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A Novel Antigen Detected by the CBF.78 Antibody Further Distinguishes
Anaplastic Large Cell Lymphoma From Hodgkin’s Disease
By Tala1 AI Saati, Jean Tkaczuk, Geoffrey Krissansen, Cristin Print, Stefan0 Pileri, Elisabeth Ralfkiaer,
Thomas M. Grogan, Fabienne Meggetto, and Georges Delsol
A novel antigen detected by the CBF.78 monoclonal antibody (MoAb) is strongly expressed on cortical thymocytes
and weakly expressed on resting peripheral T lymphocytes.
Expression of theantigen is increased on phytohemagglutinin (PHA)- and anti-CD3-activated T lymphocytes and on
Epstein-Barr virus-transformed B lymphocytes. The CBF.78
immunoprecipitated a protein of 116 kD from resting and
PHA-activated peripheral blood mononuclear cells. CBF.78
MoAb did not inhibit T-cell proliferation induced by anti-CD3
antibody. This MoAb was effective for immunostaining on
paraffin sections after microwave-oven heating
of tissue sections. Among malignant lymphomas, the antigen recognized
by CBF.78 MoAb was found t o be mainly expressed by Tcell lymphomasW + of 74). particularly thoseof high-grade
malignancy (31+ of 361, whereas only occasional B-cell lym-
phomas (4+ of 107) expressed the antigen. A distinctive pattern ofreactivity wasshown by108 casesof anaplastic large
cell lymphomas. Strong positivity for CBF.78 antibody was
observed in 86+ of 108 cases, irrespective of B,T, or null
phenotype. This multicenterstudy suggests that CBF.78
MoAb could be of diagnostic value in differentiating Hodgkin‘s-like anaplastic large cell lymphomas from cases of
Hodgkin’s disease rich in neoplastic cells. Only a few cases of
Hodgkin’s disease(13+ of 126) showed rare Reed-Sternberg
cells that stained, In these few cases, staining was weak
t o moderate and confined t o cytoplasm. CBF.78 MoAb was
nonreactive with all nonhematopoietic neoplasms examined
(0+ of 48). Further studies should delineate the function of
this new antigen and its clinical utility.
0 1995 b y The American Society of Hematology.
A
of human tonsil.’ The CBF.78 MoAb was selected for further detailed study because of its strong reactivity with both frozen and
paraffin sections of CEM tumors and because the antibody detected
only a few cells in the paracortical areas of reactive lymphoid tissues.
These observations, along with negative reactivity with resting lymphocytes on tissue sections, suggested that this MoAb might be
directed against a T-cell-associated antigen expressed by a subpopulation of T lymphocytes and lymphomas. Isotype characterization
showed that the CBF.78 MoAb was of IgGl subclass.
T THE FIFTH JNTERNATIONAL Conference on Human Leukocyte Differentiation Antigens, a group
(GR3) of new monoclonal antibodies (MoAbs) was found
to share a number of characteristics defining the CDlOO
“cluster of differentiation.”’ CDlOO is a disulfide-linked
homodimer of 150-kD polypeptide chains expressed at the
surface of the majority of hematopoietic cells, whose expression on T-lymphocytes increases readily after lectin stimulati~n.’.~
The molecule is also expressed on Epstein-Barr virus
(EBV)-transformed and various T-cell lines but is not present
on malignant nonhematopoietic cells. The CBF.78 antibody
was tentatively clustered with the GR3 MoAbs based on its
pattern of distribution; however, the structural properties of
the antigen recognized by the CBF.78 MoAb have never
been reported. With the description of anaplastic large cell
lymphoma (ALCL), the diagnosis of Hodgkin’s disease
(HD) has become more difficult. The recent recognition of
Hodgkin’s-like variant of ALCL has further emphasized this
difficult problem in diagnostic histopathology:We report
here that the CBF.78 MoAb detects a new antigen distinct
from CD100 that is predominantly expressed on activated T
and, to a lesser extent, B lymphocytes. In testing this new
MoAb with malignant lymphomas, it appeared that the
CBF.78 antigen was strongly expressed by T-cell lymphomas, especially of high grade, and by CD30+ ALCL. Thus,
the CBF.78 MoAb may have clinical utility in assisting the
differential diagnosis between ALCL and HD. It may also
be used for retrospective analysis of tumor samples, because
it is reactive on routinely processed paraffin sections.
