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Molecular and Cellular Biology, May 2000, p. 3097-3101, Vol. 20, No. 9
Laboratory of Cell Biology, Lindsley F. Kimball Research Institute, New York Blood Center, New York, New York
Received 18 January 2000/Accepted 31 January 2000
All of the antigenic determinants of the Duffy blood group system
are in a glycoprotein (gp-Fy), which is encoded by a single-copy gene
(FY) located on chromosome 1. gp-Fy is also produced in
several cell types, including endothelial cells of capillary and
postcapillary venules, the epithelial cell of kidney collecting ducts,
lung alveoli, and the Purkinje cells of the cerebellum. This protein, which spans the cell membrane seven times, is a member of the superfamily of chemokine receptors and a malarial parasite receptor. The mouse Duffy gene (Dfy) homolog of human FY
is also a single-copy gene, which maps in a region of conserved synteny
with FY and produces a glycoprotein with 60% homology to
the human protein. The mouse Duffy-like protein also binds chemokines.
To study the biological role of gp-Fy, we generated a mouse strain in
which Dfy was deleted. These homozygous
Dfy The product of FY, a
single-copy gene located on the 1q22 gp-Fy is produced in several cell types including the endothelial cells
of capillary and postcapillary venules, the epithelial cells of kidney
collecting ducts, and lung alveoli. It is also synthesized in the
Purkinje cells of the cerebellum (3, 8, 10). The Duffy
protein is also a member of the superfamily of chemokine receptors
(5, 9, 18).
We have identified the mouse Dfy orthologous to the human
FY (11). Dfy is similar to
FY in that it is a single-copy gene; it maps in a region of
conserved synteny with FY, and it consists of a small exon,
a large exon, and a single intron (11). It has been shown
that mouse erythrocytes bind human and murine chemokines (27). As with the human erythrocytes, C-C and C-X-C
chemokines appear to compete for binding with a single site on the
surface of the mouse red cells (27). We recently
demonstrated that the mouse Duffy-like protein possesses the same
chemokine binding characteristics as the human gp-Fy (11).
To determine the biological role of gp-Fy, we generated a mouse strain
that lacks Dfy. We made a comprehensive examination of the
Dfy Targeting vector and constructs.
The replacement-targeting
vector was constructed using a 9.5-kb Dfy genomic DNA clone
isolated from a mouse (129/Svj strain) genomic library (Stratagene).
The 5' untranslated region, exon 1, exon 2, and intron of
Dfy were deleted and replaced with the neomycin resistance
gene (neo). The 5' short arm of 1.5 kb, a 1.1-kb
neo cassette with the poly(A)+ signal from
pMC1neo Poly A vector (Stratagene), and a 3' long arm of 5.5 kb was
subcloned into PCR-Script SK(+) vector (Stratagene) (Fig.
1A).
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Deletion of the Murine Duffy Gene (Dfy)
Reveals that the Duffy Receptor Is Functionally Redundant
ABSTRACT
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Abstract
Introduction
Materials and Methods
Results and Discussion
References
/ mice were indistinguishable in size,
development, and health from wild-type and heterozygous littermates. We
also examined components of the immune system and found no differences
in lymph nodes or peripheral blood leukocyte levels between knockout
and wild-type mice. The gross and histological anatomy of the thymus, spleen, lung, and brain showed no significant differences between mutants and wild-type mice. There was no indication of an overall difference between the knockout and wild-type mice in systematic neurological examinations. The only significant difference between Dfy/ and Dfy+/+
mice that we found was in neutrophil migration in peritoneal inflammations induced by lipopolysaccharide and thioglycolate. In mice
homozygous for the deletion, there was less neutrophil recruitment into
the peritoneal cavity and neutrophil influx in the intestines and lungs
than in wild-type mice. Despite this, the susceptibility to
Staphylococcus aureus infection was the same in the absence
and in the presence of gp-Fy. Our results indicate that gp-Fy is
functionally a redundant protein that may participate in the neutrophil
migratory process.
