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 Previous Article | Table of Contents | Next Article 
Blood, Vol. 94 No. 8 (October 15), 1999:
pp. 2895-2900
ABO Blood Group Antigens on Human Plasma von Willebrand Factor After
ABO-Mismatched Bone Marrow Transplantation
By
Taei Matsui,
Taketo Shimoyama,
Masanori Matsumoto,
Yoshihiro Fujimura,
Yoshinobu Takemoto,
Masahiro Sako,
Jiharu Hamako, and
Koiti Titani
From the Division of Biomedical Polymer Science, Institute for
Comprehensive Medical Science, Fujita Health University; Department of
Medical Information Technology, Fujita Health University College,
Toyoake, Aichi, Japan; Department of Blood Transfusion Medicine, Nara
Medical University, Kashihara, Nara, Japan; 2nd Department of Internal
Medicine, Hyogo College of Medicine, Nishinomiya, Hyogo, Japan; and the
Department of Pediatrics, Osaka City General Hospital, Miyakojima-ku,
Osaka, Japan.
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ABSTRACT |
von Willebrand factor (vWF) is synthesized exclusively by
endothelial cells and megakaryocytes, and stored in the intracellular granules or constitutively secreted into plasma. ABO blood group antigens are covalently associated with asparagine-linked sugar chains
of plasma vWF. The effect of ABO-mismatched bone marrow transplantation
(BMT) or blood stem cell transplantation (BSCT) on the expression of
ABO blood group antigens on the vWF was examined to obtain information
on the origin of these antigens. In ABO-mismatched (HLA-matched)
groups, 8 cases of BMT and 4 cases of BSCT were examined. In all cases,
the ABO blood groups on red blood cells were gradually converted to the
donor's type within 80 to 90 days after the transplantation. The blood
group antigens on the vWF were consistent with the recipient's blood
group for the period monitored by enzyme-linked immunosorbent assay
(ELISA). When vWF was isolated from normal platelets and examined for
the blood group antigens using ELISA or immunoblotting, it showed few
antigens. However, vWF extracted from veins expressed blood group
antigens. These findings indicate that platelet (megakaryocyte)-derived vWF does not contain blood group antigens and that these antigens may
be specifically associated with vWF synthesized in endothelial cells
and secreted into plasma. Furthermore, it is possible that the
persistence of the recipient's blood group antigens on plasma glycoproteins such as vWF, independent of the donor-derived
erythrocytes, after ABO-mismatched stem cell transplantation, may
influence the immunological system in the production of anti-blood
group antibodies resulting in the establishment of immunological
tolerance in the recipient plasma.
© 1999 by The American Society of Hematology.
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INTRODUCTION |
VON WILLEBRAND FACTOR (vWF) is a
multimeric large-plasma glycoprotein that plays a key role in the
initial step of hemostasis and is also a carrier of blood coagulation
factor VIII (FVIII).1-3 vWF mediates the adhesion of
platelets to the sites of vascular damage under high-shear stress
resulting in thrombotic platelet plug formation. vWF is specifically
synthesized in endothelial cells and megakaryocytes. vWF is
constitutively secreted from endothelial cells into circulating plasma
and subendothelial matrices or stored in endothelial Weibel-Palade
bodies and platelet  granules.4-6
Human plasma vWF has ABO blood group antigens on the asparagine-linked
sugar chains.7,8 It is quite unique because only limited
human plasma glycoproteins (vWF, FVIII, and a part of 2-macroglobulin) covalently link these
antigens.9,10 The physiological function of these antigens
on plasma vWF is not clear. However, the concentration of vWF has been
known to be influenced by these blood groups and is significantly lower
in persons with blood group O.11-15 In addition, Shima et
al16 recently reported that the concentration of plasma vWF
is affected by the presence of the O gene, namely, the vWF from
homotypic genotype donors (AA and BB) showed a higher concentration
than those from the heterotypic genotype donors (AO and BO). There are
no significant differences among the blood groups in the amount of vWF
within cells,17 the specific activity, or the multimeric
pattern of plasma vWF.16 These results suggest the
structure and the amount of blood group sugar chains on vWF molecule,
such as the terminal sialic acids,18 may determine the
circulating life span of vWF.
