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 Previous Article | Table of Contents | Next Article 
Blood, Vol. 91 No. 12 (June 15), 1998:
pp. 4419-4426
Fusion of Huntingtin Interacting Protein 1 to Platelet-Derived Growth
Factor  Receptor (PDGFR) in Chronic Myelomonocytic Leukemia
With t(5;7)(q33;q11.2)
By
Theodora S. Ross,
Olivier A. Bernard,
Roland Berger, and
D. Gary Gilliland
From the Division of Hematology/Oncology, Brigham and Women's
Hospital and Division of Oncology, Dana-Farber Cancer Institute,
Boston, MA; the U 301 de L'Institut National de la Santé et de
la Recherche Medicale (INSERM) and SD 401 No. 301 CNRS, Institut de
Genetique Moleculaire, Paris, France; and the Howard Hughes Medical
Institute, Harvard Medical School, Boston, MA.
 |
ABSTRACT |
We report the fusion of the Huntingtin interactin protein 1 (HIP1) gene to the platelet-derived growth factor
 receptor (PDGFR) gene in a
patient with chronic myelomonocytic leukemia (CMML) with a
t(5;7)(q33;q11.2) translocation. Southern blot analysis of patient bone
marrow cells with a PDGFR gene probe
demonstrated rearrangement of the PDGFR gene.
Anchored polymerase chain reaction using PDGFR
primers identified a chimeric transcript containing the HIP1
gene located at 7q11.2 fused to the PDGFR gene
on 5q33. HIP1 is a 116-kD protein recently cloned by yeast two-hybrid
screening for proteins that interact with Huntingtin, the mutated
protein in Huntington's disease. The consequence of t(5;7)(q33;q11.2) is an HIP1/PDGFR fusion gene that encodes amino
acids 1 to 950 of HIP1 joined in-frame to the transmembrane and
tyrosine kinase domains of the PDGFR. The reciprocal
PDGFR/HIP1 transcript is not expressed.
HIP1/PDGFR is a 180-kD protein when expressed in the murine
hematopoietic cell line, Ba/F3, and is constitutively tyrosine
phosphorylated. Furthermore, HIP1/PDGFR transforms the Ba/F3 cells
to interleukin-3-independent growth. These data are consistent with an
alternative mechanism for activation of PDGFR tyrosine kinase
activity by fusion with HIP1, leading to transformation of
hematopoietic cells, and may implicate Huntingtin or HIP1 in the
pathogenesis of hematopoietic malignancies.
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INTRODUCTION |
MYELODYSPLASTIC syndromes (MDS) and acute
leukemias are disorders of hematopoietic progenitor cells characterized
by acquired somatic mutations that confer a proliferative advantage.
Cloning of chromosomal translocation breakpoints has been a productive strategy for identification of disease genes in MDS. Examples include
the AML1-EVI1 fusion associated with t(3;21),1 the MLL-CBP fusion with t(11;16) in therapy-related
MDS,2 the TEL-EVI1 fusion in t(3;12),3
the NPM-MLF1 fusion associated with t(3;5) in primary
MDS,4 and the TEL/JAK25 and
TEL/PDGFR fusions that are associated with
t(9;12) and t(5;12) in chronic myelomonocytic leukemia (CMML),
respectively.6
Several of the fusion genes associated with hematopoietic disorders
involve tyrosine kinases. These include BCR/ABL,7,8 TEL/PDGFR,6
TEL/ABL,9 TEL/JAK2,5,10 and
CEV14/PDGFR.11 CMML, associated
with the TEL/PDGFR, is a subtype of MDS characterized by dysplastic
monocytosis, variable bone marrow fibrosis, and progression to acute
leukemia. The clinical phenotype is similar to chronic myelogenous
leukemia associated with constitutive activation of the ABL kinase by
fusion with BCR. There is also convincing evidence for contribution of
tyrosine kinases to pathogenesis of solid tumors. Noteworthy examples
include point mutations that constitutively activate the RET
tyrosine kinase gene in medullary carcinoma of the
thyroid,12 amplification of the HER2/neu receptor tyrosine
kinase in breast cancer,13 and the ETV6-NTRK3 gene fusion in congenital fibrosarcoma.14
A subset of patients with CMML have a t(5;12)(q33;p13) that results in
fusion of the amino terminal portion of TEL, which contains the pointed
(PNT) oligomerization domain, to the transmembrane and tyrosine kinase
domains of platelet-derived growth factor receptor (PDGFR). The
consequence of the fusion is constitutive oligomerization and
activation of PDGFR tyrosine kinase activity leading to
transformation of cells.15 PDGFR kinase activity is
required for transformation of Ba/F3 cells as is the PNT
domain.15 We report here a novel PDGFR fusion associated
with CMML and t(5;7)(q33;q11.2) involving the Huntingtin Interacting
Protein 1 (HIP1).