INTRODUCTION
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Abstract
Introduction
Materials and Methods
Results and Discussion
References
q23 region of chromosome 1, is
an acidic glycoprotein which spans the plasma membrane seven times and
has an exocellular N-terminal domain and an endocellular C-terminal
domain (4, 21). gp-Fy carries all antigenic determinants of
the Duffy blood group system, which consists of four alleles, five
phenotypes, and five antigens (22). Duffy-negative
individuals, predominantly African and American blacks, lack the Duffy
protein on erythrocytes and are resistant to human malarial parasite
Plasmodium vivax and simian malarial parasite
Plasmodium knowlesi infection (14, 15). They are
healthy individuals who carry a mutation in the promoter region of
FY that disrupts the binding site for h-GATA-1 erythroid transcription factor and abolishes expression of FY in
erythroid but not nonerythroid cells (29).
/ mice including gross anatomy,
histology, hematology, and neurobiology. In addition, we studied the
response of the knockout mice to Staphylococcus aureus
infection and to aseptic inflammations induced by lipopolysaccharide (LPS), thioglycolate, and zymosan. The absence of Duffy-like protein did not produce an obvious phenotype with the exception of much less
neutrophil trafficking upon LPS or thioglycolate treatment.
MATERIALS AND METHODS
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Abstract
Introduction
Materials and Methods
Results and Discussion
References
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FIG. 1.
Targeting of the Dfy gene. (A) At the top is
the restriction map of the wild-type gene. A 2.2-kb fragment containing
the 5' untranslated region, exon 1 (E1), intron, and exon 2 (E2) was
removed by XbaI and HincII digestion. A 1.5-kb
5'-end fragment, the neo gene, and a 5.5-kb 3'-end fragment
were inserted into the XbaI-HincII deleted region
of the PCR-Script vector. (B) Genomic DNA was isolated from tail snips
of the offspring of interbreeding mice, digested with SacI,
and analyzed by Southern blot hybridization with the probe indicated in
panel A. Genotypes of mice are indicated as wild type (+/+),
heterozygous (+/ 
), and homozygous (/). (C) RNA blot analysis of
spleen and brain mRNAs from wild-type and deleted mice. (D) FACS
analysis of erythrocytes. For each condition, 30,000 red cells were
analyzed on a FACSCalibur flow cytometer (Becton Dickinson).
Generation of Dfy/ mice.
The
linearized targeting vector DNA (40 µg) was transfected by
electroporation into E14-1 embryonic stem (ES) cells (kindly provided
by J. Visser) as previously described (25). DNA isolated from ES colonies resistant to neomycin was amplified by PCR using primer 1 (5'-ATACCATGCATTCGCCACCTTTCC-3'), designed from a
sequence situated at the 5' end outside the replacement vector, and
primer 2 (5'-GCCTTCTTGACGAGTTCTTCTGAG-3'), designed from a
sequence situated at the 3' end of the neo gene (Fig. 1A).
Chimeric mice (129/SvJ-derived ES cells in blastocysts of C57BL/6J
mice) were generated as described elsewhere (20).
Heterozygous (Dfy+/) mice were used for
interbreeding to produce homozygous knockout (Dfy/) wild-type and
(Dfy+/+) mice. The experiments were performed
with 2- to 3-month-old mice weighing an average of 23 g.
Southern and Northern analyses. DNA and RNA extractions as well as Southern and Northern blot procedures were performed as explained elsewhere (11).
Necropsy studies. Gross and histopathological analyses were performed at the Research Animal Diagnostic Laboratory, Cornell University Medical College.
Behavioral evaluation of Dfy/ mice.
Dfy+/+ and Dfy/
animals were examined for appearance, posture, circadian activity, open
field activity, home cage assessment, water maze, rotating rod task
performance, balance, and reaching task performance. These behavioral
tests were carried out by Neuro-Detective Inc. (University of
Lethbridge, Lethbridge, Alberta, Canada).
