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Blood, Vol. 95 No. 2 (January 15), 2000:
pp. 375-387
REVIEW ARTICLE
From the Department of Biological and Biomedical Sciences,
University of the West of England, Bristol, England, and the New York
Blood Center, New York, NY.
The Rh blood group system is one of the most polymorphic and
immunogenic systems known in humans. In the past decade, intense investigation has yielded considerable knowledge of the molecular background of this system. The genes encoding 2 distinct Rh proteins that carry C or c together with either E or e antigens, and the D
antigen, have been cloned, and the molecular bases of many of the
antigens and of the phenotypes have been determined. A related protein,
the Rh glycoprotein is essential for assembly of the Rh protein complex
in the erythrocyte membrane and for expression of Rh antigens. The
purpose of this review is to provide an overview of several aspects of
the Rh blood group system, including the confusing terminology,
progress in molecular understanding, and how this developing knowledge
can be used in the clinical setting. Extensive documentation is
provided to enable the interested reader to obtain further information.
(Blood. 2000;95:375-387)
The Rh blood group system was first described 60 years
ago. A woman had a severe transfusion reaction when she was transfused with blood from her husband following delivery of a stillborn child
with erythroblastosis fetalis. Her serum agglutinated red blood cells
(RBCs) from her husband and from 80% of Caucasian ABO-compatible
donors.1 The following year, Landsteiner and Wiener2 found that sera from rabbits (and later guinea
pigs) immunized with RBCs from Macaca mulatta (Macacus
rhesus in the original paper) agglutinated 85% of human RBC
samples. Initially, it was thought that the animal and human antibodies
identified a common factor, Rh, on the surface of rhesus and
human RBCs. It was soon realized that this was not the
case.3 Therefore, the original terms (Rh factor and
anti-Rh) coined by Landsteiner and Wiener, although being misnomers,
have continued in common usage. The heteroantibody was renamed anti-LW
(after Landsteiner and Wiener), and the human alloantibody was renamed
anti-D.4
The Rh blood group system is the most polymorphic of the human blood
groups, consisting of at least 45 independent antigens and, next to
ABO, is the most clinically significant in transfusion medicine. The
ability to clone complementary DNA (cDNA) and sequence genes encoding
the Rh proteins has led to an understanding of the molecular bases
associated with some of the Rh antigens. Serologic detection of
polymorphic blood group antigens and of phenotypes provides a valuable
source of appropriate blood samples for study at the molecular
level. This review summarizes our present understanding of the
complexities of Rh blood group expression and how this knowledge
impacts on clinical situations that arise through Rh blood group incompatibility.
Several nomenclatures have been used to describe antigens, proteins,
and genes in the Rh system. Throughout this review, we will use
traditional terminology recommended by the International Society of
Blood Transfusion (ISBT) committee for terminology of blood group
antigens.5 The numeric portion of the ISBT terminology for
Rh antigens is based on the nomenclature described by Rosenfield et
al.6-9 RH30 and RH50 have been used to
describe genes encoding Rh proteins (Rh30) and Rh glycoprotein (Rh50),
respectively, where the numbers relate to the apparent molecular mass
of the proteins on a SDS-polyacrylamide gel. Because Rh30 and Rh50 also
relate to Goa and FPTT antigens, respectively, we will use
RH as a generic term for genes encoding either the RhD protein
or the RhCcEe (also known as RhCE) protein and use RHAG for the
gene encoding the Rh-associated glycoprotein (RhAG). The common Rh
antigens: D, C or c, and E or e, were originally written in
alphabetical order (CDE) but later, when it was recognized that C and E
antigens are inherited en bloc, the order was changed to DCE. Although d antigen, which was thought to be antithetical to D, does not exist,
the letter "d" is used to indicate the D-negative phenotype. The
most frequently occurring forms of RHCE and RHD encode
8 haplotypes: Dce, dce, DCe, dCe, DcE, dcE, DCE, and dCE, known in
short, respectively, as R0, r, R1, r',
R2, r Biochemical studies, protein purification, and amino acid sequencing
of Rh and RhAG are beyond the scope of this article but have been
reviewed elsewhere.10-16
Rh protein family
RhD and RhCcEe proteins.
