jacobs, and E. C. Borden IFN-{beta} Pretreatment Sensitizes Human Melanoma Cells to TRAIL/Apo2 Ligand-Induced Apoptosis J. Immunol., July 15, 2002; 169(2): 847 - 855. [Abstract] [Full Text] [PDF]
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Q. Sun, R. L. Burton, and K. G. Lucas Cytokine production and cytolytic mechanism of CD4+ cytotoxic T lymphocytes in ex vivo expanded therapeutic Epstein-Barr virus-specific T-cell cultures Blood, May 1, 2002; 99(9): 3302 - 3309. [Abstract] [Full Text] [PDF]
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C. P. Gray, P. Arosio, and P. Hersey Heavy chain ferritin activates regulatory T cells by induction of changes in dendritic cells Blood, May 1, 2002; 99(9): 3326 - 3334. [Abstract] [Full Text] [PDF]
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N. Mitsiades, C. S. Mitsiades, V. Poulaki, K. C. Anderson, and S. P. Treon Intracellular regulation of tumor necrosis factor-related apoptosis-inducing ligand-induced apoptosis in human multiple myeloma cells Blood, March 15, 2002; 99(6): 2162 - 2171. [Abstract] [Full Text] [PDF]
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G. Lu, B. M. Janjic, J. Janjic, T. L. Whiteside, W. J. Storkus, and N. L. Vujanovic Innate Direct Anticancer Effector Function of Human Immature Dendritic Cells. II. Role of TNF, Lymphotoxin-{alpha}1{beta}2, Fas Ligand, and TNF-Related Apoptosis-Inducing Ligand J. Immunol., February 15, 2002; 168(4): 1831 - 1839. [Abstract] [Full Text] [PDF]
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D. Siegmund, A. Hausser, N. Peters, P. Scheurich, and H. Wajant Tumor Necrosis Factor (TNF) and Phorbol Ester Induce TNF-related Apoptosis-inducing Ligand (TRAIL) under Critical Involvement of NF-kappa B Essential Modulator (NEMO)/IKKgamma J. Biol. Chem., November 16, 2001; 276(47): 43708 - 43712. [Abstract] [Full Text] [PDF]
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A. E. Tollefson, K. Toth, K. Doronin, M. Kuppuswamy, O. A. Doronina, D. L. Lichtenstein, T. W. Hermiston, C. A. Smith, and W. S. M. Wold Inhibition of TRAIL-Induced Apoptosis and Forced Internalization of TRAIL Receptor 1 by Adenovirus Proteins J. Virol., October 1, 2001; 75(19): 8875 - 8887. [Abstract] [Full Text] [PDF]
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X. D. Zhang, X. Y. Zhang, C. P. Gray, T. Nguyen, and P. Hersey Tumor Necrosis Factor-related Apoptosis-inducing Ligand-induced Apoptosis of Human Melanoma Is Regulated by Smac/DIABLO Release from Mitochondria Cancer Res., October 1, 2001; 61(19): 7339 - 7348. [Abstract] [Full Text] [PDF]
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K. Hallermalm, K. Seki, C. Wei, C. Castelli, L. Rivoltini, R. Kiessling, and J. Levitskaya Tumor necrosis factor-{alpha} induces coordinated changes in major histocompatibility class I presentation pathway, resulting in increased stability of class I complexes at the cell surface Blood, August 15, 2001; 98(4): 1108 - 1115. [Abstract] [Full Text] [PDF]
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C. S. Mitsiades, S. P. Treon, N. Mitsiades, Y. Shima, P. Richardson, R. Schlossman, T. Hideshima, and K. C. Anderson TRAIL/Apo2L ligand selectively induces apoptosis and overcomes drug resistance in multiple myeloma: therapeutic applications Blood, August 1, 2001; 98(3): 795 - 804. [Abstract] [Full Text] [PDF]
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M. Chawla-Sarkar, D. W. Leaman, and E. C. Borden Preferential Induction of Apoptosis by Interferon (IFN)-{beta} Compared with IFN-{{alpha}}2: Correlation with TRAIL/Apo2L Induction in Melanoma Cell Lines Clin. Cancer Res., June 1, 2001; 7(6): 1821 - 1831. [Abstract] [Full Text] [PDF]
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K. Ogawa, K. Tanaka, A. Ishii, Y. Nakamura, S. Kondo, K. Sugamura, S. Takano, M. Nakamura, and K. Nagata A Novel Serum Protein That Is Selectively Produced by Cytotoxic Lymphocytes J. Immunol., May 15, 2001; 166(10): 6404 - 6412. [Abstract] [Full Text] [PDF]