Flow cytometry.
A Dfy-specific rabbit polyclonal
antibody (M4) against the amino-terminal domain of the mouse gp-Fy
(kindly provided by J. Hesselgesser) was used for protein
detection in mouse erythrocytes by fluorescence-activated cell sorting
(FACS) analysis. Aliquots of 10 µl of peripheral blood from
Dfy+/+ and Dfy/ mice
were incubated with rabbit antibody M4 at room temperature for 1 h
and then incubated with fluorescein isothiocyanate-conjugated donkey
anti-rabbit immunoglobulin G (Jackson ImmunoResearch Laboratories) for
another hour at room temperature.
Aseptic infections.
Aseptic peritonitis was produced with
LPS (Escherichia coli, serotype O111:B4, Sigma),
thioglycolate (BBL), and zymosan (Sigma) as explained elsewhere
(1, 12). Briefly, Dfy+/+ and
Dfy/ animals were injected intraperitoneally
with 1 ml of phosphate-buffered sterile saline (PBS) solution
containing either 200 µg of LPS or 4 mg of zymosan per 20 g of
animal body weight. The thioglycolate peritonitis was induced with the
intraperitoneal injection of 1 ml of a 3% thioglycolate solution.
Control animals were injected with 1 ml of PBS solution. The mice were
euthanized by CO2 narcosis 24 h after injection, and
the peritoneal cavities were washed with 5 ml of PBS solution
containing 3 mM EDTA and 0.1% bovine serum albumin. At the same time,
blood samples were obtained by heart puncture. Cell counts were
determined in a Serono Diagnostic System 9010 cell counter (Biochem
ImmunoSystem). Differential leukocyte counts were determined after
staining with Wright's stain (Sigma).
S. aureus infection assay.
We used the procedure
developed by Thomas et al. (28). Briefly, S. aureus (Cowan strain 12598; American Type Culture Collection, Rockville, Md.) were grown overnight in brain heart broth (Difco, Detroit, Mich.) in a bacterial shaker at 37°C. On the day of the experiment, bacteria were washed three times in PBS and
spectrophotometrically adjusted to ~108 CFU/ml (optical
density of 2.0). The bacterial concentration was confirmed by plating
serial dilutions on brain heart agar plates.
Dfy/ and Dfy+/+ mice
were injected intraperitoneally with 1 ml of PBS solution containing
109 to 5 × 1010 CFU/ml and were observed
daily. Dying mice were euthanized with CO2. In a separated
set of experiments, 20 Dfy/ and 20 Dfy+/+ mice were injected with 109
CFU/ml and euthanized after 24 hours; then total white cells and
neutrophils in the peritoneal cavity were evaluated as described for
experiments involving aseptic infections.
Determination of PMN influx into intestine and lung. The polymorphonuclear leukocyte (PMN) count was determined by the myeloperoxidase (MPO) assay as previously described (17). The lungs and intestines were removed, blotted, and frozen on dry ice. The tissues were thawed in a solution containing 0.5% hexadecyltrimethylammonium bromide dissolved in 10 mM morpholinepropanesulfonic acid buffer (pH 7.0) and homogenized with a Polytron (Kinematic KG) tissue homogenizer. The suspension was sonicated, and large debris were removed by centrifugation at 20,000 × g at 4°C for 30 min. An aliquot of the supernatant was allowed to react with a solution of containing 1.6 mM tetramethylbenzidine and 0.3 mM H2O2. After 2 min of incubation, the reaction was stopped with 2 M acetic acid. The rate of change in absorbance was measured by a spectrophotometer at 650 nm. MPO activity was defined as the quantity of enzyme that degrades 1 µmol of peroxide/min at 25°C. The average of duplicates was expressed in units per gram of wet tissue.
Statistical analysis.
