GYPA

Last updated
GYPA
Protein GYPA PDB 1afo.png
Available structures
PDB Human UniProt search: PDBe RCSB
Identifiers
Aliases GYPA , CD235a, GPA, GPErik, GPSAT, HGpMiV, HGpMiXI, HGpSta(C), MN, MNS, PAS-2, glycophorin A (MNS blood group)
External IDs HomoloGene: 48076 GeneCards: GYPA
Gene location (Human)
Ideogram human chromosome 4.svg
Chr. Chromosome 4 (human) [1]
Human chromosome 4 ideogram.svg
HSR 1996 II 3.5e.svg
Red rectangle 2x18.png
Band 4q31.21Start144,109,303 bp [1]
End144,870,953 bp [1]
RNA expression pattern
PBB GE GYPA 205838 at fs.png

PBB GE GYPA 211820 x at fs.png

PBB GE GYPA 205837 s at fs.png
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez

2993

n/a

Ensembl

ENSG00000170180

n/a

UniProt

P02724

n/a

RefSeq (mRNA)

NM_001308187
NM_001308190
NM_002099

n/a

RefSeq (protein)

NP_001295116
NP_001295119
NP_002090

n/a

Location (UCSC) Chr 4: 144.11 – 144.87 Mb n/a
PubMed search [2] n/a
Wikidata
View/Edit Human

Glycophorin A (MNS blood group), also known as GYPA, is a protein which in humans is encoded by the GYPA gene. [3] GYPA has also recently been designated CD235a (cluster of differentiation 235a).

Protein biological molecule consisting of chains of amino acid residues

Proteins are large biomolecules, or macromolecules, consisting of one or more long chains of amino acid residues. Proteins perform a vast array of functions within organisms, including catalysing metabolic reactions, DNA replication, responding to stimuli, providing structure to cells and organisms, and transporting molecules from one location to another. Proteins differ from one another primarily in their sequence of amino acids, which is dictated by the nucleotide sequence of their genes, and which usually results in protein folding into a specific three-dimensional structure that determines its activity.

Gene basic physical and functional unit of heredity

In biology, a gene is a sequence of nucleotides in DNA or RNA that codes for a molecule that has a function. During gene expression, the DNA is first copied into RNA. The RNA can be directly functional or be the intermediate template for a protein that performs a function. The transmission of genes to an organism's offspring is the basis of the inheritance of phenotypic trait. These genes make up different DNA sequences called genotypes. Genotypes along with environmental and developmental factors determine what the phenotypes will be. Most biological traits are under the influence of polygenes as well as gene–environment interactions. Some genetic traits are instantly visible, such as eye color or number of limbs, and some are not, such as blood type, risk for specific diseases, or the thousands of basic biochemical processes that constitute life.

The cluster of differentiation is a protocol used for the identification and investigation of cell surface molecules providing targets for immunophenotyping of cells. In terms of physiology, CD molecules can act in numerous ways, often acting as receptors or ligands important to the cell. A signal cascade is usually initiated, altering the behavior of the cell. Some CD proteins do not play a role in cell signaling, but have other functions, such as cell adhesion. CD for humans is numbered up to 371.

Contents

Function

Glycophorins A (GYPA; this protein) and B (GYPB) are major sialoglycoproteins of the human erythrocyte membrane which bear the antigenic determinants for the MN and Ss blood groups. In addition to the M or N and S or s antigens, that commonly occur in all populations, about 40 related variant phenotypes have been identified. These variants include all the variants of the Miltenberger complex and several isoforms of Sta; also, Dantu, Sat, He, Mg, and deletion variants Ena, S-s-U- and Mk. Most of the variants are the result of gene recombinations between GYPA and GYPB. [3]

GYPB protein-coding gene in the species Homo sapiens

Glycophorin B also known as sialoglycoprotein delta and SS-active sialoglycoprotein is a protein which in humans is encoded by the GYPB gene. GYPB has also recently been designated CD235b.

Genomics

GypA, GypB and GypE are members of the same family and are located on the long arm of chromosome 4 (chromosome 4q31). The family evolved via two separate gene duplication events. The initial duplication gave rise to two genes one of subsequently evolved into GypA and the other which give rise via a second duplication event to GypB and GypE. These events appear to have occurred within a relatively short time span. The second duplication appears to have occurred via an unequal crossing over event.