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A. V. Franco, X. D. Zhang, E. Van Berkel, J. E. Sanders, X. Y. Zhang, W. D. Thomas, T. Nguyen, and P. Hersey The Role of NF-{{kappa}}B in TNF-Related Apoptosis-Inducing Ligand (TRAIL)-Induced Apoptosis of Melanoma Cells J. Immunol., May 1, 2001; 166(9): 5337 - 5345. [Abstract] [Full Text] [PDF]
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S. Liu, Y. Yu, M. Zhang, W. Wang, and X. Cao The Involvement of TNF-{{alpha}}-Related Apoptosis-Inducing Ligand in the Enhanced Cytotoxicity of IFN-{{beta}}-Stimulated Human Dendritic Cells to Tumor Cells J. Immunol., May 1, 2001; 166(9): 5407 - 5415. [Abstract] [Full Text] [PDF]
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C. Schmaltz, O. Alpdogan, K. J. Horndasch, S. J. Muriglan, B. J. Kappel, T. Teshima, J. L. M. Ferrara, S. J. Burakoff, and M. R. M. van den Brink Differential use of Fas ligand and perforin cytotoxic pathways by donor T cells in graft-versus-host disease and graft-versus-leukemia effect Blood, May 1, 2001; 97(9): 2886 - 2895. [Abstract] [Full Text] [PDF]
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G. Niu, K. H. Shain, M. Huang, R. Ravi, A. Bedi, W. S. Dalton, R. Jove, and H. Yu Overexpression of a Dominant-Negative Signal Transducer and Activator of Transcription 3 Variant in Tumor Cells Leads to Production of SolubleFactors That Induce Apoptosis and Cell Cycle Arrest Cancer Res., April 1, 2001; 61(8): 3276 - 3280. [Abstract] [Full Text]
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N. Mitsiades, V. Poulaki, C. Mitsiades, and M. Tsokos Ewing's Sarcoma Family Tumors Are Sensitive to Tumor Necrosis Factor-related Apoptosis-inducing Ligand and Express Death Receptor 4 and Death Receptor 5 Cancer Res., March 1, 2001; 61(6): 2704 - 2712. [Abstract] [Full Text]
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H. Matsuzaki, B. M. Schmied, A. Ulrich, J. Standop, M. B. Schneider, S. K. Batra, K. S. Picha, and P. M. Pour Combination of Tumor Necrosis Factor-related Apoptosis-inducing Ligand (TRAIL) and Actinomycin D Induces Apoptosis Even in TRAIL-resistant Human Pancreatic Cancer Cells Clin. Cancer Res., February 1, 2001; 7(2): 407 - 414. [Abstract] [Full Text]
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W. D. Thomas, X. D. Zhang, A. V. Franco, T. Nguyen, and P. Hersey TNF-Related Apoptosis-Inducing Ligand-Induced Apoptosis of Melanoma Is Associated with Changes in Mitochondrial Membrane Potential and Perinuclear Clustering of Mitochondria J. Immunol., November 15, 2000; 165(10): 5612 - 5620. [Abstract] [Full Text] [PDF]
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I. Petak, L. Douglas, D. M. Tillman, R. Vernes, and J. A. Houghton Pediatric Rhabdomyosarcoma Cell Lines Are Resistant to Fas-induced Apoptosis and Highly Sensitive to TRAIL-induced Apoptosis Clin. Cancer Res., October 1, 2000; 6(10): 4119 - 4127. [Abstract] [Full Text]
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X. D. Zhang, A. V. Franco, T. Nguyen, C. P. Gray, and P. Hersey Differential Localization and Regulation of Death and Decoy Receptors for TNF-Related Apoptosis-Inducing Ligand (TRAIL) in Human Melanoma Cells J. Immunol., April 15, 2000; 164(8): 3961 - 3970. [Abstract] [Full Text] [PDF]
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S. H. Lee, M. S. Shin, H. S. Kim, H. K. Lee, W. S. Park, S. Y. Kim, J. H. Lee, S. Y. Han, J. Y. Park, R. R. Oh, et al. Alterations of the DR5/TRAIL Receptor 2 Gene in Non-Small Cell Lung Cancers Cancer Res., November 1, 1999; 59(22): 5683 - 5686. [Abstract] [Full Text] [PDF]
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H. Winter, H.-M. Hu, W. J. Urba, and B. A. Fox Tumor Regression After Adoptive Transfer of Effector T Cells Is Independent of Perforin or Fas Ligand (APO-1L/CD95L) J. Immunol., October 15, 1999; 163(8): 4462 - 4472. [Abstract] [Full Text] [PDF]
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S.-i. Wakamatsu, M. Makino, C. Tei, and M. Baba Monocyte-Driven Activation-Induced Apoptotic Cell Death of Human T-Lymphotropic Virus Type I-Infected T Cells J. Immunol., October 1, 1999; 163(7): 3914 - 3919. [Abstract] [Full Text] [PDF]