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MATERIALS AND METHODS |
DNA isolation and Southern blots.
Leukocytes were isolated by ficoll sedimentation from the peripheral
blood and bone marrow of the index patient and normal controls after
informed consent had been obtained. DNA was prepared using
standard methods.16 After enzymatic digestion with
restriction endonucleases and electrophoretic separation of fragments,
the genomic DNA was transferred to HYbond N nylon membranes (Amersham, Arlington Heights, IL). The PDGFR genomic probe was a
1.1-kb HindIII-Xho I fragment prepared from PDGFR
cosmid B.17 Probes were labeled with 32P by
random priming, and Southern hybidizations were performed as
described.18
Cloning of the t(5;7) breakpoint.
Mononuclear cells were isolated from t(5;7) bone marrow cells by ficoll
sedimentation. Anchored polymerase chain reaction (PCR) was performed
to clone the human chromosome 7 partner gene according to the method of
Frohman19 with minor modifications. In brief, total RNA was
prepared with RNA-STAT reagents according to the manufacturer's
recommendations (Tel-Test, Inc, Friendswood, TX). RNA (3 µg) was
reverse transcribed using avian myeloblastosis virus (AMV) reverse
transcriptase and PDGFR oligonucleotide primer 1873R
(5 -CGTAACGTGGCTTCTTCTGC-3). A poly(A) tail was appended using terminal transferase and dATP at 37°C for 15 minutes. After a
single cycle of amplification (94°C for 1 minute, 50°C for 2 minutes, and 72°C for 40 minutes) using primer Qt
(5-TGAGCAGAGTGACTATTACTCGAGCTCAAGCTTTTTTTTTTTT-3) and
internal PDGFR primer 1848R
(5-AGTCTCGAGCATGATGAGGATGATAAG-3), 30 cycles of PCR
(94°C for 1 minute, 58°C for 2 minutes, and 72°C for 3 minutes) were performed with primers Qo
(5-CCAGTGAGCAGAGTGACG-3) and 1848R. The PCR products were
diluted 20-fold and reamplified with nested primers 1829R
(5-GAGATGATGGTGGAGCACCAC-3) and Q1 (5-GAGGACTCGAGCTCAAGC) using the same PCR conditions (30 cycles of 94°C for 1 minute, 58°C for 2 minutes, and 72°C for 3 minutes). Specific bands were not detected by direct visualization
after ethidium bromide staining, but were detectable by Southern blot analysis using the 32P-end-labeled PDGFR 1806R oligo
(5-GGCCAGGATGGCTGAGATCA-3). The nested PCR product was
subsequently diluted 20-fold and reamplified with primer 1806R and Q1
(30 cycles of 94°C for 1 minute, 58°C for 2 minutes, and
72°C for 3 minutes), yielding a specific 500-bp product that was
subcloned into pBluescript KS(+) (Stratagene, La Jolla,
CA) and sequenced. The DNA sequence was sent via Netscape to the BLAST server at NIH (http://www.ncbi.nlm.nih.gov) to compare to
GenBank (blastn).
Library screening.
In light of the high mRNA levels of HIP1 in tumor cell lines, the cDNA
sequence isolated by anchored PCR was used to screen a  gt11 SW480
colon cancer cell line cDNA library (Clontech, Palo Alto,
CA) to obtain more 5 sequence. The 500-bp PCR
product obtained from cloning of the breakpoint was labeled with
32P by random priming and plaque lifts were
performed.18 Positive phage clones were subcloned into
pBluescript KS(+) and sequenced.