MATERIALS AND METHODS
Production of CBF.78 MoAb
Balblc mice were immunized at 2-week intervals with 3 intraperitoneal injections of CEM-cells (ATCC CCL 119; 10 to 20 x IO6
cells per inje~tion).~
Mice received intravenous and intraperitoneal
injections of 5 X lo6 and 10 X lo6 CEM cells, respectively, 3 days
before fusion of the spleen cells with the non-Ig-producing myeloma
cell line P3 X63-Ag8-653P When hybridoma growth could be detected, supernatants were tested by an immunoperoxidase staining
method for the presence of MoAbs that could bind to frozen sections
of xenografted CEM tumors formed in nude mice and to sections
Blood, Vol 86, No 7 (October l ) , 1995: pp 2741-2746
Flow Cytometric Analysis of Peripheral Blood
Mononuclear Cells (PBMs)
PBMs from healthy donors were isolated on Ficoll gradient,
washed in RPMI 1640 (Eurobio, Paris, France), and resuspended at
a density of 1 X IO6 /mL in RPMI medium supplemented with 10%
fetal calf serum (BioWHITI’AKER, Fontenay S / S Bois, France).
Fresh PBMs and lymphoblasts stimulated for 72 hours with either
10 pg/mL phytohemagglutinin (PHA; Sigma, St Louis, MO) or 10
pg/mL of cross-linked anti-CD3 MoAb (X35 clone; Immunotech,
Marseille, France) were examined simultaneously by flow cytometry
(Becton Dickinson FACScan and LYSIS II software; Becton Dickin-
From the Department of Pathology and CIGH/CNRS, CHU-Purpan, Toulouse, France; the Department of Immunology, CHU-Rangueil, Toulouse, France; the Department of Molecular Medicine,
School of Medicine, University of Auckland, Auckland, New
Zealand; the Department of Hematology, University of Bologna,
Bologna, Italy; the Department of Pathology, Herley Hospital and
University of Copenhagen, Herley, Denmark; and the Department
of Pathology, College of Medicine, University of Arizona, Tucson,
AZ.
Submitted December 29, 1994; accepted June 5, 1995.
Supported by “Association pour la Recherche sur la Cancer No.
6229” and the “Dildgation a la Recherche Clinique. ”
Address reprint requests to GeorgesDelsol, MD, Laboratoire
d’Anatomie Pathologique, CHU Purpan, Place du Dr. Baylac,
31059, Toulouse Cedex, France.
The publication costs of this article were defrayed in part by page
charge payment. This article must therefore be hereby marked
“advertisement” in accordance with 18 U.S.C. section 1734 solely to
indicate this fact.
0 1995 by The American Society of Hematology.
0006-4971/95/8607-09$3.00/0
2741
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2742
AL SAATI ET AL
Table 1. Reactivity of CBF.78 MoAb With Lymphoma Cell Lines
Investigated Using Flow Cytometric Analysis
~~
Cell Lines
CBF.78
Reference
-
11*
12'
-
x
Lymphoma cell lines
B-cell lymphomas
DEAU
Deglis
LIB
MIEUL
OCI LY8 C3
PASC
Raji
Rec-l
VAL
T-cell lymphomas
CEM
GER
HSB-2
lchikawa
Jurkat
Monocyte/histiocytecell lines
*
~
~
+
+
+
+
+
U-937
+
THP-1
TIB
-
13
x
(ATTC CCL 86)
14
15
(ATTC CCL 119)
*
(ATTC CCL 120.1)
16
(ATTC CRL 8163)
(ATTC CRL 1593)
(ATTC
202)
~~
Abbreviation: ATTC, American Type Culture Collection, Rockville,
MD.