Bone marrow transplantation (BMT) or blood stem cell transplantation
(BSCT) is an established medical treatment for patients with aplastic
anemia, acute leukemia, and immunodeficiency diseases. Because ABO
blood group antigens are independent of HLA gene complex, HLA-matched
donors may be ABO-incompatible.19-21 In such cases, the
blood group antigen of the recipient on red blood cells gradually turns
to the donor's type, but there is little information about the changes
in plasma components containing blood group antigens. In the present
study, we examined the blood group antigens on plasma vWF after
ABO-mismatched BMT and BSCT, and the origin of the vWF with blood group antigens.
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MATERIALS AND METHODS |
Materials.
Plasma samples were collected from normal adults, and from donors and
recipients of ABO-matched (three cases) or mismatched BMT (four cases
of minor, three cases of major, and one case of major-minor mismatched,
but HLA-matched) at intervals before and after transplantation, and
stored at  80°C after addition of 1/50 volume to each of a
protease-inhibitor mixture (final 4 mmol/L EDTA, 4 mmol/L
N-ethylmaleimide, 4 mmol/L benzamidine, 400 kallikrein inhibitor units/mL of aprotinin). Three cases of allogeneic peripheral blood and one case of cord blood stem cell transplantation were also
examined. Standard vWF was purified from FVIII concentrates as
described previously.22
Enzyme-linked immunosorbent assay (ELISA).
ELISA plate (Immuno module; Nunc Intermed, Kamstrup, Denmark) was
coated with 50 or 100 µL (in each well) of anti-vWF goat immunoglobulin G (IgG) (20 µg/mL; Medical and Biological Laboratory (MBL), Nagoya, Japan) in 100 mmol/L bicarbonate buffer, pH 9.6 overnight at 4°C, and blocked with 200 µL of Tris-buffered saline (TBS; 10 mmol/L Tris-HCl, pH 7.5, 150 mmol/L NaCl) containing 1%
bovine serum albumin (BSA) overnight at 4°C. The coated plate was
used within 3 weeks after preparation and washed twice with 200 µL of
TBS containing 0.05% tween 20 (TwTBS) before use. Plasma samples were
appropriately diluted (10 to 100-fold with TwTBS) and 50 or 100 µL of
each was applied to the anti-vWF coated plate and incubated for 90 minutes at room temperature. The plate was washed five times with 200 µL of TwTBS and incubated with either 50 or 100 µL of anti-A,
anti-B monoclonal antibody (MoAb) (Ortho Diagnostics Systems, Raritan,
NJ) diluted with TwTBS (10-fold for anti-A, fivefold for anti-B),
biotin-conjugated UEA-I lectin (5 µg/mL, EY Laboratories, San Mateo,
CA) that recognizes the type-2 H structure rich in blood group O, or
horseradish peroxidase (HRP)-conjugated anti-vWF rabbit IgG (1/1,000
diluted with TwTBS; Dakopatts, Glostrup, Denmark) for 60 minutes. After
washing with TwTBS, the plate treated with anti-A, anti-B, and UEA-I
was incubated with HRP-conjugated anti mouse IgM (1/1,000 diluted with
TwTBS, Zymed Laboratories, San Francisco, CA), anti mouse IgM (1/1,000) plus anti mouse IgG (1/1,000; TAGO Immunologicals, Camarillo, CA) and
streptavidin (1/1,000, Vector Laboratories, Burlingame, CA) for 45 minutes, respectively. Peroxidase reaction was performed with 100 µL
of solution containing 100 mmol/L NaCl, 0.5 mg/mL o-phenylenediamine, 0.02% H2O2, and 50 mmol/L Tris-HCl, pH 7.5, for 30 to 60 minutes at room temperature in
the dark. The absorbance at 490 nm was measured with a plate reader
after the addition of 100 µL of 8 mol/L
H2SO4. vWF concentration was measured by ELISA
using the control plasma N (Dade Behring, Marburg, Germany) and
expressed as U/dL. Protein concentration was determined by bicinchoninic acid protein assay kit (Pierce, Rockford, IL) using BSA
as a standard.
vWF from platelets.