In the longest clone, SW9, there were 2 new potential in frame
initiator methionines in the additional 5 sequence. The first ATG at nucleotides 16-19 has a better Kozak consensus sequence than the
second ATG (nucleotides 37-39). The third methionine at position
368-370 (or 248-250 of the previously published sequence20) has the best fit of the 3, because it has a purine at position  3. No upstream stop codons were identified. However, native HIP1 migrates as a protein of 116 kD by Western blot
analysis,20,21 which is consistent with a preferred start
site at methionine 368-370.
Reconstruction of the fusion cDNA for expression experiments.
The chromosome translocation breakpoint was amplified from patient
material using primers HIP1301F
(5-CCTGAAACTGCTAAGAACCA-3) and PDGFR 1806R, and the
product was digested with Bgl I and Nhe I. The
Bgl I-Sac II fragment of the
PDGFR was isolated after Bgl I and
Sac II digestion of the PDGFR cDNA and
ligated to the Nhe I-Bgl I breakpoint fragment. This
ligation reaction was amplified with primers containing the Nhe
I and Sac II sites
(5-AAATTGCTGCTAGCACAGCCCAGCTTG-3 and
5-CTGGTCCCGCGGCAGCTCCCACGTGGA-3 respectively), digested with Sac II, and ligated with the 3 end of
PDGFR.22 The reaction mixture was
then digested with Nhe I and ligated with the 5 end of
HIP1 (from SW480 l clone 9) via the unique Nhe I site.
The region amplified by PCR was confirmed to be void of PCR generated mutations by sequence analysis.
Stable expression of HIP1/PDGFR.
The full-length fusion cDNA was subcloned into the pMSCVneo vector
(kindly provided by R. Hawley, University of Toronto, Toronto, Ontario,
Canada). Bosc cells (the kind gift of W. Pear, University of Pennsylvania, Philadelphia, PA) were transfected via
the calcium phosphate technique.18 The 48-hour supernatent
(1 mL) was then added to 106 Ba/F3 cells (1 mL) in the
presence of polybrene (4 µL) as described previously.23
Cells with stable expression were selected in the presence of G418 and
interleukin-3 (IL-3) as described.15
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RESULTS |
Identification of HIP1/PDGFR in CMML.
The HIP1/PDGFbR fusion was cloned from a single patient with a clinical
phenotype of CMML. The patient was a 54-year-old man who presented with
fatigue, weight loss, and splenomegaly. Laboratory evaluation showed
monocytosis, anemia, and peripheral eosinophilia. Bone marrow biopsy
showed a hypercellular marrow with increased myeloid:erythroid ratio,
eosinophilia, and dysplastic maturation of monocyte lineage cells.
Cytogenetic analysis of the bone marrow cells showed t(5;7)(q33;q11.2)
(data not shown).
We hypothesized that the PDGFR on 5q33 was activated as a
consequence of fusion to a novel partner on chromosome 7. This region
of chromosome 7 is of particular interest because it is frequently
deleted in de novo and therapy-related MDS/AML. Rearrangement of the
PDGFR gene was demonstrated by Southern blot
analysis of EcoRI, BamHI, Pst I, EcoRV,
and HindIII digests using a 1.1-kb PDGFR genomic probe localized near the
TEL/PDGFR breakpoint (Fig 1). These data demonstrated that the
chromosome 5 breakpoint was at or near the same intron of
PDGFR as for the t(5;12)(q33;p12) breakpoint.6
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| Fig 1.
Identification and molecular analysis of
t(5;7)(q33;q11.2). Southern blot analysis of the
PDGFR gene locus in patient DNA with
t(5;7)(q33;q11.2). Genomic DNA of patient t(5;7)-positive cells (lane
1) and control cells (lane 2) was analyzed by Southern blotting with a
1.1-kb HindIII-Xho I PDGFR
probe.6 Arrows indicate the rearranged bands in the
EcoRI, BamHI, Pst I, EcoRV, and
HindIII digests.