* Lymphoma cell lines from own laboratory.
son, Mountain View, CA) for the presence of CBF.78 and other
cell surface markers. Lymphocytes and lymphoblasts were gated for
differential analysis. Unstimulated PBMs cultured for 72 hours in
the absence of activating agents were used as control. Fresh PBMs
and blast cells were double-stained with the CBF.78 MoAb, followed
by a fluorescein-conjugated rabbit antimouse Ig antibody (Dakopatts,
Copenhagen, Denmark), and then with one of the following phycoerythrin-labeled antibodies: anti-CD19Leul2 (Becton Dickinson),
anti-CDUDAKO-CD2 (Dakopatts), anti-CD40OT4a and anti-CDS/
IOT8a (Immunotech). The effect of CBF.78 MoAb on T-cell proliferation was evaluated by the addition of 10 to 300 pL CBF.78
supernatantlml of culture medium. The number of proliferative T
cells was assessed by double-labeling with phycoerythrin-conjugated
anti-CD2DAKO-CD2 and fluorescein-conjugated Ki-67 MoAb (Dakopatts).' PBMs were permeabilized with a solution of 1% Saponin
(Merck CO, Paris, France) before labeling with the Ki-67 MoAb.'
Quantification of the relative number of CBF.78 molecules on resting
and stimulated T cells was performed using QUIFIKIT calibrated
beads of (Biocytex-France, Marseille) as previously described.'" Sixteen lymphoma cell lines of B-cell (n = 9), T-cell (n = S), or
monocytichistiocytic-cell (n = 2) origin were also analyzed for their
reactivity with CBF.78 antibody (Table 1).
Immunoprecipitation Analysis
PBMs were isolated from fresh heparinized venous blood of a
healthy donor, by centrifugation on Ficoll-Hypaque density gradients
(Pharmacia, Uppsala, Sweden). Cells were washed in RPMI 1640,
and lymphoblasts were prepared by culturing for 3 days in RPMI
1640 medium containing penicillin, streptomycin, 10% (vol/vol) fetal calf serum (GIBCO-BRL, Gaithersburg, MD), and 1:lOO dilution
of PHA (M-form; GIBCO) at 37°C in a 6% CO, incubator. Resting
PBMs and PHA-stimulated lymphoblasts were labeled at the cell
surface by lactoperoxidase-catalyzed iodination and were solubilized
for 30 minutes in 1%(voUvol) Nonidet P-40 in 10 mmolL TrisHCI buffer [pH 7.41 and IS0 mmovL NaCl containing 20 m m o K
iodoacetamide, 2 mmolL phenylmethylsulfonyl fluoride, 10 pg/mL
pepstatin A, 20 pg/mL leupeptin, 10 U/mL aprotinin, and S0 pg/
mL soybean trypsin inhibitor. Lysates were precleared with 1 0 0 pL
of a 10% (wtlvol) suspension of Staphylococcus aureus (Cowan
strain; Sigma), with 20 pL of Protein G-Sepharose, and with S0 pL
of rabbit-IgG-Sepharose 4B. Immunoprecipitation was performed
for 1 hour using 4 pL of CBF.78 ascites, 3 pL of BB18 ( 1 mg/mL).
and IS pL of Protein-G-Sepharose 4B; and for the Ig control, IS
pL of rabbit IgG-Sepharose 4B was used. Immunoprecipitates were
processed as described previously," and analyzed by sodium dodecyl
sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) on 7.5%
polyacrylamide slab gels. Labeled proteins were detected by autoradiography at -70°C using Kodak XAR-Sfilm (Eastman Kodak.