The GypA gene itself consists of 7 exons and has 97% sequence homology with GypB and GypE from the 5' untranslated transcription region (UTR) to the coding sequence encoding the first 45 amino acids. The exon at this point encodes the transmembrane domain. Within the intron downstream of this pint is an Alu repeat. The cross over event which created the genes ancestral to GypA and GypB/E occurred within this region.

GypA can be found in all primates. GypB can be found only in gorillas and some of the higher primates suggesting that the duplication events occurred only recently.

Gorilla genus of mammals

Gorillas are ground-dwelling, predominantly herbivorous apes that inhabit the forests of central Sub-Saharan Africa. The genus Gorilla is divided into two species: the eastern gorillas and the western gorillas, and either four or five subspecies. They are the largest living primates. The DNA of gorillas is highly similar to that of humans, from 95 to 99% depending on what is included, and they are the next closest living relatives to humans after the chimpanzees and bonobos.

Molecular biology

There are about one million copies of this protein per erythrocyte. [Reference needed]

Blood groups

The MNS blood group was the second set of antigens discovered. M and N were identified in 1927 by Landsteiner and Levine. S and s in were described later in 1947.

The frequencies of these antigens are

White people is a racial classification specifier, used mostly and often exclusively for people of European descent; depending on context, nationality, and point of view. The term has at times been expanded to encompass persons of Middle Eastern and North African descent, persons who are often considered non-white in other contexts. The usage of "white people" or a "white race" as nomenclature for European populations - indicated by their light skin, among other physical characteristics, and contrasting with "black people", Amerindians, and other "colored" people or "persons of color" - originated in the 17th century. It was only during the 19th century that the category of white people was transformed in a quasi-scientific system of race and skin color relations. The term "Caucasian" is sometimes used as a synonym for "white" in its racial sense and sometimes to refer to a larger racial category that includes white people among other groups.

Negroid grouping of human beings historically regarded as a biological taxon

Negroid is a grouping of human beings historically regarded as a biological taxon. The term has been used by forensic and physical anthropologists to refer to individuals and populations that share certain morphological and skeletal traits that are frequent among populations in most of Sub-Saharan Africa and isolated parts of South and Southeast Asia (Negritos). Within Africa, a racial dividing line separating Caucasoid physical types from Negroid physical types was held to have existed, with Negroid groups forming most of the population south of the area which stretched from the southern Sahara desert in the west to the African Great Lakes in the southeast.

Molecular medicine

Transfusion medicine

The M and N antigens differ at two amino acid residues: the M allele has serine at position 1 (C at nucleotide 2) and glycine at position 5 (G at nucleotide 14) while the N allele has leucine at position 1 (T at nucleotide 2) and glutamate at position 5 (A at nucleotide 14). Both glycophorin A and B bind the Vicia graminea anti-N lectin.

There are about 40 known variants in the MNS blood group system. These have arisen largely as a result of mutations within the 4 kb region coding for the extracellular domain. These include the antigens Mg, Dantu, Henshaw (He), Miltenberger, Nya, Osa, Orriss (Or), Raddon (FR) and Stones (Sta). Chimpanzees also have an MN blood antigen system. [4] In chimpanzees M reacts strong but N only weakly.

Null mutants

In individuals who lack both glycophorin A and B the phenotype has been designated Mk. [5]

Dantu antigen

The Dantu antigen was described in 1984. [6] The Dantu antigen has an apparent molecular weight of 29 kiloDaltons (kDa) and 99 amino acids. The first 39 amino acids of the Dantu antigen are derived from glycophorin B and residues 40-99 are derived from glycophorin A. Dantu is associated with very weak s antigen, a protease-resistant N antigen and either very weak or no U antigen. There are at least three variants: MD, NE and Ph. [7] The Dantu phenotype occurs with a frequency of Dantu phenotype is ~0.005 in American Blacks and < 0.001 in Germans. [8]

Henshaw antigen

The Henshaw (He) antigen is due to a mutation of the N terminal region. There are three differences in the first three amino acid residues: the usual form has Tryptophan 1-Serine-Threonine-Serine-Glycine 5 while Henshaw has Leucine 1-Serine-Threonine-Threonine-Glutamate 5. This antigen is rare in Caucasians but occurs at a frequency of 2.1% in US and UK of African origin. It occurs at the rate of 7.0% in blacks in Natal [9] and 2.7% in West Africans. [10] At least 3 variants of this antigen have been identified.

