Isolation of membrane components associated with human red cell antigens Rh(D), (c̄), (E) and Fya

Moore, Stephen; Woodrow, Christina F.; McClelland, D. B. L.

doi:10.1038/295529a0

Cited by 229 publications

(107 citation statements)

References 18 publications

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“…We could not adequately test this hypothesis in relation to the Rh C/c proteins but, given the close structural similarity of C/c and E/e polypeptides (35) and their possible encoding by a single gene (36), we suspect that autoreactive epitope(s) may prove to be present on C/c as well as E/e. This concept would fit with observations that the C/c and E/e polypeptides share (with p34) a slightly higher apparent molecular mass than the D polypeptide (23,27,28) and with the accumulated serological experience that when RBC autoantibodies exhibit apparent specificity for individual Rh antigens (i.e., those defined by alloantibodies), it has frequently been for E/e or C/c but rarely for D (2,(6)(7)(8)13). Alternatively, it cannot be excluded that p34 and gp37-55 could be distinct from any of the known alloantigen-expressing proteins of the Rh complex but still members of the Rh family.…”

Section: Rbcssupporting

confidence: 53%

“…The 41 -kD bands in lanes A and B (Fig. 6 a) (23). This does not mean, however, that the very dense autoradiographic bands obtained with many of the autoantibody eluates just discussed are nonspecific.…”

Section: Rbcsmentioning

confidence: 90%

“…The possibility that the 31-kD component in the double band (Fig. 4 a) (27) and that these E/e-or C/c-related patterns generally differ from the patterns observed with the Rh(D) polypeptide (23,27,28) or D-related glycoprotein (27). In our hands, allo-anti-e isolated both a 34-kD band indistinguishable from the autoantibody-isolated p34 polypeptide and a polydisperse smear that closely resembled autoantibodyproduced gp37-55 (Fig.…”

Section: Rbcsmentioning

confidence: 99%

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Erythrocyte membrane proteins reactive with human (warm-reacting) anti-red cell autoantibodies.

Leddy¹,

Falany²,

Kissel³

et al. 1993

J. Clin. Invest.

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Immunoglobulin G (IgG) autoantibodies of 20 patients with autoimmune hemolytic anemia (AHA) were used in immunoaffinity assays with surface-radioiodinated human red was not seen in the absence of p34, and both proteins are likely to be members of the Rh family. Indeed, a 34-kD polypeptide band and 37-55-kD polydisperse "smear," isolated concurrently from the same labeled RBCs by IgG allo-anti-e, were indistinguishable from their autoantibody-isolated counterparts and may well be the same protein identified at different epitopes by the auto-and allo-antibodies. Individual AHA patients' autoantibodies isolated p34 and gp37-55, alone or in combination with band 3 (nine cases); strong band 3 alone (five cases); and combinations of band 3 with GPA (six cases). The autoantibodies of three additional patients whose AHA had been induced by a-methyldopa also isolated p34 and gp37-55. (J. Clin. Invest. 1993. 91:1672-1680

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Section: Rbcssupporting

confidence: 53%

Section: Rbcsmentioning

confidence: 90%

Section: Rbcsmentioning

confidence: 99%

See 1 more Smart Citation

Erythrocyte membrane proteins reactive with human (warm-reacting) anti-red cell autoantibodies.

Leddy¹,

Falany²,

Kissel³

et al. 1993

J. Clin. Invest.

View full text Add to dashboard Cite

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“…In contrast, anti-SSEA-1 has a strict requirement for a l-3-linked terminal fucose Hounsell et al, 1981) and anti-I Ma and anti-i Den require terminal galactose residues (Feizi et al, 1971;Tang et al, 1986). Moreover, there remains a question mark as to whether peptide determinants are always resistant to mild periodate treatment, since the Rh(D) antigen of erythrocytes, now thought to be of ipolypeptide nature (Moore et al, 1982), was susceptible to the mildest periodate oxidation conditions (Moskowitz & Treffers, 1950;Morgan & Watkins, 1951).…”

Section: Glycoprotein Oligosaccharides As Major Antigens Of Whole Cellsmentioning

confidence: 99%

Carbohydrates as antigenic determinants of glycoproteins

Feizi

Childs

1987

Biochemical Journal

261

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“…In the transcription-translation coupled system, the plasmids pT7TS-RhD and pT7TS-RhcE directed the synthesis of polypeptides of apparent molecular mass of 31 and 32 kD, respectively (Fig 4, lanes 1 and 2), which were similar in size to that of the RhD and RhCc/Ee proteins of human erythrocytes (Moore et al, 1982;Gahmberg, 1982). The plasmid pT7TS-RhD-D4-6, in which the sequence encoding for the 151 amino acids specified by exons 4-6 of the D protein was lacking, directed the synthesis of a polypeptide of apparent molecular mass of 18-21 kD (Fig 4, lane 3).…”

Section: Coupled Transcription-translation Assaysmentioning

confidence: 99%

A human monoclonal anti‐D antibody which detects a nonconformation‐dependent epitope on the RhD protein by immunoblot

Apoil

Halverson

et al. 1997

Br J Haematol

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Summary.We describe the first human monoclonal anti-D (LOR-15C9) which reacts with a D-specific motif exposed either on a native form on intact D-positive red cells or on a denatured form of the RhD protein (33 kD), and detected by immunoblotting. LOR-15C9 was able to precipitate RhD but not RhcE proteins produced by in vitro transcriptiontranslation assays. The reactivity of the antibody, using panels of red cells with various partial D phenotypes known to lack some D epitopes and corresponding in RHD gene variants, suggested that LOR-15C9 reactivity depends on the portion of the RhD polypeptide encoded by the exon 7 (amino acids 314-358). These findings correlate well with the reactivity of LOR-15C9 with erythrocytes of some nonhuman primates (D gor -positive gorillas), but not of chimpanzee and Old or New World monkeys.In membrane proteins from partial D VI red cells, LOR-15C9 detected two proteins of molecular weight 33 and 21 kD; the presence of the latter was specific for category D VI and presumably represented the product of an alternatively spliced RHD VI transcript in these cells. This is consistent with the finding that LOR-15C9 can precipitate a shortened D protein mutant resulting from in vitro transcriptiontranslation and lacking amino-acids 163-313 encoded by exons 4-6. In addition, a 21 kD band polypeptide was detected by immunoblot in all red cell samples but D ¹¹ , using a rabbit anti-Rh polypeptide antibody (MPC8) raised against the C-terminal domain of Rh proteins. This 21 kD polypeptide most probably results from the translation of an alternatively spliced RHCE gene transcript.This study demonstrates that LOR-15C9 detects an epitope on the RhD protein that is independent of the membrane environment, and therefore could be a useful tool for the study of RhD polypeptides.

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Isolation of membrane components associated with human red cell antigens Rh(D), (c̄), (E) and Fya

Cited by 229 publications

References 18 publications

Erythrocyte membrane proteins reactive with human (warm-reacting) anti-red cell autoantibodies.

Erythrocyte membrane proteins reactive with human (warm-reacting) anti-red cell autoantibodies.

Carbohydrates as antigenic determinants of glycoproteins

A human monoclonal anti‐D antibody which detects a nonconformation‐dependent epitope on the RhD protein by immunoblot

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