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The chromosome 7 fusion partner was identified using anchored PCR with
PDGFR primers to amplify the fusion transcript
from the patient's bone marrow cell cDNA
(Fig 2A). Analysis of the amplified cDNA
clones demonstrated 500 bp of non-PDGFR
sequence encoding an open reading frame fused to the transmembrane
and tyrosine kinase encoding regions of the
PDGFR gene (Fig 2B). A database search showed
this sequence to be identical to the HIP 1 gene20,21 localized by fluorescence in situ hybridization (FISH) to 7q11.2.20 Southern blot analysis with an
HIP1 cDNA probe (nucleotides 1141-3041) demonstrated rearranged
bands in Pst I and Xba I digests of patient DNA (Fig
2C).
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| Fig 2.
Identification of the chromosome 7 fusion partner. (A)
Schematic diagram of anchored PCR.6,19 (B) Sequence of the
HIP1/PDGFR breakpoint and schematic of the
fusion protein. (C) Southern blot analysis of HIP1 gene locus
in control DNA (lanes 1 and 2) and patient DNA (lane 3). Arrows
indicate rearranged fragments in the Pst I and Xba I
digests.
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HIP1 is a 116-kD protein that was cloned by yeast two-hybrid screening
for proteins that interact with Huntingtin. Huntingtin is the protein
mutated in Huntington's disease.24 HIP1 has a leucine
zipper motif and homology to talin, a cytoskeletal associated protein,
at amino acids 412-433 and 861-900, respectively.20
HIP1 has homology with the SLA2 gene product (Sla2p) from
Saccharomyces cerevisiae,25 an
essential cytoskeletal associated protein. The leucine zipper motif and
talin homology domain of HIP1 are conserved in Sla2p. HIP1 is also
homologous to the Caenorhabditis elegans ZK370.3
gene product that has no known function.26 The degree of
homology (40% similarity, 20% identity in both yeast and worm)
suggests that HIP1 is the human homologue of these proteins. The
highest degree of homology is at the carboxy terminus, where all 3 proteins share homology with talin.27
Tissue expression of HIP1/PDGFR and HIP1.
Reverse transcription-PCR (RT-PCR) using PDGFR
3 primers and 5 primers spanning the coding sequence of
HIP1 generated the expected size fragments from patient cDNA
(Fig 3), but was not detected in mRNA from
normal bone marrow. The reciprocal PDGFR/HIP1 fusion could not be detected by RT-PCR analysis (data not shown). Because bone marrow cells from the patient were limited, detection of
the fusion transcript required the use of nested PCR primers. In
addition, because of this limitation, Northern blot analysis of patient
material was not possible. HIP1/PDGFR protein contained nearly all
of the HIP1 coding sequence, including the leucine zipper and
talin homology domains, fused in frame to the transmembrane and
tyrosine kinase domain of the PDGFR (Fig 2B). Only 18 C-terminal amino acids of HIP1 were excluded from the fusion protein.
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| Fig 3.
Expression of the chimeric
HIP1/PDGFR mRNA in patient bone marrow. RT-PCR
analysis of HIP1/PDGFR was performed using
total RNA (2 µg) from t(5;7) patient bone marrow that had been
reverse transcribed using the Qt primer. PCR was performed using a
HIP301F forward primer and the PDGFR 1848R primer for 30 cycles
(94°C for 1 minute, 60°C for 2 minutes, and 72°C for 3 minutes). Nested PCR was performed on PCR products from the first
reaction diluted 20-fold and amplified using the same PCR reaction
conditions with HIP1 forward primers HIP721F, HIP1141F, HIP1561F,
HIP2372F, HIP2494F, and HIP2613F in lanes 1 through 6, respectively,
and the PDGFR reverse primer 1806R. HIP1 primer numbers
correspond to the first nucleotide of a 20-bp primer of HIP1 sequence
according to Kalchman et al.20 The expected band sizes are
2,279, 1,859, 1,439, 628, 506, and 387 bp for lanes 1 through 6, respectively. Control experiments with no template or in the absence of
reverse transcriptase gave no PCR product (not shown). The
HIP1/PDGFR fusion was not detected in normal
bone marrow and neither was the reciprocal
PDGFR/HIP1 fusion transcript detected in t(5;7)
patient bone marrow using a nested PCR reaction with primers
PDGFR1691F, PDGFR1711F, HIP13071R, and
HIP12966R (primer numbers correspond to the first nucleotide of a 20-bp
primer of either PDGFR22 or
HIP120 sequence).
