Estimation of the Number of Binding Sites for a Murine Monoclonal Anti‐Lu<sup>b</sup> on Human Erythrocytes

Merry, Anthony H.; Gardner, Brigitte; Parsons, Stephen; Anstee, D. J.

doi:10.1111/j.1423-0410.1987.tb04915.x

Cited by 25 publications

(6 citation statements)

References 13 publications

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“…This should have been sufficient to render the mab in excess. The original technique was modified by using affinity-purified antibody and by separating free from bound antibody by centrifugation through a mixture of phthalate esters [19]. The 5 samples of category D' " red cells quantitated here were confirmed as such by C. Lomas, MRC Blood Group Unit [pers.…”

Section: Quantitation Of Cell-bound Antibodymentioning

confidence: 86%

Human Monoclonal Anti-D with Reactivity against Category D^VI Cells Used in Blood Grouping and Determination of the Incidence of the Category D^VI Phenotype in the D^U Population

Leader¹,

Kumpel²,

Poole³

et al. 1990

Vox Sanguinis

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B-lymphoblastoid cell lines transformed by Epstein-Barr virus were produced from cells obtained from a hyperimmunised donor with serum anti-D activity against category D^VI red cells and enriched for this activity by rosetting with category D^VI red cells. Three clones produced IgG1 anti-D and had stable cell growth and continuous secretion of antibody in prolonged culture. The monoclonal antibodies reacted with category D^VI red cells, when assessed manually and in an automated blood grouping system, and are useful blood grouping reagents for the detection of the category D^VI phenotype. Using a radiometric technique, the number of antibody molecules bound to category D^VI red cells from 5 individuals was estimated to range from 2,800 to 11,200 per cell. Five percent of blood donors classed as D^u in the south western region were found to have the category D^VI phenotype.

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Section: Quantitation Of Cell-bound Antibodymentioning

confidence: 86%

Human Monoclonal Anti-D with Reactivity against Category D^VI Cells Used in Blood Grouping and Determination of the Incidence of the Category D^VI Phenotype in the D^U Population

Leader¹,

Kumpel²,

Poole³

et al. 1990

Vox Sanguinis

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“…Site numbers of 1,640-4,070/cell were obtained for Lu(a-b+) cells and 850-1,820 sites/cell for Lu(a+b+) cells [152].…”

Section: Fy Glycoproteinmentioning

confidence: 99%

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

Anstee¹

1990

Vox Sanguinis

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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 10^6 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 10^5 copies/red cell. Several polypeptides associate together to form the Rh complex. The major components of this complex (abundance 1-2 x 10^5 copies/red cell) are polypeptides of M(r) 30,000, polypeptides of M(r) 45,000-100,000 and Glycophorin B. The antigens of the Rh blood group system appear to be associated with the polypeptides of M(r) 30,000 and those of M(r) 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 10^5 copies/red cell. The complete protein sequence of all the above-mentioned proteins is known, except for the M(r) 30,000 and M(r) 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 <1.2 x 10^4 /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 In^a / In^b 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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“…3 Erythrocytes express 500 to 4000 Lu/BCAM molecules on their surface, a quantity that gradually decreases as erythrocytes shed membrane and become increasingly dense during their lifespan. 4,5 Lu/BCAM can interact with the extracellular matrix (ECM) component laminin-a5, allowing the capturing of erythrocytes through this interaction even under flow conditions. 6,7 As the ECM is normally not exposed to circulating erythrocytes, the function of Lu/BCAM on terminally differentiated erythrocytes is currently unclear.…”

Section: Introductionmentioning

confidence: 99%

Glycophorin-C sialylation regulates Lu/BCAM adhesive capacity during erythrocyte aging

et al. 2018

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Key Points• The Lu/BCAM adhesion molecule is gradually activated during erythrocyte aging due to loss of sialic acid on glycophorin-C.• Upon activation, Lu/ BCAM engages a sialic acid-dependent interaction with the extracellular matrix protein laminin-a5.Lutheran/basal cell adhesion molecule (Lu/BCAM) is a transmembrane adhesion molecule expressed by erythrocytes and endothelial cells that can interact with the extracellular matrix protein laminin-a5. In sickle cell disease, Lu/BCAM is thought to contribute to adhesion of sickle erythrocytes to the vascular wall, especially during vaso-occlusive crises.On healthy erythrocytes however, its function is unclear. Here we report that Lu/BCAM is activated during erythrocyte aging. We show that Lu/BCAM-mediated binding to laminin-a5 is restricted by interacting, in cis, with glycophorin-C-derived sialic acid residues. Following loss of sialic acid during erythrocyte aging, Lu/BCAM is released from glycophorin-C and allowed to interact with sialic acid residues on laminin-a5.

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Estimation of the Number of Binding Sites for a Murine Monoclonal Anti‐Lu^b on Human Erythrocytes

Cited by 25 publications

References 13 publications

Human Monoclonal Anti-D with Reactivity against Category D^VI Cells Used in Blood Grouping and Determination of the Incidence of the Category D^VI Phenotype in the D^U Population

Human Monoclonal Anti-D with Reactivity against Category D^VI Cells Used in Blood Grouping and Determination of the Incidence of the Category D^VI Phenotype in the D^U Population

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

Glycophorin-C sialylation regulates Lu/BCAM adhesive capacity during erythrocyte aging

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Estimation of the Number of Binding Sites for a Murine Monoclonal Anti‐Lub on Human Erythrocytes

Cited by 25 publications

References 13 publications

Human Monoclonal Anti-D with Reactivity against Category D^VI Cells Used in Blood Grouping and Determination of the Incidence of the Category D^VI Phenotype in the D^U Population

Human Monoclonal Anti-D with Reactivity against Category D^VI Cells Used in Blood Grouping and Determination of the Incidence of the Category D^VI Phenotype in the D^U Population

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

Glycophorin-C sialylation regulates Lu/BCAM adhesive capacity during erythrocyte aging

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Estimation of the Number of Binding Sites for a Murine Monoclonal Anti‐Lu^b on Human Erythrocytes