The RhD protein expresses the D antigen, while the RhCcEe protein
carries either C or c antigens (involving the second extracellular loop) together with E or e antigens (involving the fourth extracellular loop) on the same protein.19,28-30 Characteristics of the
RhD protein (synonyms: Rh30, Rh30B, Rh30D, D30, Rh30
polypeptide [30 kd], RhXIII, Rh13) and of the RhCcEe protein
(synonyms: Rh30, Rh30A, Rh30C [RhCE], Rh30 polypeptide [32 kd],
RhIXb cDNA, [RhcE], Rh21 cDNA [RhcE], R6A32, Rhce,
RhCe, RhcE, RhCE, CcEe) are summarized in Table 1 and depicted in
Figure 1. Analysis of the primary amino acid sequences (inferred from
cDNAs) shows that the first 41 N-terminal amino acids of RhD and RhCE/e
are identical.20,31-33 and that RhD differs from the
common forms of RhCE by only 30 to 35 amino acids along the
entire protein.20,28,31-33,35,36 Despite the high degree of
homology, the various RhCcEe proteins do not express any D
epitopes, and RhD protein does not express C or e antigens.
Rh-associated glycoprotein.
The characteristics of RhAG (synonyms: Rh50, Rh glycoprotein Rh50A,
D50, MB-2D10 protein, R6A45, GP50, GP50A) are
summarized in Table 1 and depicted in Figure 1. One of the 2 potential
N-glycan sites is glycosylated. A third site is predicted to be
cytoplasmic and, therefore, not accessible for
glycosylation.17,39 The N-glycan carries ABH
antigens,12 but RhAG is not known to possess a
protein-based blood group polymorphism. Based on the predicted amino
acid sequence, RhAG shares 39.2% and 38.5% amino acid sequence identity with, respectively, the Rhce and RhD
proteins.17,20,31-33
Expression of Rh proteins and RhAG during erythropoiesis.
Rh antigens appear early during erythropoietic differentiation. Anti-D
binds to approximately 3% of BFU-E (burst-forming unit, erythroid),
68% of CFU-E (colony-forming unit, erythrocyte), and to all of the
more mature erythroid cells. However, the binding of anti-D to
proerythroblasts, basophilic erythroblasts, polychromatophilic erythroblasts, and normoblasts was, respectively, 25%, 50%, 66%, and
75% compared with mature RBCs.33 RhAG protein is
detectable on CD34 progenitors isolated from cord blood, after culture
for 3 to 5 days, while RhCcEe appears after 5 to 7 days, and RhD
appears after 9 to 11 days of culture.40 In the fetus, Rh
antigens are expressed on RBCs from the 6-week conceptus.41
Possible function of Rh protein family.
The function of the Rh complex remains unclear. Rh proteins have
approximately 20% homology to the methylamine permease (Mep) transporters and ammonium transporters (Amt) in yeast, bacteria, and
simple plants.42 This family of transporters are uniporters that have evolved to concentrate ammonium salts from the surrounding environment. Higher animals use more complex nitrogen sources, and they
eliminate toxic ammonium via the urea cycle and transport it in the
form of glutamine and alanine. The role of the Rh complex as a
dedicated ammonium transporter is unlikely, but the complex could
cotransport ammonium with other cations; however, further study is
needed. Matassi et al43 report that RHAG shares greatest homology to MEP2, which behaves as an ammonium sensor and transporter in yeast.44 Furthermore, the presence of RhAG
homologs in Caenorhabditis elegans and Geodia cydonium infers
they have roles that are not confined to RBCs.
Rh accessory proteins
LW glycoprotein.
The LW glycoprotein (synonym: ICAM-4) is a single pass (type I)
membrane protein with homology to intercellular adhesion molecules (ICAMs), which are ligands for Integrin-associated protein.
Isoform 2 of integrin-associated protein (IAP; synonyms: CD47, BRIC 125 glycoprotein, AgOAB, 1D8) is present in the RBC membrane, where it is
predicted to pass through the RBC membrane 5 times and have 6 potential
N-glycan motifs.50,51 IAP carries ABH antigens but no known
protein-based blood group antigen. IAP occurs as different isoforms in
various tissues where it binds to Glycophorin B.
Glycophorin B (GPB; synonyms: Ss sialoglycoprotein [SGP],
Fy glycoprotein.