Miltenberger subsystem

The Miltenberger (Mi) subsystem originally consisting of five phenotypes (Mia, Vw, Mur, Hil and Hut) [11] now has 11 recognised phenotypes numbered I to XI (The antigen 'Mur' is named after to the patient the original serum was isolated from - a Mrs Murrel.) The name originally given to this complex refers to the reaction erythrocytes gave to the standard Miltenberger antisera used to test them. The subclasses were based on additional reactions with other standard antisera.

Mi-I (Mia), Mi-II(Vw), Mi-VII and Mi-VIII are carried on glycophorin A. Mi-I is due to a mutation at amino acid 28 (threonine to methionine: C→T at nucleotide 83) resulting in a loss of the glycosylation at the asparagine26 residue. [12] [13] Mi-II is due to a mutation at amino acid 28 (threonine to lysine:C->A at nucleotide 83). [13] Similar to the case of Mi-I this mutation results in a loss of the glycosylation at the asparagine 26 residue. This alteration in glycoslation is detectable by the presence of a new 32kDa glycoprotein stainable with PAS. [14] Mi-VII is due to a double mutation in glycophorin A converting an arginine residue into a threonine residue and a tyrosine residue into a serine at the positions 49 and 52 respectively. [15] The threonine-49 residue is glycosylated. This appears to be the origin of one of the Mi-VII specific antigens (Anek) which is known to lie between residues 40-61 of glycophorin A and comprises sialic acid residue(s) attached to O-glycosidically linked oligosaccharide(s). This also explains the loss of a high frequency antigen ((EnaKT)) found in normal glycophorin A which is located within the residues 46-56. Mi-VIII is due to a mutation at amino acid residue 49 (arginine->threonine). [16] M-VIII shares the Anek determinant with MiVII. [17] Mi-III, Mi-VI and Mi-X are due to rearrangements of glycophorin A and B in the order GlyA (alpha)-GlyB (delta)-GlyA (alpha). [18] Mil-IX in contrast is a reverse alpha-delta-alpha hybrid gene. [19] Mi-V, MiV(J.L.) and Sta are due to unequal but homologous crossing-over between alpha and delta glycophorin genes. [20] The MiV and MiV(J.L.) genes are arranged in the same 5' alpha-delta 3' frame whereas Sta gene is in a reciprocal 5'delta-alpha 3' configuration.

The incidence of Mi-I in Thailand is 9.7%. [21]

Peptide constructs representative of Mia mutations MUT and MUR have been attached onto red blood cells (known as kodecytes) and are able to detect antibodies against these Miltenberger antigens [22] [23] [24]

Although uncommon in Caucasians (0.0098%) and Japanese (0.006%), the frequency of Mi-III is exceptionally high in several Taiwanese aboriginal tribes (up to 90%). In contrast its frequency is 2-3% in Han Taiwanese (Minnan). The Mi-III phenotype occurs in 6.28% of Hong Kong Chinese. [25]

Mi-IX (MNS32) occurs with a frequency of 0.43% in Denmark. [26]

Stone's antigen

Stones (Sta) has been shown to be the product of a hybrid gene of which the 5'-half is derived from the glycophorin B whereas the 3'-half is derived from the glycophorin A. Several isoforms are known. This antigen is now considered to be part of the Miltenberger complex.

Sat antigen

A related antigen is Sat. This gene has six exons of which exon I to exon IV are identical to the N allele of glycophorin A whereas its 3' portion, including exon V and exon VI, are derived from the glycophorin B gene. The mature protein SAT protein contains 104 amino acid residues.