Rochester, NY) with intensifying screens (Cronex lightning plus:
DuPont, Wilmington, DE). Apparent molecular weights were calculated by reference to the mobilities of the following proteins: myosin
(205 kD), @galactosidase (1 16 kD), phosphorylase b (95 kD), bovine serum albumin (66 kD), and ovalbumin (45 kD).
Immunostaining of Various Human Normal und Neoplastic
Tissue Sections
Tissue samples obtained from the institutes in Toulouse, France,
were fixed in ethanol-based Bouin's (Duboscq-Brasil) fluid, and tissue samples obtained from the institutes in Bologna, Italy, Copenhagen, Denmark, and Tucson, AZ, were fixed in 10% formalin. Different human tumors from our tissue bank (n = 469) were investigated.
These included (1) 421 cases of hematopoietic neoplasms (including
289 non-Hodgkin's lymphomas of BorT phenotype, 126 cases
HD, and 6 myeloid leukemias [see Table 21) and (2) 48 cases of
nonlymphoid tumors of different categories.
Table 2. Reactivity of CBF.78 MoAb With Hematopoietic
Neoplasms on Paraffin-Embedded Sections
Type
CBF.78'INo. Tested
(Oh)
NHLs other than ALCL
B-cell lymphomas
Low grade
High grade
Unclassified
Total
T-cell lymphomas
Low grade
High grade
Unclassified
Total
0145 (0)
3/59 (51
1l 3
4/107 (4)
9/21 (43)
31/36 (86)
9117
49/74 (66)
ALCL
B
T
BTr
Null
Undetermined
Total
HD
LP
NS
MC
Unclassified
Total
Myeloid leukemia
Total (overall)
13/20
36/43
212
20/28
15/15
861108 (80)
0/8
1OB6
3/29
013
13/126 (10)
0/6
152/421 (36)
Abbreviations: NHL, non-Hodgkin's lymphoma; LP, lymphocyte
predominance; NS, nodular sclerosis; MC, mixed cellularity.
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MoAb REACTIVE WITH ANAPLASTICLARGECELL
Supernatants and ascites fluids were used for studying CBF.78
MoAb reactivity on paraffin-embedded tissue sections of various
types of tumorsandnormal tissues. In all cases, antigen retrieval
byheat-treatmentin a microwave oven was used.Ix Most sections
were immunostained by the streptavidin-biotin-peroxidase complex
(ABC) method using the Dako StreptABComplexMRP Duet
(Mousernabbit) kit (code No. K492; Dakopatts), described elsewhere.” Depending on the method routinely used by the study
groups, some cases were also stained with biotin-streptavidin-alkaline phosphatase,”’biotin-streptavidin-peroxidase?’or alkaline phosphatase and anti-alkaline phosphatase (APAAP) methods.”
RESULTS
ImmunoprecipitationAnalysis
Results of SDS-PAGE analysis of the CBF.78 antigen
performed with surface-’2SI-labeledlymphocytes is shown
in Fig 1. A protein of 1 I6 kD (nonreduced) was immunoprecipitated with the CBF.78 MoAb from freshly isolated PBMs
1
2
3
4
5
kDa
->
2743
LYMPHOMAS
-
205
-
116
-
97
-
66
and PHA-activated lymphoblasts. The CBF.78 antigen did
not shift on reduction (data not shown).
Flow Cytometric Analysis of Unstimulated and Stimulated
Peripheral Blood Lymphocytes With CBF.78 MoAb
Expression of CBF.78 antigen. The results obtained using double-staining with CBF.78 MoAb and MoAbs to Tcell markers on fresh and PHA- (data not shown) or antiCD3-stimulated PBMs are shown in Fig 2. A total of 95% of
resting T lymphocytes showed weak, but detectable, CBF.78
reactivity (Fig 2a) regardless of their CD4 or CD8 phenotype. Reactivity was markedly increased after stimulation of
cells for 3 days with PHA (data not shown) and an anti-CD3
MoAb (Fig 2b). The mean fluorescence values vaned from
60 fluorescent units (W) for fresh PBMs to 391 FU for 3day lymphoblasts. Unstimulated PBMs cultured for 3 days
in the absence of activating agents had only a mean fluorescence value of 96 W. The number of CBF.78 molecules
per cell was determined by reference to calibration beads
after autofluorescence subtraction. The number of CBF.78
molecules per cell increased from a mean value of approximately13,000 molecules/cell onfresh lymphocytes to approximately 43,000 molecules/cell on activated cells. Resting B lymphocytes labeled with the anti-B antibody CD191
Leu12 showed no reactivity of with CBF.78 MoAb (Fig 2c).