Data are presented as the mean ± standard error of the mean. Data for Dfy/
and Dfy+/+ mice were compared by t
test using the Number Cruncher Statistical System 2000 software and
were considered statistically significant when P was <0.05.
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RESULTS AND DISCUSSION |
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Top
Abstract
Introduction
Materials and Methods
Results and Discussion
References
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Deletion of Dfy in mice. We generated a mouse strain lacking the promoter region, exon 1, exon 2, and the single intron of Dfy (Fig. 1A). The deletion was confirmed by Southern blot analysis using exon 2 as a probe (Fig. 1B). The same probe was used in a Northern blot analysis of mRNA obtained from spleens and brains of the knockout mice, and no Dfy-specific mRNA was observed (Fig. 1C). In human and mouse brains, the coding sequences of gp-Fy are located at the 3' end of an 8.5-kb mRNA (4, 11). The absence of a Dfy product was further validated by FACS analysis of mouse erythrocytes with a Dfy-specific rabbit polyclonal antibody (Fig. 1D).
Genotypic analysis of offspring from heterozygous × heterozygous breeding pairs.
Mice that carried one copy of the
deleted gene were interbred to generate litters that were +/+, +/,
and / for Dfy as determined from genomic PCR of DNA
extracted from tail snips. Pups from heterozygous parents were
genotyped in this way, and the ratios of +/+, +/, and / mice
yielded the predicted Mendelian ratios of 1:2:1 (41:84:43) as expected
for nonlethal alleles. Thus, the Dfy knockout pups were no
less viable than their wild-type littermates. Mice heterozygous or
homozygous for the Dfy allele appeared healthy, developed
normally, and did not display any impairment of reproductive capacity
and neonatal survival. Both heterozygous × heterozygous and
homozygous × homozygous breeding pairs produced litters similar
in size to those produced by wild-type breeding pairs, demonstrating
that the absence of the Duffy-like protein does not hinder the
fertility of male or female mice (Table
1).
|
Phenotypic analysis of homozygous Dfy/
mice.
At a gross phenotypic level, the absence of gp-Fy had no
discernible impact. Dfy/ mice were
indistinguishable from their wild-type littermates with respect to body
weight, body length, head length, and tail length (not shown). In
addition, they exhibited no macroscopic or microscopic alterations in
all organs examined (spleen, lung, intestine, kidney, liver, lymph
nodes, thymus, brain, and heart [not shown]). We found no differences
in white or red blood cell counts or in levels of hemoglobin between
wild-type and knockout mice (not shown), nor were alterations in
embryonic development observed.
Neurological analysis of homozygous
Dfy/ mice.
There was no indication of
an overall difference between the knockout and wild-type mice in 20 items included in neurological examinations or differences in 15 behavioral measures (not shown).
/ mice.
The observations in Dfy/ mice are similar to
those of Duffy mutant humans who do not express gp-Fy in all cell
types. The human equivalent to mouse Dfy/ is
a nonsense mutation that produces a premature stop codon (UAG) in the
coding sequence. The consequence of the mutation is the production of a
truncated, nonfunctioning, and disposable protein in all cell types
(22, 24). For example, we studied a woman with a premature
stop codon in exon 2 who was healthy and had borne 15 children.
Dfy in mice, like FY in humans, is not an
essential gene (24).
Aseptic infections.
In the absence of an overt phenotype, even
in mice as old as 15 months, the Dfy/ mice
were tested for their response to septic and aseptic infection. We
hypothesized that gp-Fy might participate in leukocyte migration since
it is an endothelial cell membrane protein (3). This idea is
reinforced when one considers that gp-Fy is in the apical and
basolateral plasma membrane domains, including caveolae (3). Mechanistically, the neutrophil transendothelial pathway is in some
respects comparable to malarial parasite invasion; in both cases, the
invading cell enters via invagination of the cell membrane rather than
intracellular penetration (7, 13, 16). In the absence of
Duffy protein, the merozoites cannot invade the erythrocytes (16).