A possible association between the Fy glycoprotein (synonyms:
Duffy, DARC) and the Rh complex is indicated by the Fy5 antigen, which
is absent from Fy(a Band 3.
Band 3 (synonyms: AE1, anion exchanger, solute carrier family 4 anion
exchanger member 1) is a glycosylated protein that is predicted to pass
through the RBC membrane 12 or 14 times and is the major anion
transporter.61,62 Unlike the proteins described above, band
3 is apparently normal in Rhnull RBCs; however, based on
hemagglutination studies, antigens on Rh proteins and on band 3 are
decreased in South-East Asian ovalocytic RBCs.63 The
molecular defect associated with South-East Asian ovalocytic RBCs
results from a deletion of a segment of DNA encoding 9 amino acids
located at the boundary of the cytoplasmic N-terminal domain and
membrane domain of band 3.64-67 Recent evidence that the
expression of endogenous and retrovirally expressed Rh antigens were
enhanced following transduction of K562 cells with band 3 suggests that
band 3 and Rh proteins associate in erythroid cells.68
The genes encoding RhD and RhCcEe are highly homologous, while the
gene encoding RhAG is almost 40% homologous. The 3 genes are each
composed of 10 exons; RHCE and RHD in tandem encompass 69 kilobases (kb) of DNA (Figure 2), while
RHAG encompasses 32 kb. The RhD protein is encoded by
RHD (synonyms: RH30, RH30B, RH30D, RHXIII, RH13); the
RhCcEe protein is encoded by RHCE (synonyms: RH30, RH30A,
RH30C (RHCE), RHIXB, RH21); and the RHAG
glycoprotein is encoded by RHAG (synonyms: RH50,
RH50A).
Evolution of the RH gene family
Since the first descriptions of Rh
cDNAs,20,31-33 much effort has been expended in
differentiating the molecular bases underlying the antigens of the Rh
system. The different genetic mechanisms that give rise to the major
clinically relevant Rh antigens are described within this section.
These include gene deletion (D-negative phenotype); gene
conversion (C/c polymorphism); antithetical missense mutations (E/e);
and other missense mutations (VS and V). The RH genes appear to
be a source of massive diversity, and combinations of these different
genetic rearrangements abound among all racial groups. We have selected
examples of Rh polymorphisms that are of clinical significance and have
been defined at the molecular level. Figures 3-6 detail the molecular
basis of published examples of Rh variants. Enthusiastic readers
requiring more data regarding Rh variants should consult
references.16,25,85,86
D antigen
CcEe antigens
VS and V antigens
G antigen
Rh variants
Low-incidence antigens associated with partial D antigens.
Low-incidence antigens associated with some partial D phenotypes are
due to novel structures on the RBC surface and are useful markers for
the identification of the partial D (Figure 4).110 A few
low-incidence antigens are associated with more than 1 molecular background, eg, the FPTT (Rh50) antigen is expressed on DFR,
RoHar, and DIVa(C) RhD epitope mapping Partial D antigens were classically identified by testing the RBCs with well-characterized polyclonal anti-D made by other people with partial D phenotypes and, also, by testing the patient's anti-D against RBCs with known partial D antigens. Human monoclonal antibodies are now being used to classify partial D antigens in terms of expressed epitopes. The original model consisted of 8- and 9-epitope D (epD)112,113 but has been expanded to consist of 16,110 30,114 and 37 epitopes.115 When using monoclonal anti-D to define D epitopes, it is important to perform the testing at the correct pH, temperature, ionic strength, and antibody concentration; to use RBCs that have been stored appropriately; and to include controls.110,114 Most D epitopes are conformation-dependent and may be influenced by other proteins and lipids in the RBC membrane. Indeed, only 1 monoclonal anti-D has been described that reacts strongly by immunoblotting, implying that the epitope it recognizes may be linear.116
Clinical complications result from RBC destruction due to the interaction of an alloantibody with RBCs carrying the corresponding antigen. The D antigen is highly immunogenic and induces an immune response in 80% of D-negative persons when transfused with 200 mL of D-positive blood.123 For this reason, in most countries D typing is performed routinely on every blood donor and transfusion recipient so that D-negative patients receive D-negative RBC products. Consequently, clinical complications due to mismatched transfusions are infrequent. In contrast, despite the use of immunosuppressive therapy with anti-D immunoglobulin prophylaxis, D alloimmunization in pregnancy still occurs. Alloantibodies Alloantibodies that recognize Rh antigens are usually IgG and react by the indirect antiglobulin test. This is a test in which RBCs are incubated in serum, washed to remove free immunoglobulin, and then exposed to an antiglobulin reagent that is formulated to detect the cell-bound IgG. The end point of the test is hemagglutination. Alloantibodies in the Rh blood group system can cause destruction of transfused RBCs and of fetal RBCs in hemolytic disease of the newborn (HDN). People whose RBCs have a rare deleted Rh phenotype (Rhnull, D ) readily make alloantibodies.