Orriss antigen

Orriss (Or) appears to be a mutant of glyphorin A but its precise nature has not yet been determined. [27]

Mg antigen

The Mg antigen is carried on glycophorin A and lacks three O-glycolated side chains. [28]

Os antigen

Osa (MNS38) is due to a mutation at nucleotide 273 (C->T) lying within exon 3 resulting in the replacement of a proline residue with a serine. [29]

Ny antigen

Nya (MNS18) is due to a mutation at nucleotide 194 (T->A) which results in the substitution of an aspartate residue with a glutamate. [29]

Reactions

Anti-M although occurring naturally has rarely been implicated in transfusion reactions. Anti-N is not considered to cause transfusion reactions. Severe reactions have been reported with anti-Miltenberger. Anti Mi-I (Vw) and Mi-III has been recognised as a cause of haemolytic disease of the newborn. [30] Raddon has been associated with severe transfusion reactions. [31]

Relevance for infection

The Wright b antigen (Wrb) is located on glycophorin A and acts as a receptor for the malaria parasite Plasmodium falciparum . [32] Cells lacking glycophorins A (Ena) are resistant to invasion by this parasite. [33]

The erythrocyte binding antigen 175 of P. falciparum recognises the terminal Neu5Ac(alpha 2-3)Gal-sequences of glycophorin A. [34]

Several viruses bind to glycophorin A including hepatitis A virus (via its capsid), [35] bovine parvovirus , [36] Sendai virus , [37] influenza A and B , [38] group C rotavirus , [39] encephalomyocarditis virus [40] and reovirus es. [41]

See also

Related Research Articles

Glycophorin C plays a functionally important role in maintaining erythrocyte shape and regulating membrane material properties, possibly through its interaction with protein 4.1. Moreover, it has previously been shown that membranes deficient in protein 4.1 exhibit decreased content of glycophorin C. It is also an integral membrane protein of the erythrocyte and acts as the receptor for the Plasmodium falciparum protein PfEBP-2.

Duffy antigen system protein-coding gene in the species Homo sapiens

Duffy antigen/chemokine receptor (DARC), also known as Fy glycoprotein (FY) or CD234, is a protein that in humans is encoded by the DARC gene.

Complement receptor 1 protein-coding gene in the species Homo sapiens

Complement receptor type 1 (CR1) also known as C3b/C4b receptor or CD35 is a protein that in humans is encoded by the CR1 gene.

CD36 protein-coding gene in the species Homo sapiens

CD36, also known as platelet glycoprotein 4, fatty acid translocase (FAT), scavenger receptor class B member 3 (SCARB3), and glycoproteins 88 (GP88), IIIb (GPIIIB), or IV (GPIV) is a protein that in humans is encoded by the CD36 gene. The CD36 antigen is an integral membrane protein found on the surface of many cell types in vertebrate animals. It imports fatty acids inside cells and is a member of the class B scavenger receptor family of cell surface proteins. CD36 binds many ligands including collagen, thrombospondin, erythrocytes parasitized with Plasmodium falciparum, oxidized low density lipoprotein, native lipoproteins, oxidized phospholipids, and long-chain fatty acids.

ABO blood group system Classification of blood types

The ABO blood group system is used to denote the presence of one, both, or neither of the A and B antigens on erythrocytes. In human blood transfusions it is the most important of the 36 different blood type classification systems currently recognized. A very rare mismatch in this, or any other serotype, can cause a serious, potentially fatal, adverse reaction after a transfusion, or a contra-indicated immune response to an organ transplant. The associated anti-A and anti-B antibodies are usually IgM antibodies, which are produced in the first years of life by sensitization to environmental substances, such as food, bacteria, and viruses.

The Kell antigen system is a group of antigens on the human red blood cell surface which are important determinants of blood type and are targets for autoimmune or alloimmune diseases which destroy red blood cells. Kell can be noted as K, k, or Kp. The Kell antigens are peptides found within the Kell protein, a 93-kilodalton transmembrane zinc-dependent endopeptidase which is responsible for cleaving endothelin-3.

McLeod syndrome

McLeod syndrome is an X-linked recessive genetic disorder that may affect the blood, brain, peripheral nerves, muscle, and heart. It is caused by a variety of recessively inherited mutations in the XK gene on the X chromosome. The gene is responsible for producing the Kx protein, a secondary supportive protein for the Kell antigen on the red blood cell surface.

Animal erythrocytes have cell surface antigens that undergo polymorphism and give rise to blood types. Antigens from the human ABO blood group system are also found in apes and Old World monkeys, and the system traces back to the origin of hominoids. Other animal blood sometimes agglutinates with human blood group reagents, but the structure of the blood group antigens in animals is not always identical to those typically found in humans. The classification of most animal blood groups therefore uses different blood typing systems to those used for classification of human blood.