/ mice that
migrated into the peritoneal cavity was one-half of that of
Dfy+/+ mice with LPS and thioglycolate
peritonitis (Fig. 2). However, there was
no difference between wild-type and knockout mice in zymosan
peritonitis (Fig. 2). The migration of lymphocytes and monocytes into
the peritoneal cavity was not affected by the absence of Duffy-like
protein (not shown).
|
/ animals (Fig.
3).
|
Bacterial infections.
Susceptibility to bacterial infection is
an appropriate test of whether the absence of Duffy-like protein
affects the ability of the organism to fight infection. We used the
S. aureus model of gram-positive infection since it is a
clinically important gram-positive pathogen (28). The
absence of Duffy-like protein did not affect the ability of
Dfy/ mice to resist the pathogen (Fig.
4). Dfy/ mice did not
show an increase in susceptibility to this bacterial infection.
Moreover, in S. aureus peritonitis, like in zymosan peritonitis, we found equal recruitment of leukocytes in the absence and in the presence of Duffy-like protein (not shown). It remains to be
demonstrated whether a different response will occur with other
pathogens.
|
) and
Dfy+/+ (
) mice after S. aureus
challenge. Mice were injected intraperitoneally with various
concentrations of S. aureus. Animals were observed daily for
signs of systemic infections, and very sick animals were euthanized.
Conclusion.
In this study, a mouse strain lacking the mouse
gene orthologous to the human Duffy gene was generated by homologous
recombination with a gene-targeting vector. The homozygous
Dfy/ mice were indistinguishable from their
wild-type littermates in size, health, embryonic development, and
neurological behavior. Moreover, Dfy/ mice
were not more susceptible to S. aureus infection than
homozygous Dfy+/+ mice. The only difference
between Dfy/ and
Dfy+/+ mice that we found was a diminution for
PMN trafficking in the mutant mice after thioglycolate or LPS aseptic
inflammation. No such compromise in neutrophil migration was observed
when zymosan was injected or when the animals were infected with
S. aureus. The human counterparts of
Dfy/ mice are healthy individuals, and the
study reported here indicates that both Dfy in mice and
FY in humans are redundant genes.
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ACKNOWLEDGMENTS |
|---|
We thank J. Visser and M. Ershler (Laboratory of Stem Cell Biology, New York Blood Center) for the E14-1 ES cells; in particular, we are grateful to M. Ershler for technical help with identification and isolation of the transfected ES cells. We thank J. Hesselgesser (Department of Immunology and Pharmaceutical Discovery, Berlex BioScience, Richmond, Calif.) for the Dfy-specific rabbit polyclonal antibody M4. We thank A. Molinaro (Laboratory of Microchemistry, New York Blood Center) for work in DNA sequencing, T. Huima and Y. Oksov for artwork, and B. Faris and H. Sender for secretarial assistance.
This research was supported by SCOR (Specialized Center of Research) grant HL 54459 to A.O.P. from the National Heart, Lung, and Blood Institute, National Institutes of Health.
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FOOTNOTES |
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* Corresponding author. Mailing address: Laboratory of Cell Biology, Lindsley F. Kimball Research Institute of the New York Blood Center, 310 E. 67th St., New York, NY 10021. Phone: (212) 570-3023. Fax: (212) 570-3195. E-mail: opogo{at}nybc.org.
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REFERENCES |
|---|
|
Top
Abstract
Introduction
Materials and Methods
Results and Discussion
References
|
|---|
| 1. | Ajuebor, M. N., R. J. Flower, R. Hannon, M. Christie, K. Bowers, A. Verity, and M. Perretti. 1998. Endogenous monocyte chemoattractant protein-1 recruits monocytes in the zymosan peritonitis model. J. Leukoc. Biol. 63:108-116[Abstract]. |
| 2. |
Carlos, T. M., and J. M. Harlan.