People with the Rhnull phenotype of amorph or regulator
type can make anti-Rh29 (an antibody to "total" Rh), anti-Rh17
(an antibody to the RhCc/Ee protein), anti-D, anti-C, or a mixture of
specificities. Transfusion of a patient with anti-Rh29 is a problem
because only Rhnull RBCs will be compatible: People with
the Rhnull phenotype are not only rare, but they have a
compensated hemolytic anemia and are therefore unlikely to meet
predonation criteria.124 People with either the
D, D , DCW, or Dc
phenotype make anti-Rh17. A patient with anti-Rh17 also represents a
transfusion conundrum because only RBCs with a deleted phenotype will
be compatible.
Autoantibodies An autoantibody is one that reacts with an antigen on the antibody maker's own RBCs. Autoantibodies that react optimally at 37°C are present in the serum of about 80% of patients with warm autoimmune hemolytic anemia.125 Although most of these autoantibodies appear to be "nonspecific," many have specificity to an Rh antigen, notably to e. Rarely is the specificity clear-cut, but the autoantibody commonly reacts more weakly with antigen-negative RBCs than with antigen-positive RBCs; however, in these cases, transfused antigen-negative RBCs only rarely survive better than antigen-positive RBCs.123 Autoantibodies in serum from patients with warm autoimmune hemolytic anemia may be nonreactive only with Rhnull and D RBCs (autoanti-Rh17), or only
with Rhnull RBCs (autoanti-Rh29). In such cases,
antigen-negative blood will not be available, and transfusion with
antigen-positive RBCs should not be withheld if the patient has
life-threatening anemia.125,126 In most cases, the
autoantibody is equally reactive with all RBCs tested whether from
donors or antibody detection/identification kits. Thus, in the clinical
setting, it is important to perform tests to ensure that the patient's
serum does not have potentially clinically significant alloantibodies
underlying the autoantibodies before transfusing incompatible RBCs.
Detection and identification of such antibodies is required to prevent
transfusion reactions but is beyond the scope of this review. For more
information, see a current textbook on laboratory aspects of
transfusion medicine.125-127
Partial and weak D phenotypes As described earlier, people whose RBCs have a weak D phenotype (quantitative D variant) do not make anti-D, whereas people whose RBCs have a partial D phenotype (qualitative D variant with or without weakening of the D antigen) can make alloanti-D. This presents a different problem depending on whether the person is a donor or a patient. For donors, detection of weak and partial D antigens would eliminate the possibility of immunization should such blood be transfused to a true D-negative patient. However, historical data show that weakly expressed D antigens are most unlikely to be immunogenic. For transfusion recipients and pregnant women, it is common practice to use a procedure that will classify RBCs with a weak D antigen or some partial D antigens as D-negative. Thus, blood donated from such a person should be labeled as D-positive (Rh-positive), but the same person should be listed as D-negative (Rh-negative) when they are recipients in need of transfusion. The transfusion recipient will receive D-negative RBC products, and the pregnant woman will receive prophylactic Rh immunoglobulin, thereby preventing alloimmunization. Although a pregnant woman with the DVI partial phenotype may make alloanti-D, this has rarely caused a clinical problem to a D-positive fetus.128 In the autologous transfusion setting (in which the person is both the donor and patient), the above policy can cause confusion because partial D RBCs may be typed as D-positive at the donor center but D-negative at the hospital. In practice, it is difficult to distinguish RBCs with the DVI phenotype from other weak D; however, this now can be accomplished by immunoblotting with the unique anti-D, LOR-15C9.129Rh and hemolytic disease of the newborn HDN is caused by maternal IgG antibody crossing the placenta, binding to the fetal antigen-positive RBCs, and initiating their destruction, thereby causing anemia. Prior to the use of prophylactic Rh immunoglobulin, anti-D frequently caused fetal brain damage due to increased levels of bilirubin (kernicterus) and even death (erythroblastosis fetalis). Despite the widespread use of prophylactic Rh immunoglobulin, a significant