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Northern blot analysis using an HIP1 cDNA probe demonstrated a
previously reported 9.4-kb transcript in all tissues
tested20 as well as a 2.4-kb transcript present in testis.
There are high levels of expression in solid tumor cell lines,
including HeLa, SW480, A549, and G861, as well as in testis. Although
HIP1 has been implicated in pathogenesis of central nervous system
disorders such as Huntington syndrome, there are lower levels of
expression in brain and other adult tissues such as bone marrow and
peripheral blood (Fig 4 and data not
shown).
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| Fig 4.
Northern blot analysis of HIP1 mRNA in various
tissues. Blots (Clontech) were probed with with an
32P-end-labeled probe from HIP1 nucleotides 2890 to
2930.20 Exposure time was 12 hours. The lower panels are
the same blots stripped and reprobed with actin cDNA. (A) Cell lines.
RNA sources were HL60, HELA, K562, MOLT4, Raji, SW480, A549, and G361,
designated 1 through 8, respectively. (B) Adult tissue RNA sources are
spleen, thymus, prostate, testis, ovary, small intestine, colonic
mucosa, and peripheral blood, designated 1 through 8, respectively.
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Transformation of Ba/F3 cells by HIP1/PDGFR.
To characterize the biological properties of the HIP1/PDGFR fusion,
a full-length cDNA encoding HIP1 was obtained by screening a
gt11 SW480 colon cancer cell line cDNA library. The sequence of the
longest clone, SW9, from this library is identical to the published
sequence, but incorporates and additional 120 nucleotides of 5
sequence.
Clone SW9 was then used to reconstruct the full-length
HIP1/PDGFR (see the Materials and Methods).
Transforming properties of HIP1/PDGFR were tested by
subcloning the cDNA encoding the HIP1/PDGFR
into the retroviral vector MSCVneo and obtaining stable expression of
the fusion protein under control of the LTR in the murine Ba/F3
hematopoietic cell line (Fig 5A). The
HIP1/PDGFR protein was constitutively tyrosine phosphorylated in
stably transfected cells (Fig 5B).
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| Fig 5.
HIP1/PDGFR transforms Ba/F3 cells to factor
independence. Two independent infections of Ba/F3 cells were performed.
To assess protein expression and phosphorylation, lysates were
immunoprecipitated with anti-PDGFR antibody (tail; Pharmingen),
separated on 8% polyacrylamide gel electrophoresis
(PAGE), and blotted onto nitrocellulose. Proteins were
detected with anti-PDGFR peptide antibody directed against the
C-terminus (part a) and HRP-conjugated anti-phosphotyrosine 4G10
monoclonal antibody (part b). Lanes 1 and 2 are the HIP1/PDGFR stable infectants, and lanes 3 and 4 are neomycin-resistant controls. (C) The G418-resistant cells growing in IL-3 were seeded in 96-well trays with 2 × 104 cells per 200 µL per well in RPMI
1640 and 10% fetal calf serum media with or without IL-3. Cells were
assessed for number and viability (trypan blue) in triplicate at
24-hour intervals. Each point is the average of the triplicate samples,
with standard deviations ranging from 1% to 3% of the number of cells
counted each day.
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To assay the ability of HIP1/PDGFR to confer IL-3-independent
proliferation, Ba/F3-transfected cells were seeded in 96-well trays at
a concentration of 2 × 104 cells/well. Cells infected
with insert-free virus failed to proliferate in the absence of IL-3 and
died. In contrast, HIP/PDGFR-expressing cells grew at the same rate
in the presence or absence of IL-3 (Fig 5C).
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DISCUSSION |
Involvement of HIP1 in the pathogenesis of leukemia is a novel finding.