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N. Kayagaki, N. Yamaguchi, M. Nakayama, K. Takeda, H. Akiba, H. Tsutsui, H. Okamura, K. Nakanishi, K. Okumura, and H. Yagita Expression and Function of TNF-Related Apoptosis-Inducing Ligand on Murine Activated NK Cells J. Immunol., August 15, 1999; 163(4): 1906 - 1913. [Abstract] [Full Text] [PDF]
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 C. Beltinger, S. Fulda, T. Kammertoens, E. Meyer, W. Uckert, and K.-M. Debatin Herpes simplex virus thymidine kinase/ganciclovir-induced apoptosis involves ligand-independent death receptor aggregation and activation of caspases PNAS, July 20, 1999; 96(15): 8699 - 8704. [Abstract] [Full Text] [PDF]
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X. D. Zhang, A. Franco, K. Myers, C. Gray, T. Nguyen, and P. Hersey Relation of TNF-related Apoptosis-inducing Ligand (TRAIL) Receptor and FLICE-inhibitory Protein Expression to TRAIL-induced Apoptosis of Melanoma Cancer Res., June 1, 1999; 59(11): 2747 - 2753. [Abstract] [Full Text] [PDF]
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N. Kayagaki, N. Yamaguchi, M. Nakayama, H. Eto, K. Okumura, and H. Yagita Type I Interferons (IFNs) Regulate Tumor Necrosis Factor-related Apoptosis-inducing Ligand (TRAIL) Expression on Human T Cells: A Novel Mechanism for the Antitumor Effects of Type I IFNs J. Exp. Med., May 3, 1999; 189(9): 1451 - 1460. [Abstract] [Full Text] [PDF]
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S. Mori, K. Murakami-Mori, S. Nakamura, A. Ashkenazi, and B. Bonavida Sensitization of AIDS-Kaposi's Sarcoma Cells to Apo-2 Ligand-Induced Apoptosis by Actinomycin D J. Immunol., May 1, 1999; 162(9): 5616 - 5623. [Abstract] [Full Text] [PDF]
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 L. L. Perry, K. Feilzer, S. Hughes, and H. D. Caldwell Clearance of Chlamydia trachomatis from the Murine Genital Mucosa Does Not Require Perforin-Mediated Cytolysis or Fas-Mediated Apoptosis Infect. Immun., March 1, 1999; 67(3): 1379 - 1385. [Abstract] [Full Text] [PDF]
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N. Kayagaki, N. Yamaguchi, M. Nakayama, A. Kawasaki, H. Akiba, K. Okumura, and H. Yagita Involvement of TNF-Related Apoptosis-Inducing Ligand in Human CD4+ T Cell-Mediated Cytotoxicity J. Immunol., March 1, 1999; 162(5): 2639 - 2647. [Abstract] [Full Text] [PDF]
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L. Zamai, M. Ahmad, I. M. Bennett, L. Azzoni, E. S. Alnemri, and B. Perussia Natural Killer (NK) Cell-mediated Cytotoxicity: Differential Use of TRAIL and Fas Ligand by Immature and Mature Primary Human NK Cells J. Exp. Med., December 21, 1998; 188(12): 2375 - 2380. [Abstract] [Full Text] [PDF]
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F. Muhlenbeck, P. Schneider, J.-L. Bodmer, R. Schwenzer, A. Hauser, G. Schubert, P. Scheurich, D. Moosmayer, J. Tschopp, and H. Wajant The Tumor Necrosis Factor-related Apoptosis-inducing Ligand Receptors TRAIL-R1 and TRAIL-R2 Have Distinct Cross-linking Requirements for Initiation of Apoptosis and Are Non-redundant in JNK Activation J. Biol. Chem., October 6, 2000; 275(41): 32208 - 32213. [Abstract] [Full Text] [PDF]
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C. A. Benedict, P. S. Norris, T. I. Prigozy, J.-L. Bodmer, J. A. Mahr, C. T. Garnett, F. Martinon, J. Tschopp, L. R. Gooding, and C. F. Ware Three Adenovirus E3 Proteins Cooperate to Evade Apoptosis by Tumor Necrosis Factor-related Apoptosis-inducing Ligand Receptor-1 and -2 J. Biol. Chem., January 26, 2001; 276(5): 3270 - 3278. [Abstract] [Full Text] [PDF]
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A. K. Simon, O. Williams, J. Mongkolsapaya, B. Jin, X. N. Xu, H. Walczak, and G. R. Screaton Tumor necrosis factor-related apoptosis-inducing ligand in T cell development: Sensitivity of human thymocytes PNAS, April 24, 2001; 98(9): 5158 - 5163. [Abstract] [Full Text] [PDF]
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