number of women still become alloimmunized during pregnancy for a variety of reasons, including nonadministration of Rh immunoglobulin, unrecognized miscarriage, leakage of fetal RBCs into the maternal circulation late in pregnancy, and exposure to maternal D-positive RBCs while in utero (grandmother effect).130Rh immunoglobulin prophylaxis in the prevention of HDN. The immunologic mechanism responsible for preventing production of maternal anti-D following administration of prophylactic Rh immunoglobulin may be due, at least in part, to antigen blocking and central inhibition of the immune response by negative feedback in the spleen (for review, see Bowman130). In some instances, recommendations have been made to administer anti-D to partial D-phenotype mothers (eg, DVI and DBT phenotypes) following the birth of D-positive babies.110,136 In Europe, anti-D reagents are selected to deliberately type DVI mothers as D-negative and, thus, ensure that such mothers would automatically receive prophylactic Rh immunoglobulin therapy following pregnancy. Prenatal Rh genotyping When a pregnant woman has a potentially clinically significant alloantibody and the father of the fetus is phenotypically heterozygous for the gene encoding the corresponding antigen (or is unknown), prenatal determination can be considered. The potential benefits of identifying a fetus whose RBCs are predicted to be antigen-negative is enormous in that the need for further invasive techniques is diminished. Fetal DNA can be obtained from amniocytes, chorionic villi, vaginal swabs, and mother's blood (see later). Following cloning and sequencing of RHCE and RHD, many polymerase chain reaction (PCR)-based tests to analyze DNA prepared from amniocytes have been reported (for recent review, see Flegel86). However, the genetic diversity of the Rh genes, particularly among blacks and Japanese, has reduced the clinical utility of this approach because false-negative and false-positive results can occur. Prenatal diagnosis of fetal RHD status exploits structural differences between the RHD and RHCE genes and is based on the assumption that D-negative individuals have a deleted RHD gene. As the knowledge regarding the molecular basis of partial D antigens evolved, use of multiplex,70,86,140,141 heteroduplex,142,143 and multiple sequence-specific PCR reactions144,145 have replaced the single exon genotyping assays32,146,147 in an attempt to avoid "false-negative" typing of a fetus with a partial D antigen. However, because HDN in a fetus whose RBCs have a partial D antigen is rare,148 the clinical value of RHD multiplex analysis may only have marginal added value.
Noninvasive prenatal Rh genotyping. It is now possible to obtain fetally derived DNA using noninvasive procedures. Fetally derived RHD has been detected using nested PCR analysis on genomic DNA (gDNA) extracted from maternal peripheral blood or plasma160-163 or from transcervical samples.164-166 An alternative approach uses cDNA templates derived by reverse transcriptase-PCR from maternal peripheral blood and detection of fetal RhD mRNA targets.167 All noninvasive procedures have limited value because there is no suitable way to assess the presence of fetal cells in a given sample and, thus, negative results cannot be interpreted with confidence. Nevertheless, the fact that fetally derived Rh mRNAs and gDNA can be detected in maternal blood indicates that this area of prenatal diagnosis may soon have an impact. However, it is possible that fetal-nucleated RBCs are the most pertinent target cell type for noninvasive diagnosis168,169 because other fetally derived CD34+ cells have been detected in maternal blood for as long as 27 years postpartum169 and thus could interfere with analyses in women who have had multiple pregnancies. Rh and other disease states Rhnull disease. RBCs from people who have the Rhnull phenotype (synonyms: Rhnull syndrome, Rhnull disease) lack Rh proteins and, thus, Rh antigens. This phenotype is rare (approximately 1 in 6 × 106 individuals)170 and most often results from a consanguineous mating. The syndrome is associated with stomatocytosis, spherocytosis, increased osmotic fragility, altered phospholipid asymmetry, altered cell volume, defective cation fluxes, and elevated Na+/K+ ATPase activity.13,14,171-173 Rhnull RBCs may have a shortened in vivo survival, and the person may have a mild compensated hemolytic anemia.