Platelets (three samples each for A and B) were prepared from
platelet-rich plasma by centrifugation (2,800 rpm, 10 minutes at
25°C), washed with phosphate-buffered saline (PBS; 150 mmol/L NaCl,
10 mmol/L Na-phosphate, pH 7.2) containing 9 mmol/L EDTA and 15%
acid-citrate-dextrose (ACD) and twice with 150 mmol/L NaCl containing
10 mmol/L HEPES buffer, pH 7.5, and stored at 80°C until use.
Platelets were suspended in five volumes of TwTBS containing protease
inhibitors as described above and disrupted by sonication at 0°C with
a Branson Sonifier 250 (Danbury, CT). After centrifugation at 15,000 rpm at 4°C for 45 minutes, the supernatant was used for ELISA as
described above.
In a separate experiment, the soluble fraction of platelets and plasma
from normal adults with blood group A or B (200 µL each) were mixed
with 20 µL of anti-vWF goat IgG (15 mg/mL, MBL), respectively, for 3 days at 4°C. The immunoprecipitates were collected by centrifugation
(15,000 rpm, 100 minutes at 4°C) and washed with TBS.
Aliquots of the washed immunoprecipitates were resolved with 25 µL of
sodium dodecyl sulfate (SDS) buffer (2% SDS, 25% glycerol, 62.5 mmol/L Tris-HCl, pH 6.5) containing 5% 2-mercaptoethanol at 95°C,
subjected to SDS-polyacrylamide gel electrophoresis
(PAGE)23 and transferred to a polyvinylidene difluoride
(PVDF) membrane as described.24 The membrane was incubated
with TwTBS containing anti-A (1/10 diluted), anti-B (1/5 diluted) MoAb,
or HRP-conjugated anti-vWF antibody (1/1,000 diluted) for 90 minutes at
room temperature. After washing with TwTBS, HRP-conjugated second
antibodies were used for detection of anti-A and -B binding, as
described above. HRP reaction was performed using 0.2 mg/mL of
diaminobenzidine and 0.05% H2O2 as a substrate.
vWF from vein.
Small pieces of renal vein from postmortem individuals with type A (two
samples) and O (one sample), obtained with informed consent, were
carefully cleaned and canurated with PBS before freezing. The frozen
veins (0.2 g, wet weight) were cut into small pieces on ice, suspended
in 1 mL of TwTBS containing 10 mmol/L EDTA and protease inhibitors, and
disrupted by sonication at 0°C. After centrifugation (15,000 rpm, 2 hours at 4°C), the supernatant was used for ELISA. The concentration
of fibrinogen, transferrin, 2-macroglobulin and vWF in
the vein extracts and normal plasma were measured by sandwich ELISA
using the corresponding HRP-conjugated antibodies (MBL, Dakopatts).
Other methods.
The blood group of the red blood cells and the anti-blood group
antibodies was determined by conventional hemagglutination assay using
anti-A and -B MoAbs and standard human type A1 and B red blood cells
(Ortho Diagnostics) according to the manufacturer's instructions.
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RESULTS |
ABO blood group antigens on red blood cells.
ABO blood group antigens on the surface of red blood cells and the
anti-blood group antibodies in the plasma of the recipient with acute
lymphocytic leukemia in first relapse (blood group AB, male, 36 years
old), who was transplanted from a sibling donor (blood group O, female,
35 years old), were monitored for 161 days at intervals before and
after BMT (Fig 1A) (the recipient experienced complete remission, but
relapsed 7 months after transplantation and died of fungal infection
even though a second BMT was performed). The recipient's red blood
cells with type AB showed a mixed field with anti-A and -B antibodies 1 week after transplantation, but had completely lost their reactivity to
the antibodies after 90 days indicating that the blood group of the
recipient was gradually converted to the donor's type by
ABO-mismatched BMT. The anti-blood group antibodies assayed by standard
red blood cells (type A1 and B) showed that there was no production of
either of these antibodies for the duration of the monitoring period
(130 days after transplantation) (Fig 1A).
In all cases of ABO-mismatched BMT examined, the antibodies against the
recipient's original blood group were not found in the plasma (Table
1).
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| Fig 1.
Blood group antigens on plasma vWF after ABO minor
mismatched BMT. (A) The recipient (patient M.N.; type AB) who suffered
from acute lymphocytic leukemia was transplanted with bone marrow from
an HLA-matched but ABO minor mismatched donor (sister; type O). Plasma
and red blood cells (RBC) were serially collected from the recipient.