The MNS antigen system is a human blood group system based upon two genes on chromosome 4. There are currently 46 antigens in the system, but the five most important are called M, N, S, s, and U.

The LW blood system was first described by Landsteiner and Wiener in 1940. It was often confused with the Rh system, not becoming a separate antigen system until 1982. The LW and RhD antigens are genetically independent though they are phenotypically related and the LW antigen is expressed more strongly on RhD positive cells than on RhD negative cells. In most populations, the antithetical LW antigens, LWa and LWb are present as very high and very low frequency, respectively.

Fucosyltransferase 3 protein-coding gene in the species Homo sapiens

Galactoside 3(4)-L-fucosyltransferase is an enzyme that in humans is encoded by the FUT3 gene.

<i>RHCE</i> (gene) protein-coding gene in the species Homo sapiens

Blood group Rh(CE) polypeptide is a protein that in humans is encoded by the RHCE gene. RHCE has also recently been designated CD240CE.

RHAG protein-coding gene in the species Homo sapiens

Rh-associated glycoprotein (RHAG) is an ammonia transporter protein that in humans is encoded by the RHAG gene. RHAG has also recently been designated CD241. Mutations in the RHAG gene can cause stomatocytosis.

ART4 protein-coding gene in the species Homo sapiens

Ecto-ADP-ribosyltransferase 4 is an enzyme that in humans is encoded by the ART4 gene. ART4 has also been designated as CD297.

ERMAP protein-coding gene in the species Homo sapiens

Erythroid membrane-associated protein is a protein that in humans is responsible for the Scianna blood group system, and is encoded by the ERMAP gene.

GYPE protein-coding gene in the species Homo sapiens

Glycophorin-E is a protein that in humans is encoded by the GYPE gene.

ABO (gene) protein-coding gene in the species Homo sapiens

Histo-blood group ABO system transferase is an enzyme with glycosyltransferase activity, which is encoded by the ABO gene in humans. It is ubiquitously expressed in many tissues and cell types. ABO determines the ABO blood group of an individual by modifying the oligosaccharides on cell surface glycoproteins. Variations in the sequence of the protein between individuals determine the type of modification and the blood group. The ABO gene also contains one of 27 SNPs associated with increased risk of coronary artery disease.

The BGMUT Database documents allelic variations in the genes encoding for human blood group systems. It was set up in 1999 through an initiative of the Human Genome Variation Society (HGVS). Since 2006, it has been a part of the dbRBC resource of NCBI at the NIH. In addition to being a repository of the genetic variations of the blood group antigen-encoding genes, the database also provides information on the blood group systems, the genes that encode them, the serological phenotypes associated with the alleles of the genes, etc. Information on genetic variations in some non-human orthologous genes is also provided.

RHD (gene) protein-coding gene in the species Homo sapiens

Rh blood group, D antigen also known as Rh polypeptide 1 (RhPI) or cluster of differentiation 240D (CD240D) is a protein that in humans is encoded by the RHD gene.