Myeloid leukemia
Considerable progress has been made in our understanding of the molecular basis of Rh and other blood group antigens in the past 10 years. Despite this, our knowledge concerning the function of many of the components in the RBC remains speculative. The Rh protein complex is a prime example of this; it is a major red cell protein of considerable clinical importance, yet our understanding of its functional significance in human RBCs and other animals relies almost entirely on circumstantial evidence.
We thank Christine Lomas-Francis, Narla Mohandas, Olga Blumenfeld, Geoff Daniels, Michael J. A. Tanner, Jill Storry, and Karina Yazdanbakhsh for reading the manuscript and giving helpful suggestions. Neil Avent thanks Willy Flegel, Giorgio Matassi, and Tim Kemp for providing manuscripts prior to publication. We also thank Robert Ratner for preparing the manuscript and cataloging the references.
Submitted June 11, 1999; accepted August 31, 1999.
Supported in part by a National Institutes of Health Specialized Center of Research (SCOR) grant in transfusion medicine and biology HL54 459.
Reprints: Marion E. Reid, Immunochemistry Laboratory, New York Blood Center, 310 East 67th St, New York, NY 10021; e-mail: mreid{at}nybc.org.
The publication costs of this article were defrayed in part by page charge payment. Therefore, and solely to indicate this fact, this article is hereby marked "advertisement" in accordance with 18 U.S.C. section 1734.
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M. Kjaersgaard, R. Aslam, M. Kim, E. R. Speck, J. Freedman, D. I. H. Stewart, E. J. Wiersma, and J. W. Semple Epitope specificity and isotype of monoclonal anti-D antibodies dictate their ability to inhibit phagocytosis of opsonized platelets Blood, August 15, 2007; 110(4): 1359 - 1361. [Abstract] [Full Text] [PDF]
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Q. Ji, S. Hashmi, Z. Liu, J. Zhang, Y. Chen, and C.-H. Huang CeRh1 (rhr-1) is a dominant Rhesus gene essential for embryonic development and hypodermal function in Caenorhabditis elegans PNAS, April 11, 2006; 103(15): 5881 - 5886. [Abstract] [Full Text] [PDF]
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M. E. Handlogten, S.-P. Hong, C. M. Westhoff, and I. D. Weiner Apical ammonia transport by the mouse inner medullary collecting duct cell (mIMCD-3) Am J Physiol Renal Physiol, August 1, 2005; 289(2): F347 - F358. [Abstract] [Full Text] [PDF]
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K.-S. Kim, E. Feild, N. King, T. Yaoi, S. Kustu, and W. Inwood Spontaneous Mutations in the Ammonium Transport Gene AMT4 of Chlamydomonas reinhardtii Genetics, June 1, 2005; 170(2): 631 - 644. [Abstract] [Full Text] [PDF]
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C. Lopez, S. Metral, D. Eladari, S. Drevensek, P. Gane, R. Chambrey, V. Bennett, J.-P. Cartron, C. Le Van Kim, and Y. Colin The Ammonium Transporter RhBG: REQUIREMENT OF A TYROSINE-BASED SIGNAL AND ANKYRIN-G FOR BASOLATERAL TARGETING AND MEMBRANE ANCHORAGE IN POLARIZED KIDNEY EPITHELIAL CELLS J. Biol. Chem., March 4, 2005; 280(9): 8221 - 8228. [Abstract] [Full Text] [PDF]
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N. L. Nakhoul, H. DeJong, S. M. Abdulnour-Nakhoul, E. L. Boulpaep, K. Hering-Smith, and L. L. Hamm Characteristics of renal Rhbg as an NH4+ transporter Am J Physiol Renal Physiol, January 1, 2005; 288(1): F170 - F181. [Abstract] [Full Text] [PDF]
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P. Ripoche, O. Bertrand, P. Gane, C. Birkenmeier, Y. Colin, and J.-P. Cartron Human Rhesus-associated glycoprotein mediates facilitated transport of NH3 into red blood cells PNAS, December 7, 2004; 101(49): 17222 - 17227. [Abstract] [Full Text] [PDF]