1994.
Leukocyte-endothelial adhesion molecules.
Blood
84:2068-2101 |
| 3. |
Chaudhuri, A.,
S. Nielsen,
M.-L. Elkjaer,
V. Zbrzezna,
F. Fang, and A. O. Pogo.
1997.
Detection of Duffy antigen in the plasma membranes and caveolae of vascular endothelial and epithelial cells of nonerythroid organs.
Blood
89:701-712 |
| 4. |
Chaudhuri, A.,
J. Polyakova,
V. Zbrzezna,
K. Williams,
S. Gulati, and A. O. Pogo.
1993.
Cloning of glycoprotein D cDNA, which encodes the major subunit of the Duffy blood group system and the receptor for the Plasmodium vivax malaria parasite.
Proc. Natl. Acad. Sci. USA
90:10793-10797 |
| 5. |
Chaudhuri, A.,
V. Zbrzezna,
J. Polyakova,
A. O. Pogo,
J. Hesselgesser, and R. Horuk.
1994.
Expression of the Duffy antigen in K562 cells.
J. Biol. Chem.
269:7835-7838 |
| 6. | Darbonne, W. C., G. C. Rice, M. A. Mohler, T. Apple, C. A. Hébert, A. J. Valente, and J. B. Baker. 1991. Red blood cells are a sink for interleukin 8, a leukocyte chemotaxin. J. Clin. Investig. 88:1362-1369. |
| 7. |
Feng, D.,
J. A. Nagy,
K. Pyne,
H. F. Dvorak, and A. M. Dvorak.
1998.
Neutrophils emigrate from venules by a transendothelial cell pathway in response to FMLP.
J. Exp. Med.
187:903-915 |
| 8. | Hadley, T. J., Z. Lu, K. Wasniowska, A. W. Martin, S. C. Peiper, J. Hesselgesser, and R. Horuk. 1994. Postcapillary venule endothelial cells in kidney express a multispecific chemokine receptor that is structurally and functionally identical to the erythroid isoform, which is the Duffy blood group antigen. J. Clin. Investig. 94:985-991. |
| 9. |
Horuk, R.,
C. E. Chitnis,
W. C. Darbonne,
T. J. Colby,
A. Rybicki,
T. J. Hadley, and L. H. Miller.
1993.
A receptor for the malarial parasite Plasmodium vivax: the erythrocyte chemokine receptor.
Science
261:1182-1184 |
| 10. | Horuk, R., A. Martin, J. Hesselgesser, T. Hadley, Z. H. Lu, Z. X. Wang, and S. C. Peiper. 1996. The Duffy antigen receptor for chemokines: structural analysis and expression in the brain. J. Leukoc. Biol. 59:29-38[Abstract]. |
| 11. |
Luo, H.,
A. Chaudhuri,
K. R. Johnson,
K. Neote,
V. Zbrzezna,
Y. He, and A. O. Pogo.
1997.
Cloning, characterization, and mapping of a murine promiscuous chemokine receptor gene: homolog of the human Duffy gene.
Genome Res.
7:932-941 |
| 12. | Mayadas, T. N., R. C. Johnson, H. Rayburn, R. O. Hynes, and D. D. Wagner. 1993. Leukocyte rolling and extravasation are severely compromised in P selectin-deficient mice. Cell 74:541-554[CrossRef][Medline]. |
| 13. | Middleton, J., S. Neil, J. Wintle, I. Clark-Lewis, H. Moore, C. Lam, M. Auer, E. Hub, and A. Rot. 1997. Transcytosis and surface presentation of IL-8 by venular endothelial cells. Cell 91:385-395[CrossRef][Medline]. |
| 14. | Miller, L. H., S. J. Mason, D. F. Clyde, and M. H. McGinniss. 1976. The resistance factor to Plasmodium vivax in Blacks: the Duffy-blood-group genotype, FyFy. N. Engl. J. Med. 295:302-304[Abstract]. |
| 15. |
Miller, L. H.,
S. J. Mason,
J. A. Dvorak,
M. H. McGinniss, and K. I. Rothman.
1975.