By contrast, EBV-transformed B-lymphoblastoid cellline
BON” was strongly positive for CBF.78 antibody (Fig 2d).
Similar results were obtained on immunostained cytospins
of eight EBV’ lymphoblastoid cell lines. All eight cell lines
were found to be strongly positive for CBF.78 (8+ of 8).
Flow cytometric analysis of the 16 lymphoma cell lines (Table l ) showed that all T-cell lymphoma cell lines (eg, Fig
2f) were strongly positive, which is in sharp contrast to the
negativity of the B-cell lines examined (eg, Fig 2e). Of the
two monocytic/histiocytic cell lines analyzed, only U937
was positive.
Effect of CBF.78 MoAb on T-cell proliferation. The addition of CBF.78 antibody (10 to 300 pUmL) to culture
medium showed no effect on the proliferation of anti-CD3induced T cells (data not shown).
Reactivity of CBF.78 With Normal Human Tissues
-
45
Fig 1. SDS-PAGE analysis of immunopurified CBF.78 antigen.
Freshly isolated lymphocytes (lanes l and 2). and day-3 PHA-activated lymphoblasts (lane 3-5) wereradioiodinated, lysed, and immunoprecipitated with the CBF.78 MoAb (lanes l and 41, rabbit IgGSepharose control (lanes 2 and 5). and the anti-CD100 MoAb BB18
(lane 3). Immunoprecipitates were analyzed on 7.5% SDS-polyacrylamide gels under nonreducing conditions and were autoradiographed. A protein of 116 kD (arrow) was immunoprecipitated with
the CBF.78 MoAb from freshly isolated PBMs and PHA-activated
lymphoblasts (lanes 1 and 4). The size of the CBF.78 antigen is in
marked contrast to the much higher molecular weight CD100 antigen
of 300 kD (lane 31.
The CBF.78 MoAb detected a few positive cells in the
paracortical areas of human tonsil and reactive lymph nodes
(Fig 3A). Some epithelioid histiocytes were also labeled. No
other cells in reactive lymph nodes were positive for this
antibody. In the thymus, most cortical thymocytes were
strongly positive, whereas only scattered positive cells could
be seen in the medulla (Fig 3B). CBF.78 MoAb wasnegative
with all the other human normal tissues examined, except
for occasional staining of Kupffer cells in the liver.
Reactivity of CBF.78 MoAb With Neoplastic Human
Tissues
The reactivities of CBF.78 antibody with hemolymphatic
tumors are shown in Table 2. Among malignantlymphomas,
the antigen recognized by CBF.78 MoAb was mainly expressed by T-cell lymphomas (49+ of 74; 66%), especially
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AL SAATI ET AL
2744
A distinctive pattern of reactivity of CBF.78 MoAb was
found in studying 108 cases of ALCLs. Strong positivity for
CBF.78 antibody was observed in 86+ of 108 (80%) cases
(Fig 3D), regardless of the phenotype of these lymphomas
and including those of null phenotype (Table 2).
CBF.78 MoAb was not reactive with the 48 nonlymphoid
tumors investigated on paraffin sections.