The reactivity of RBC against anti-A and -B antibodies was expressed as
positive (+), negative () or mixed field (±) observations. The
anti-blood group antibody production was expressed as titers. Each
plasma sample was diluted to 1:20 with TwTBS and vWF in plasma was
measured by ELISA using anti-vWF antibody and the concentration of vWF
( ), the binding of anti-A ( ), anti-B MoAbs ( ) and UEA-I ( )
were monitored. Data express the average of three measurements. Arrow
indicates reactivities of the donor. (B) HLA-matched and ABO minor
mismatched BMT between patient K.Y. with type A who suffered from
severe aplastic anemia at the second remission and the donor with type
O (father). Concentration of vWF () and the blood group A antigen
() on vWF in 1:80 diluted plasma were monitored. RBC showed the
mixed field to anti-A from 14 days after transplantation.
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Table 1.
ABO Blood Group Antigens on Plasma vWF and Red Blood
Cells (RBC) of the Recipients after ABO-Matched and Mismatched BMT
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ABO blood group antigens on plasma vWF.
vWF in plasma was monitored using ELISA. Concentration of the vWF in
the patients receiving a BMT was significantly higher (204 ± 42
U/dL, n = 6, P < .001) when compared with the average concentration in normal adults (91 ± 22 U/dL, n = 9) regardless of ABO-matched or mismatched BMT (Table 1). Plasma vWF, especially, was
transiently increased after transplantation and gradually decreased as
reported25,26 (Fig 1A and 1B). The level of ABO blood group
antigens on the vWF also varied with the concentration of vWF, but it
never converted to the donor's type after ABO-mismatched BMT (Fig 1A
and 1B). UEA-I lectin reacts with vWF from blood group O because it has
more H-substance than the other groups.9 Reactivity of the
recipient's plasma vWF against UEA-I was less than that of the
donor's vWF except for a short period after BMT (Fig 1A).
In the case of major mismatched BMT from a type A donor to a type O
recipient (Fig 2), plasma vWF of the
recipient at 7 months after transplantation still showed UEA-I binding
activity similar to the level before transplantation. No reactivity was
shown to anti-A antibody, indicating neither a significant reduction of the vWF with blood group O, nor the production of vWF with blood group
A antigen.
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| Fig 2.
Blood group antigens on plasma vWF after ABO major
mismatched BMT. The reactivities of the recipient's plasma vWF before
and after (7 months) major mismatched BMT (patient S.Y. with type O and
the donor with type A) against UEA-I (white) and anti-A MoAb (black)
were measured using ELISA and normalized as the reactivity
(A490) of 6 U/dL (1 µg/mL) of vWF solution. The
reactivities of plasma vWF from normal subjects with blood group O and
A against UEA-I and anti-A antibody were also measured as a control.
Data express the means ± SE (n = 3) for a patient and the means ± SD (n = 6) for a control.
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In the eight cases of ABO-mismatched BMT examined, there was no change
in the blood group of plasma vWF (Table 1). Examination 3 years, 9 months after transplantation showed that the vWF still continued to
express the recipient's blood group antigens but not the donor's type.
In addition to bone marrow, BSCT was also examined. Three cases of
allogeneic peripheral and one case of cord ABO-mismatched BSCT showed
the same results as BMT (Table 2). Plasma
vWF expressed the original blood groups in contrast to red blood cells,
which were converted to express the donor's type.
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Table 2.
Blood Group Antigens on Plasma vWF and RBC of the
Recipients after ABO-Mismatched Allogeneic-Peripheral Blood Stem Cell
(PBSCT) and Cord Blood Stem Cell Transplantation (CBT)
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Blood group antigens on vWF from platelets and vein.
To elucidate the origin of blood group antigens on plasma vWF, we
examined vWF extracted from both platelets and the renal vein. vWF
immunoprecipitated from platelets and plasma both showed the 270 kD
subunit band with some minor degraded bands by immunoblotting with
anti-vWF antibody (Fig 3). Plasma vWF
showed the corresponding blood group, whereas platelet vWF had no or
only a faint blood group antigenicity. The latter showed two bands at
about 110 and 130 kD that were reactive to the corresponding anti-blood
group antibody, but did not react with anti-vWF antibody. Also using ELISA, platelet vWF showed no significant binding to the anti-blood group antibody (Fig 4).