Erythrocyte receptors for (Plasmodium knowlesi) malaria: Duffy blood group determinants.
Science
189:561-563 |
| 16. | Miller, L. H., F. M. McAuliffe, and J. G. Johnson. 1979. Invasion of erythrocytes by malaria merozoites. Prog. Clin. Biol. Res. 30:497-502[Medline]. |
| 17. | Mullane, K. M., R. Kraemer, and B. Smith. 1985. Myeloperoxidase activity as a quantitative assessment of neutrophil infiltration in ischemic myocardium. J. Pharmacol. Methods 14:157-167[CrossRef][Medline]. |
| 18. |
Neote, K.,
J. Y. Mak,
L. F. Kolakowski, and T. J. Schall.
1994.
Functional and biochemical analysis of the cloned Duffy antigen: identity with the red blood cell chemokine receptor.
Blood
84:44-52 |
| 19. |
Oquendo, P.,
J. Alberta,
D. Wen,
J. L. Graycar,
R. Derynck, and C. D. Stiles.
1989.
The platelet-derived growth factor-inducible KC gene encodes a secretory protein related to platelet  -granule proteins.
J. Biol. Chem.
264:4133-4137 |
| 20. | Papaioannou, V., and R. Johnson. 1993. Production of chimeras and genetically defined offspring from targeted ES cells, p. 107-146. In A. L. Joyner (ed.), Gene targeting, a practical approach. Oxford University Press, Oxford, England. |
| 21. | Pogo, A. O., and A. Chaudhuri. 1997. The Duffy blood group system and its extension in nonhuman primates, p. 219-235. In A. Blancher, J. Klein, and W. W. Socha (ed.), Molecular biology and evolution of blood group and MHC antigens in primates. Springer-Verlag, Berlin, Germany. |
| 22. | Pogo, A. O., and A. Chaudhuri. The Duffy protein: a malarial and chemokine receptor. Semin. Hematol., in press. |
| 23. | Premack, B. A., and T. J. Schall. 1996. Chemokine receptors: gateways to inflammation and infection. Nat. Med. 2:1174-1178[CrossRef][Medline]. |
| 24. | Rios, M., A. Chaudhuri, G. Mallinson, L. Sausais, A. E. Gomensoro-Garcia, J. Hannon, S. Rosenberger, J. Poole, G. Burgess, L. Castilho, R. Oyen, A. O. Pogo, and M. Reid. New genotypes in Fy(a-b-) individuals: nonsense mutations (Trp to stop) in the coding sequence of either FYA or FYB. Br. J. Haematol., in press. |
| 25. | Samokhvalov, I., J. Hendrikx, J. Visser, A. Belyavsky, D. Sotiropolous, and H. Gu. 1997. Mice lacking a functional Chk gene have no apparent defects in the hematopoietic system. Biochem. Mol. Biol. Int. 43:115-122[Medline]. |
| 26. | Springer, T. A. 1994. Traffic signals for lymphocyte recirculation and leukocyte emigration: the multistep paradigm. Cell 76:301-314[CrossRef][Medline]. |
| 27. |
Szabo, M. C.,
K. S. Soo,
A. Zlotnik, and T. J. Schall.
1995.
Chemokine class differences in binding to the Duffy antigen-erythrocyte chemokine receptor.
J. Biol. Chem.
270:25348-25351 |
| 28. |
Thomas, C. A.,
T. Kodama,
H. Suzuki,
S. Silverstein, and J. El Khoury.
2000.
Protection from lethal gram-positive infection by macrophage scavenger receptor dependent phagocytosis.