DISCUSSION
- Frbsh Lymphocytes I - EON C411
line
Fig 2. Flow cytometry analysis of CBF.78 MoAb expression on
PBMs and lymphoma cell lines. (a and b) Fresh PBMs were doublestained with theCD2 and CBF.78 MoAbs after 3
days of culture without (a) or with (b) anti-CD3 antibody. Gates for lymphocytes and
lymphoblasts were constructed from forward scatterlside
scatter
(FSCISSC)dot plot. UnstimulatedT lymphocytes are weakly positive
for CBF.78 MoAb (meanfluorescence, 96; a), whereas anti-CD3-activated lymphoblasts show increased reactivity (mean fluorescence,
391; b). (c and d) Fresh PBMs (cl and EBV-transformed B-cell line
(BON; d) were double-stained with the CD19 and CBF.78 MoAbs.
Resting B lymphocytes show no reactivity with CBF.78 MoAb (c),
whereas the BON lymphoblastoid cell line was strongly positive
lmean fluorescence, 97; d). (e and 11The DEAU B-lymphoma (e) and
the Jurkat T-lymphoma (f) cell lines were double-stained with the
CD19 or CD2 antibodies, respectively, and with CBF.78 MoAbs. Note
the strong positivity of the T-cell line positive (mean fluorescence,
132; f l which contrasts with the negativityof the B-cell line (e). The
abscissa is the green fluorescence from CBF.78 MoAb, whereas the
ordinate is the orange fluorescence from the anti-T ICD2) or anti-B
(CD19) antibodies. All dot plotsare given with quadrant markers, as
defined by cell autofluorescence, except for (a1 and (b) cellcultures,
in which quadrants are placed t o distinguish cells with enhanced
CBF.78 expression. The mean fluorescence values given in brackets
correspond t o double-positive cells.
those of high-grade malignancy (3I + of 36; 86%). Thenumber of positive cells varied from case to case, but, in most
cases, the staining was most intense on the cell membrane
(Fig 3C). Only a minority of B-cell lymphomas (4+ of 107;
4%) expressed this antigen. Occasional cases of HD ( I 3+
of 126; 10%) showed some Reed-Stemberg cells labeled
withCBF.78 MoAb. In the latter cases, the staining was
often weak and predominantly cytoplasmic.
The results of immunoprecipitation and cytoflurometric
analyses distinguish the antigen recognized by CBF.78
MoAb as being different from CDIOO. Indeed, contrary to
anti-CD100 MoAbs (BB 18, BD16, F93-7G2, and A8)?*
which detect an antigen of 300 kD (nonreduced)/l50 kD
(reduced), the CBF.78 MoAb detects a band of 116 kD
(nonreduced or reduced). The CBF.78 MoAb detects a leukocyte-associated antigen expressed predominantly by T
lymphocytes. Quantification of the expression of this membrane-associated antigen showed that it increased threefold
to fourfold on PHA- and anti-CD3-activated T cells and on
EBV-transformed B lymphocytes, as compared with that on
resting T lymphocytes. These findings suggest that CBF.78
MoAb reacts with an activation antigen expressed on both
T and B lymphocytes. However, the strong reactivity of
cortical thymocytes with CBF.78 MoAb is unusual, given
that these cells are negative for virtually all well-characterized activation antigens such as CD25, CD30, and CD70.”5-27
In addition, this antigen is expressed on a subpopulation of
T lymphocytes that is predominantly of small size in reactive
lymph node, which is in marked contrast to the large-sized
activated lymphocytes detected by CD30/Ber-H2 antibody.’x
Among malignant lymphoid tumors, theantigen recognized by CBF.78 MoAb is expressed preferentially by highgrade T-cell lymphomas. The reactivity of CBF.78 antibody
with B-cell neoplasms seems to be infrequent. Of note, the
results of flow cytometry analysis of T-or B-lymphoma cell
lines are in agreement with those obtained on paraffin sections. However, the main goal of the present study was to
assess the reactivity of CBF.78 antibody with ALCLs, because these tumors are known to express several activation