As for TEL/PDGFR, fusion of HIP1 to PDGFR results in constitutive
activation of PDGFR as assessed by tyrosine autophosphorylation and
may be mediated by oligomerization through the HIP1 leucine zipper
domain. However, other interactions with this fusion may be relevant to
the pathogenesis of leukemia in addition to the protein-protein
interation mediated by the leucine zipper. For example, the leucine
zipper is not necessary for the interaction of HIP1 with
Huntingtin.20 Although the role of HIP1 in Huntingtin's disease is still under investigation, it is conceivable that inhibition of apoptosis mediated by HIP1, as suggested in by Kalchman et al,20 is also relevant in leukemogenesis mediated by the
HIP1/PDGFR fusion. Thus, there may be an additional role for HIP1 in
the leukemogenic pathway.
There are several possible consequences of expression of the
HIP1/PDGFR fusion that may be relevant to leukemogenesis. These could include interference with the function of the native HIP1 protein
or the Huntingtin protein through HIP1/PDGFR heterodimerization. In
addition, it is possible that, because the HIP1/PDGFR is an activated tyrosine kinase, heterodimerization with HIP1 or Huntingtin could modify function or protein stability of these associated proteins
through tyrosine phosphorylation. Because the physiologic roles of
HIP1, Huntingtin, and the HIP1/Huntingtin complex are not well
understood, it is difficult to speculate at this time about the
relevance of these interactions in the mechanism of transformation.
However, it should be possible to directly assay for these interactions
and determine whether dysregulation of the apoptotic pathway in
hematopoietic cells as a consequence of HIP1/PDGFR interactions with
HIP1 or Huntingtin contributes to leukemogenesis.
Finally, HIP1 localization to 7q11.2 raises the possibility of
involvement in 7q deletions. Loss of chromosome 7 or deletion of
the long arm, del(7q), is observed in 10% of MDS or AML de novo and in
greater than 50% of therapy-related AML.28 7q
cytogenetics are associated with particularly poor
prognosis.28 It has been hypothesized that deleted
chromosomal bands contain as yet unidentified myeloid-specific tumor
suppressor loci. Most 7q deletions are interstitial and some have been
found to be the result of cryptic translocations.29-31 The
majority of patients with deletions have proximal breakpoints in bands
q11-21 and distal break points in q31-36.29-31 FISH has
been used with a panel of YAC clones from 7q to examine patients with
deletion breakpoints near 7q22. These data are being used to to narrow
down the region of deletion to clone tumor-suppressor genes on 7q
involved in myeloid leukemia.29-31 Other data that may be
useful in narrowing the critically deleted region is to characterize
translocations in this area, such as the t(5;7) described herein, that
could result in inactivation or dysregulaton of tumor-suppressor genes.
Examples in which translocations that disrupt the function or
expression of tumor-supporssor genes include a translocation that
disrupts p16.32 In addition, it has been proposed
that disruption of PML, a putative growth suppressor, as a consequence
of the t(15;17) chromosomal translocation, may contribute to the
pathogenesis of acute promyelocytic leukemia.33 The
possibility that HIP1 is one of the important genes in this area is
currently being investigated.
Analysis of HIP1/PDGFR should contribute to our understanding of the
pathogenesis of CMML and may help to elucidate the function of
Huntingtin and HIP1 in normal and neoplastic cells. Furthermore, localization of HIP1 to 7q11.2 warrants an investigation of its relevance in pathogenesis of hematopoietic malignancies with 7q deletions.
| |
FOOTNOTES |
Submitted February 24, 1998;
accepted March 18, 1998.
Supported in part by National Institutes of Health Grants No. T32
HL07623 and PO1CA66996-01, the Lawrence Family foundation, the Ligue
Nationale Contre le Cancer and the Ligue Nationale Contre le Cancer,
Comité de Paris. D.G.G. is a Stephen Birnbaum Scholar of the
Leukemia Society of America and an assistant investigator of the Howard
Hughes Medical Institute.
Address reprint requests to D. Gary Gilliland, MD, PhD, Division of
Hematology/Oncology, Brigham and Women's Hospital, 4 Blackfan Circle,
Boston, MA 02115.
The publication costs of this article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" is accordance with 18 U.S.C. section 1734 solely to indicate this fact.
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ACKNOWLEDGMENT |
The authors are grateful to James Griffin, Charis Eng, and Thomas
McClean for critical review of this work.
| |
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Abstract
Introduction
Abstract