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| Fig 3.
Blood group antigens on vWF from plasma and platelets.
vWF was immunoprecipitated from plasma (Pls) and the platelets (Plt)
extracts from normal subjects with blood groups A and B. Aliquots of
each immunoprecipitates and the standard vWF (vWF, 0.5 µg) were
solubilized in SDS-buffer and subjected to SDS-PAGE under reducing
conditions. Proteins were transferred to a PVDF membrane followed by
immunoblotting with anti-vWF antibody, anti-A and B MoAbs. vWF showed
the subunit band at about 270 kD. Blood group antigens were detected on
the vWF band including minor degraded band at about 140 kD prepared
from plasma and the purified vWF. vWF from platelets showed no or a
very faint reactivity against blood group antibody, but platelets
contained smaller bands at about 110 and 130 kD that weakly reacted
with anti-blood group antibodies but not with anti-vWF antibody.
Numbers on the left indicate the positions of molecular mass standard
(kDa). The same results were obtained when using the other two platelet
specimens from blood groups A and B.
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| Fig 4.
Blood group antigens on vWF extracted from renal veins
and platelets. vWFs in the normal plasma (Pls) and in the extracts of
veins and platelets (Plt) from the subjects with type A were captured
with anti-vWF antibody on an ELISA plate. The concentration of vWF and
the reactivity against anti-A MoAb was measured and normalized as the
anti-A reactivity (A490) of 6 U/dL (1 µg/mL) of vWF
solution. Each value indicates means ± SD (n = 3 except for type
A vein, n = 2).
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vWF in the renal vein extracts was examined using ELISA. Among the
samples from two subjects with type A and one subject with type O, vWF
from the type A subjects clearly showed blood group A antigenicity,
although the reactivity was about half that of plasma vWF from normal
blood type A subjects (Fig 4). Vein vWF from the type O subject showed
only UEA-I reactivity (data not shown). To address the question of
whether vWF in the vein extracts used was mostly derived from
contaminated plasma, we measured the contents of several plasma
proteins in the extracts and compared them with those in normal plasma.
Fibrinogen, transferrin, and 2-macroglobulin in the vein
extracts used were estimated to be 0.4 ± 0.1, 0.4 ± 0.1, and 0.6 ± 0.3 U/dL, respectively (n = 3), whereas the vWF in the extracts
was 12.2 ± 2.2 U/dL. These findings suggest that the vein extracts
contained a greater amount of vWF compared with other plasma proteins
and that vWF derived from plasma appeared to be less than 1%.
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DISCUSSION |
HLA-matched but ABO-mismatched BMT has no influence on marrow
engraftment, graft rejection, and graft-versus-host disease if
appropriate care, such as plasma exchange and antibody absorption, is
performed to avoid acute hemolysis.19-21 However, delayed
hemolysis, retarded growth of erythroblast, or undergrown erythrocytes
have often been observed as complications.27-29 Production
of anti-blood group antibody must be controlled by the remaining host
antigens and the donor-derived lymphocytes. It has been reported that
blood group antigens are covalently linked to vWF, FVIII, and
2-macroglobulin in plasma.7-10 In the
present study, the blood group antigens on erythrocytes gradually
converted to the donor's type, but the blood group on plasma vWF did
not change after ABO-incompatible BMT (and BSCT). No antiblood group
antibody against the recipient's original blood group was detected
after the transplantation. Wernet and Mayer30 reported that
isoagglutinins against the recipient's original red blood cell type
are produced only during the early days after transplantation even
though the patient has converted to the donor's red blood cell type
after ABO-mismatched BMT. Although it is probable that the
immunosuppressing treatment might interfere with the production of
antibodies in the recipient, the observed pattern of antibody
production (Table 1) suggests that the remaining blood group antigens
on plasma glycoproteins such as vWF might contribute to the
establishment of immunological tolerance.