antigen^?^".'^ Interestingly, the results of the multicenter
study clearly showed that this antibody was strongly positive
with the majority (80%) of ALCLs, whatever their phenotype. The reactivity of tumors showing a null phenotype
might suggest that most of these tumors are derived from
T lymphocytes. Alternatively, because CBF.78 antigen is
inducible by stimulation of lymphocytes byPHA or antiCD3 or by EBV infection, its expression by ALCLs could
just emphasize that these tumors do originate from activated
As mentioned above, a problem in diagnostic histopathology, expected to arise in approximately 10% of cases
in a large series such as ours, is the distinction of some cases
of neoplastic cell-rich HDfrom Hodgkin’s-like ALCLS.~
CBF.78 MoAb appeared to be of value in making this distinction. As found in this study, ALCLs, more often than
not,showedCD30’
and CBF.78’ phenotype. Conversely,
we found the antigen detected by CBF.78 MoAb to be expressed rarely byReed-Stemberg cells in HD. Thus, CBF.78
antigen together with the expression of CD1 5 , EMA, and H
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ANAPLASTIC WITH
MoAb REACTIVE
2745
Fig 3. The CBF.78 MoAb was
used t o immunostain tissuesections of a reactive lymph node
(AI, a thymus(B), a case of T-cell
lymphoblastic
lymphoma
(C),
and a case of ALCL (Dl. Only a
few positive cells can be seen in
the paracortical area of the reactive lymph node (A). Cortical
thymocytes are stronglypositive
with CBF.78 MoAb, whereas
only scattered positive cells can
be seen in the medulla(B). Note
the intense membrane labeling
of virtually allneoplastic cells of
the T-cell lymphoma (C) and
ALCL (D) with CBF.78 MoAb.
Note the negativity of the polynuclear cell in the blood vessel
(arrow; C). lmmunoperoxidase
technique with nuclear counterstaining: original magnification,
x125 (A and B); x800 (C); and
x1.000 (Dl.
and Y blood group antigens recognized by BNH.9 antibody
couldfurther assist in the distinctionofHodgkin's-like
ALCL (CD30'. CD15', EMA', BNH.9', and CBF.78')
from neoplasticcell-rich
HD (CD30', CD15'. EMA-,
BNH.9-, and CBF.78-).29"3
In summary,CBF.78MoAbdetects
a 116-kDantigen
predominantly expressed on a subpopulation of lymph node
T lymphocytes. The increased expression on stimulated T
cells and on EBV-transformed B lymphocytes suggests that
CBF.78 MoAb reacts with an activation antigen
expressed
on both T and B lymphocytes. CBF.78 antibody is suitable
for use on routinely processed paraffin sections and should
be of value in the diagnosis of T-cell lymphoma and in the
differential diagnosisofALCLsfrom
neoplasticcell-rich
HD. However, the function of this new antigen and its clinical utility require further investigation.
ACKNOWLEDGMENT
We thank Prof S.M. Chittal (Memorial University, St John's, NF.
Canada) for critically reading the manuscript and Drs R. Rimokh,
Rec-l,
C.Bastard, and N.L. Berinsteinforkindlyprovidingthe
also grateful
VAL, and OCI LY8 C3 lymphoma cell lines. We are
to the staff of the Pathological Anatomy Laboratory,
in particular
to J. Boyes and M. March. All of the cases from the University of
Arizona, including the anaplastic, the HD, and the large cell cases
are from the Southwest Oncology Group Central Repository (Grant
No. CA 32102). The excellent technical assistance by M. Durand
and Ch. Perez is gratefully acknowledged.
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From www.bloodjournal.org by guest on June 14, 2017. For personal use only.
1995 86: 2741-2746
A novel antigen detected by the CBF.78 antibody further
distinguishes anaplastic large cell lymphoma from Hodgkin's disease
T al Saati, J Tkaczuk, G Krissansen, C Print, S Pileri, E Ralfkiaer, TM Grogan, F Meggetto and G
Delsol
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