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000170180 - Ensembl, May 2017
  2. ↑ "Human PubMed Reference:".
  3. 1 2 "Entrez Gene: GYPA glycophorin A (MNS blood group)".
  4. ↑ Blumenfeld OO, Adamany AM, Puglia KV, Socha WW (April 1983). "The chimpanzee M blood-group antigen is a variant of the human M-N glycoproteins". Biochem. Genet. 21 (3–4): 333–48. doi:10.1007/BF00499143. PMID   6860297.
  5. ↑ Tokunaga E, Sasakawa S, Tamaka K, Kawamata H, Giles CM, Ikin EW, Poole J, Anstee DJ, Mawby W, Tanner MJ (December 1979). "Two apparently healthy Japanese individuals of type MkMk have erythrocytes which lack both the blood group MN and Ss-active sialoglycoproteins". J. Immunogenet. 6 (6): 383–90. doi:10.1111/j.1744-313X.1979.tb00693.x. PMID   521666.
  6. ↑ Contreras M, Green C, Humphreys J, Tippett P, Daniels G, Teesdale P, Armitage S, Lubenko A (1984). "Serology and genetics of an MNSs-associated antigen Dantu". Vox Sang. 46 (6): 377–86. doi:10.1111/j.1423-0410.1984.tb00102.x. PMID   6431691.
  7. ↑ Dahr W, Pilkington PM, Reinke H, Blanchard D, Beyreuther K (May 1989). "A novel variety of the Dantu gene complex (DantuMD) detected in a Caucasian". Blut. 58 (5): 247–53. doi:10.1007/BF00320913. PMID   2470445.
  8. ↑ Unger P, Procter JL, Moulds JJ, Moulds M, Blanchard D, Guizzo ML, McCall LA, Cartron JP, Dahr W (July 1987). "The Dantu erythrocyte phenotype of the NE variety. II. Serology, immunochemistry, genetics, and frequency". Blut. 55 (1): 33–43. doi:10.1007/BF00319639. PMID   3607294.
  9. ↑ Reid ME, Lomas-Francis C, Daniels GL, Chen V, Shen J, Ho YC, Hare V, Batts R, Yacob M, Smart E (1995). "Expression of the erythrocyte antigen Henshaw (He; MNS6): serological and immunochemical studies". Vox Sang. 68 (3): 183–6. doi:10.1111/j.1423-0410.1995.tb03924.x. PMID   7625076.
  10. ↑ Chalmers JN, Ikin EW, Mourant AE (July 1953). "A study of two unusual blood-group antigens in West Africans". Br Med J. 2 (4829): 175–7. doi:10.1136/bmj.2.4829.175. PMC   2028931  Lock-green.svg. PMID   13059432.
  11. ↑ Cleghorn TE (1966). "A memorandum on the Miltenberger blood groups". Vox Sang. 11 (2): 219–22. doi:10.1111/j.1423-0410.1966.tb04226.x. PMID   5955790.
  12. ↑ Huang CH, Spruell P, Moulds JJ, Blumenfeld OO (July 1992). "Molecular basis for the human erythrocyte glycophorin specifying the Miltenberger class I (MiI) phenotype". Blood. 80 (1): 257–63. PMID   1611092.
  13. 1 2 Dahr W, Newman RA, Contreras M, Kordowicz M, Teesdale P, Beyreuther K, Krüger J (January 1984). "Structures of Miltenberger class I and II specific major human erythrocyte membrane sialoglycoproteins". Eur. J. Biochem. 138 (2): 259–65. doi:10.1111/j.1432-1033.1984.tb07910.x. PMID   6697986.
  14. ↑ Blanchard D, Asseraf A, Prigent MJ, Cartron JP (August 1983). "Miltenberger Class I and II erythrocytes carry a variant of glycophorin A". Biochem. J. 213 (2): 399–404. PMC   1152141  Lock-green.svg. PMID   6615443.
  15. ↑ Dahr W, Beyreuther K, Moulds JJ (July 1987). "Structural analysis of the major human erythrocyte membrane sialoglycoprotein from Miltenberger class VII cells". Eur. J. Biochem. 166 (1): 27–30. doi:10.1111/j.1432-1033.1987.tb13478.x. PMID   2439339.
  16. ↑ Dahr W, Vengelen-Tyler V, Dybkjaer E, Beyreuther K (August 1989). "Structural analysis of glycophorin A from Miltenberger class VIII erythrocytes". Biol. Chem. Hoppe-Seyler. 370 (8): 855–9. doi:10.1515/bchm3.1989.370.2.855. PMID   2590469.
  17. ↑ Dybkjaer E, Poole J, Giles CM (1981). "A new Miltenberger class detected by a second example of Anek type serum". Vox Sang. 41 (5–6): 302–5. doi:10.1111/j.1423-0410.1981.tb01053.x. PMID   6172902.
  18. ↑ Huang CH, Blumenfeld OO (April 1991). "Molecular genetics of human erythrocyte MiIII and MiVI glycophorins. Use of a pseudoexon in construction of two delta-alpha-delta hybrid genes resulting in antigenic diversification". J. Biol. Chem. 266 (11): 7248–55. PMID   2016325.