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J. E. Brittain, J. Han, K. I. Ataga, E. P. Orringer, and L. V. Parise Mechanism of CD47-induced {alpha}4{beta}1 Integrin Activation and Adhesion in Sickle Reticulocytes J. Biol. Chem., October 8, 2004; 279(41): 42393 - 42402. [Abstract] [Full Text] [PDF]
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E. Soupene, W. Inwood, and S. Kustu From The Cover: Lack of the Rhesus protein Rh1 impairs growth of the green alga Chlamydomonas reinhardtii at high CO2 PNAS, May 18, 2004; 101(20): 7787 - 7792. [Abstract] [Full Text] [PDF]
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H. Innan A two-locus gene conversion model with selection and its application to the human RHCE and RHD genes PNAS, July 22, 2003; 100(15): 8793 - 8798. [Abstract] [Full Text] [PDF]
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V. Nicolas, C. Le Van Kim, P. Gane, C. Birkenmeier, J.-P. Cartron, Y. Colin, and I. Mouro-Chanteloup Rh-RhAG/Ankyrin-R, a New Interaction Site between the Membrane Bilayer and the Red Cell Skeleton, Is Impaired by Rhnull-associated Mutation J. Biol. Chem., July 3, 2003; 278(28): 25526 - 25533. [Abstract] [Full Text] [PDF]
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F. Noizat-Pirenne, K. Lee, P.-Y. L. Pennec, P. Simon, P. Kazup, D. Bachir, A.-M. Rouzaud, M. Roussel, G. Juszczak, C. Menanteau, et al. Rare RHCE phenotypes in black individuals of Afro-Caribbean origin: identification and transfusion safety Blood, December 1, 2002; 100(12): 4223 - 4231. [Abstract] [Full Text] [PDF]
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F. F. Wagner, N. I. Eicher, J. R. Jorgensen, C. B. Lonicer, and W. A. Flegel DNB: a partial D with anti-D frequent in Central Europe Blood, August 28, 2002; 100(6): 2253 - 2256. [Abstract] [Full Text] [PDF]
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F. F. Wagner, B. Ladewig, K. S. Angert, G. A. Heymann, N. I. Eicher, and W. A. Flegel The DAU allele cluster of the RHD gene Blood, June 17, 2002; 100(1): 306 - 311. [Abstract] [Full Text] [PDF]
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P.-A. Oldenborg, H. D. Gresham, Y. Chen, S. Izui, and F. P. Lindberg Lethal autoimmune hemolytic anemia in CD47-deficient nonobese diabetic (NOD) mice Blood, May 15, 2002; 99(10): 3500 - 3504. [Abstract] [Full Text] [PDF]
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U. Ludewig, N. von Wiren, and W. B. Frommer Uniport of NH4+ by the Root Hair Plasma Membrane Ammonium Transporter LeAMT1;1 J. Biol. Chem., April 12, 2002; 277(16): 13548 - 13555. [Abstract] [Full Text] [PDF]
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C. M. Westhoff, M. Ferreri-Jacobia, D.-O. D. Mak, and J. K. Foskett Identification of the Erythrocyte Rh Blood Group Glycoprotein as a Mammalian Ammonium Transporter J. Biol. Chem., April 5, 2002; 277(15): 12499 - 12502. [Abstract] [Full Text] [PDF]
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L.-M. Stott, R. N. Barker, and S. J. Urbaniak Identification of alloreactive T-cell epitopes on the Rhesus D protein Blood, December 15, 2000; 96(13): 4011 - 4019. [Abstract] [Full Text] [PDF]
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Top
Abstract
Introduction
, Rz, and ry. The
uppercase "R" is used when the D antigen is expressed, lowercase
"r" when it is not. This notation has practical value in
transfusion medicine as a means to communicate the Rh phenotype of a
patient or donor. Rare deletion phentoypes use dashes in the notation
to indicate a lack of antithetical antigens; eg,
Dc
2 integrins. LW has been reported to
be a ligand for the integrin LFA-1 (synonyms: 
L
-SGP,
PAS-3) is a type I membrane glycoprotein that has several O-glycans but
no N-glycan. The Rh complex appears to aid, but is not essential for,
the correct insertion of GPB in RBC membranes. In
S
N90; E
Cat II and III
Cys) (Figure 
The Evans antigen is expressed on D
) found in persons of African
ancestry has been defined.