J. Exp. Med.
191:147-156 |
| 29. | Tournamille, C., Y. Colin, J. P. Cartron, and C. Le Van Kim. 1995. Disruption of a GATA motif in the Duffy gene promoter abolishes erythroid gene expression in Duffy-negative individuals. Nat. Gen. 10:224-228[CrossRef][Medline]. |
| 30. | VanOtteren, G. M., R. M. Strieter, S. L. Kunkel, R. Paine, M. J. Greenberger, J. M. Danforth, M. D. Burdick, and T. J. Standiford. 1995. Compartmentalized expression of RANTES in a murine model of endotoxemia. J. Immunol. 154:1900-1908[Abstract]. |
Molecular and Cellular Biology, May 2000, p. 3097-3101, Vol. 20, No. 9
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Copyright © 2000, American Society for Microbiology. All rights reserved.
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(2005). Endothelial Activation and Increased Heparan Sulfate Expression in Cystic Fibrosis. Am. J. Respir. Crit. Care Med.
172: 892-898
[Abstract] [Full Text] -
Kashiwazaki, M., Tanaka, T., Kanda, H., Ebisuno, Y., Izawa, D., Fukuma, N., Akimitsu, N., Sekimizu, K., Monden, M., Miyasaka, M.
(2003). A high endothelial venule-expressing promiscuous chemokine receptor DARC can bind inflammatory, but not lymphoid, chemokines and is dispensable for lymphocyte homing under physiological conditions. Int Immunol
15: 1219-1227
[Abstract] [Full Text] -
Lee, J. S., Frevert, C. W., Wurfel, M. M., Peiper, S. C., Wong, V. A., Ballman, K. K., Ruzinski, J. T., Rhim, J. S., Martin, T. R., Goodman, R. B.
(2003). Duffy Antigen Facilitates Movement of Chemokine Across the Endothelium In Vitro and Promotes Neutrophil Transmigration In Vitro and In Vivo. J. Immunol.
170: 5244-5251
[Abstract] [Full Text] -
Heidemann, J., Ogawa, H., Dwinell, M. B., Rafiee, P., Maaser, C., Gockel, H. R., Otterson, M. F., Ota, D. M., Lugering, N., Domschke, W., Binion, D. G.
(2003). Angiogenic Effects of Interleukin 8 (CXCL8) in Human Intestinal Microvascular Endothelial Cells Are Mediated by CXCR2. J. Biol. Chem.
278: 8508-8515
[Abstract] [Full Text] -
Lee, J. S., Frevert, C. W., Thorning, D. R., Segerer, S., Alpers, C. E., Cartron, J.-P., Colin, Y., Wong, V. A., Martin, T. R., Goodman, R. B.
(2003). Enhanced Expression of Duffy Antigen in the Lungs During Suppurative Pneumonia. J. Histochem. Cytochem.
51: 159-166
[Abstract] [Full Text] -
Middleton, J., Patterson, A. M., Gardner, L., Schmutz, C., Ashton, B. A.
(2002). Leukocyte extravasation: chemokine transport and presentation by the endothelium. Blood
100: 3853-3860
[Abstract] [Full Text] -
Carter, R., Mendis, K. N.
(2002). Evolutionary and Historical Aspects of the Burden of Malaria. Clin. Microbiol. Rev.
15: 564-594
[Abstract] [Full Text] -
White, P., Liebhaber, S. A., Cooke, N. E.
(2002). 129X1/SvJ Mouse Strain Has a Novel Defect in Inflammatory Cell Recruitment. J. Immunol.
168: 869-874
[Abstract] [Full Text] -
Du, J., Luan, J., Liu, H., Daniel, T. O., Peiper, S., Chen, T. S., Yu, Y., Horton, L. W., Nanney, L. B., Strieter, R. M., Richmond, A.
(2002). Potential role for Duffy antigen chemokine-binding protein in angiogenesis and maintenance of homeostasis in response to stress. J. Leukoc. Biol.
71: 141-153
[Abstract] [Full Text]
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