  19. ↑ Huang CH, Skov F, Daniels G, Tippett P, Blumenfeld OO (November 1992). "Molecular analysis of human glycophorin MiIX gene shows a silent segment transfer and untemplated mutation resulting from gene conversion via sequence repeats". Blood. 80 (9): 2379–87. PMID   1421409.
  20. ↑ Huang CH, Blumenfeld OO (April 1991). "Identification of recombination events resulting in three hybrid genes encoding human MiV, MiV(J.L.), and Sta glycophorins". Blood. 77 (8): 1813–20. PMID   2015404.
  21. ↑ Chandanyingyong D, Pejrachandra S (1975). "Studies on the Miltenberger complex frequency in Thailand and family studies". Vox Sang. 28 (2): 152–5. doi:10.1111/j.1423-0410.1975.tb02753.x. PMID   1114793.
  22. ↑ Heathcote D, Flower R, Henry S (2008). "Development of novel alloantibody screening cells – the first example of the addition of peptide antigens to human red cells using KODE technology. ISBT Regional Congress, Macao SAR China, 2008". (P-303)". Vox Sanguinis. 95 (Suppl 1): 174.
  23. ↑ Heathcote D, Carroll T, Wang JJ, Flower R, Rodionov I, Tuzikov A, Bovin N, Henry S (2010). "Novel antibody screening cells, MUT+Mur kodecytes, created by attaching peptides onto erythrocytes". Transfusion. 50: 635–641. doi:10.1111/j.1537-2995.2009.02480.x.
  24. ↑ Flower R, Lin P-H, Heathcote D, Chan M, Teo D, Selkirk A, Shepherd R, Henry S. Insertion of KODE peptide constructs into red cell membranes: Creating artificial variant MNS blood group antigens. ISBT Regional Congress, Macao SAR China, 2008. (P-396) Vox Sanguinis 2008; 95:Suppl 1, 203-204
  25. ↑ Mak KH, Banks JA, Lubenko A, Chua KM, Torres de Jardine AL, Yan KF (March 1994). "A survey of the incidence of Miltenberger antibodies among Hong Kong Chinese blood donors". Transfusion. 34 (3): 238–41. doi:10.1046/j.1537-2995.1994.34394196622.x. PMID   8146897.
  26. ↑ Skov F, Green C, Daniels G, Khalid G, Tippett P (1991). "Miltenberger class IX of the MNS blood group system". Vox Sang. 61 (2): 130–6. doi:10.1111/j.1423-0410.1991.tb00258.x. PMID   1722368.
  27. ↑ Bacon JM, Macdonald EB, Young SG, Connell T (1987). "Evidence that the low frequency antigen Orriss is part of the MN blood group system". Vox Sang. 52 (4): 330–4. doi:10.1111/j.1423-0410.1987.tb04902.x. PMID   2442891.
  28. ↑ Green C, Daniels G, Skov F, Tippett P (1994). "Mg+ MNS blood group phenotype: further observations". Vox Sang. 66 (3): 237–41. doi:10.1111/j.1423-0410.1994.tb00316.x. PMID   8036795.
  29. 1 2 Daniels GL, Bruce LJ, Mawby WJ, Green CA, Petty A, Okubo Y, Kornstad L, Tanner MJ (May 2000). "The low-frequency MNS blood group antigens Ny(a) (MNS18) and Os(a) (MNS38) are associated with GPA amino acid substitutions". Transfusion. 40 (5): 555–9. doi:10.1046/j.1537-2995.2000.40050555.x. PMID   10827258.
  30. ↑ Rearden A, Frandson S, Carry JB (1987). "Severe hemolytic disease of the newborn due to anti-Vw and detection of glycophorin A antigens on the Miltenberger I sialoglycoprotein by Western blotting". Vox Sang. 52 (4): 318–21. doi:10.1111/j.1423-0410.1987.tb04900.x. PMID   2442890.
  31. ↑ Baldwin ML, Barrasso C, Gavin J (1981). "The first example of a Raddon-like antibody as a cause of a transfusion reaction". Transfusion. 21 (1): 86–9. doi:10.1046/j.1537-2995.1981.21181127491.x. PMID   7466911.
  32. ↑ Ridgwell K, Tanner MJ, Anstee DJ (January 1983). "The Wrb antigen, a receptor for Plasmodium falciparum malaria, is located on a helical region of the major membrane sialoglycoprotein of human red blood cells". Biochem. J. 209 (1): 273–6. PMC   1154085  Lock-green.svg. PMID   6342608.
  33. ↑ Facer CA (November 1983). "Merozoites of P. falciparum require glycophorin for invasion into red cells". Bull Soc Pathol Exot Filiales. 76 (5): 463–9. PMID   6370471.
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