The finding that plasma vWF continued to express the recipient's blood
group after ABO-mismatched BMT suggested two possibilities for the
origin of these antigens on the vWF. One was that vWF produced in
megakaryocytes, differentiated from bone marrow stem cells, would not
be secreted but stored in platelets. The other was that vWF in
platelets originally had no blood group antigens. Almost all plasma vWF
has been shown to be supplied from endothelial cells rather than
platelets by crossed BMT of pigs,31 suggesting that the
secretion of vWF from platelets is limited to the local area at
thrombosis. Platelets have been known to have both covalently and
noncovalently bound blood group antigens.32,33 Recently, the covalently bound antigens have been found in platelet membrane glycoproteins (GP) such as GPIa, Ib, IIa, IIb, IIIa,34,35
IV, and V,36 suggesting that platelets (megakaryocytes)
have a machinery to assemble the blood group antigens. We have prepared
platelet vWF, but it has no or only a faint blood group antigenicity.
The 110 and 130 kD proteins observed in the immunoprecipitated platelet vWF (Fig 3) seem to be GPs coprecipitated with vWF. The absence of
blood group antigens in platelet vWF has also been recently reported by
two groups.37,38 The very faint blood group reactivity observed in the platelet vWF (Fig 3 and 4) might be a contamination from the plasma vWF adsorbed onto the platelets.
Another vWF producing site is endothelial cells. We found that the
renal vein extracts contained vWF with blood group antigens. Expression
of the blood group antigens by the vWF molecule was about half that of
the plasma vWF, suggesting that vWF molecules with no or a small amount
of blood group antigens also exist. It is possible that these vWFs are
incompletely glycosylated. Alternatively, the glycosylation may be
different between vWF that is constitutively secreted and that stored
in the regulated Weibel-Palade body pathway. Recently, Yamamoto et
al39 reported that the synthesis of vWF in endothelial
cells varied among the organs in mice. Glycosylation is regulated by
glycosyltransferases and trimming glycosidases in cells, suggesting
that the blood group antigen production might also be altered by each
organ. When we analyzed vWF extracted from cultured human umbilical
vein endothelial cells, no significant blood group antigens were
observed and neonatal plasma vWF showed a lower expression of these
antigens (Matsui, unpublished observations), suggesting that the blood group antigens on plasma glycoproteins may also be developmentally regulated like embryonic antigens.40
Our present findings, together with the recent findings of Brown et
al37 showing that plasma vWF with blood group antigens was
rapidly increased after administration of DDAVP to a type 1 von
Willebrand disease patient, strongly suggest that vWF with blood group
antigens is specifically glycosylated in endothelial cells but not in
megakaryocytes. It is also possible that the blood group antigens are
attached to vWF extracellularly by plasma glycosyltransferases after
secretion. A or B transferases are still present in plasma in
accordance with the recipient's type even after ABO-mismatched
BMT.41 However, transplanted O-type erythrocytes to type-A
recipients did not show A antigens even though the plasma contained
A-type vWF (Table 1) and A transferase (Sako, unpublished observation).
Furthermore, it is not likely that the plasma contains enough sugar
nucleotide donors such as UDP-N-acetylgalactosamine and UDP-galactose
for A and B transferase, respectively.
Although the biological function of the blood group antigens on vWF is
still not clear, the different glycosylation between platelet and
endothelial vWF might influence the function of each pool of vWF in
hemostasis or in its association with FVIII. Recently, Sarode et
al38 reported that the blood group sugar chains on vWF
influenced the ristocetin-induced platelet agglutinating activity. Further studies on the relationships between thrombotic complications followed by ABO-mismatched BMT or BSCT and the presence of blood group
antigens on vWF may contribute to more successful transplantation.
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ACKNOWLEDGMENT |
We thank S. Nishida and S. Ishihara for their technical assistance. We
also thank Dr D. Mrozek for editing the manuscript.
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FOOTNOTES |
Submitted December 29, 1998; accepted May 25, 1999.
Supported in part by Grants-in-Aid for Scientific Research from the
Japanese Ministry of Education, Science, Sports, and Culture (to T.M.
and K.T.) and Fujita Health University (to K.T. and J.H.).
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.
Address correspondence to Taei Matsui, PhD, Division of Biomedical
Polymer Science, Institute for Comprehensive Medical Science, Fujita
Health University, Toyoake, Aichi 470-1192, Japan; e-mail: tmatsui{at}fujita-hu.ac.jp.
| |
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