Loss of Rh Antigen Activity Following the Action of
Phospholipase A(2) on Red Cell Stroma

Hughes-Jones, N.C.; Green, Elizabeth J.; Hunt, V.A.M.

doi:10.1159/000465444

Cited by 2 publications

(2 citation statements)

References 7 publications

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“…Early indications that interaction with phospholipid is required for expression of the D antigen were obtained by Green [125] and by Hughes-Jones et al [126], the latter demonstrating that treatment of red cells with phospholipase AZ resulted in loss of D antigen activity. The association of the Rh complex with membrane phospholipid has also been demonstrated by Kuypers et al [127] who showed that in Rh,,,, cells there is a distortion of the normal phospholipid asymmetry of the lipid bilayer, such that twice the normal amount of phosphatidyl ethanolamine is found in the outer leaflet.…”

Section: Pssociation Of Lipid With the Rh Complexmentioning

confidence: 99%

Blood Group‐Active Surface Molecules of the Human Red Blood Cell

Anstee

1990

Vox Sanguinis

120

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Abstract. The surface of the human red blood cell is dominated by a small number of abundant blood group active proteins. The major proteins are the anion transport protein (band 3) which has AB(H) activity, and Glycophorin A which has MN activity. Band 3 and Glycophorin A are of equal abundance in the normal red cell membrane (approximately lo6 copies of each) and the two proteins may associate together as a complex. The glucose transporter (band 4.5) has AB(H) activity and there are about 5 x lo5 copiedred cell. Several polypeptides associate together to form the Rh complex. The major components of this complex (abundance 1-2 x lo5 copieshed cell) are polypeptides of M, 30,000, polypeptides of MI 45,000-100,000 and Glycophorin B. The antigens of the Rh blood group system appear to be associated with the polypeptides of M, 30,000 and those of M, 45,000-100,000 (the latter also express AB(H) activity). Glycophorin B expresses the blood group 'N' antigen and the Ss antigens. Glycophorins C and D carry the Gerbich antigens and, together, these polypeptides comprise approximately lo5 copiedred cell. The complete protein sequence of all the above-mentioned proteins is known, except for the MI 30,000 and M, 45,000-100,000 polypeptides of the Rh complex for which only partial sequences are available, and Glycophorin D, the sequence of which can be inferred from that of Glycophorin C . Several of the minor blood group active proteins at the red cell surface (abundance 4 . 2 x 104/red cell) have been the subject of recent studies. The polypeptide expressing Cromer-related blood group antigens has been identified as decay-accelerating factor and that carrying the Ina/Inb antigens as CD44. The protein sequence of both of these proteins has been deduced form nucleotide sequencing. The polypeptides expressing Kell antigens, Lutheran antigens, Fy antigens, and LW antigens have also been identified and partially characterised.

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Section: Pssociation Of Lipid With the Rh Complexmentioning

confidence: 99%

Blood Group‐Active Surface Molecules of the Human Red Blood Cell

Anstee

1990

Vox Sanguinis

120

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“…Since the discovery of the Rh system, there have been numerous attempts to isolate the antigen but all efforts have been thwarted by the fact that the D epitope is extremely labile and is lost as soon as the Rh molecule is removed from its lipid environment in the red cell membrane (Hughes-Jones et al, 1975). The breakthrough came when Moore et al (1982) found that the epitope was stabilized if it was first combined with antibody.…”

mentioning

confidence: 99%

Quantitation and the Rh blood group system*

Hughes‐Jones

1991

Transfusion Medicine

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Loss of Rh Antigen Activity Following the Action of Phospholipase A(2) on Red Cell Stroma

Cited by 2 publications

References 7 publications

Blood Group‐Active Surface Molecules of the Human Red Blood Cell

Blood Group‐Active Surface Molecules of the Human Red Blood Cell

Quantitation and the Rh blood group system*

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