Abnormal Beta and Gamma Sialoglycoprotein Associated with the
Low-Frequency Antigen Ls

Macdonald, E.B.; Condon, Jennifer A.; Ford, D. S.; Fisher, B; Gerns, L.M.

doi:10.1159/000461138

Cited by 6 publications

(6 citation statements)

References 8 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…GPC.An", GPC.Dh", GPC.Ls" and GPC.Wb, and thus is located at the N-terminal domains of these glycoproteins (Reid et al, 1985;Macdonad & Gerns, 1986;Dahr et al, 1987;Telen & Bolk, 1987;Dahr et al, 1988Dahr et al, , 1989Daniels et af., 1988;McShane & Chung, 1989;Macdonald et al, 1990;Spring, 1991). Ge4 is also present at the N-terminal domain of the trypsin-resistant domain of GPC.Ge (Telen & Bolk, 1987;Dahr et af., 1988;Daniels et al, 1988;McShane & Chung, 1989).…”

Section: Humanmentioning

confidence: 99%

“…The fact that the Ls" antigen is a consequence of the novel amino acid sequence on GPC.Ls" and GPD.Ls", which arises from the nucleotides at the boundary of the two copies of exon 3 in the GYPC.Ls' gene, has been demonstrated by using a synthetic peptide (TPTIMDTV-VTAEPDPG) specifically to inhibit the activity of anti-Lsa (King et al, 1991). Since GPC.Ls" molecules have amino acid residues encoded by duplicate copies of exon 3, both the GPC.Lsd and GPD.Ls" variants have two copies of the Ge3 antigen (Macdonald et al, 1990; see Fig. 2).…”

Section: Molecular Basis Of Gpcge Gpc Yus and Gpcls"mentioning

confidence: 99%

See 1 more Smart Citation

Molecular basis of glycophorin C variants and their associated blood group antigens

Reid

Spring

1994

Transfusion Medicine

View full text Add to dashboard Cite

The normal and variant forms of GPC and GPD molecules carry antigens of the Gerbich blood group system. This blood group system comprises three high-incidence antigens (Ge2, Ge3 and Ge4) and four low-incidence antigens (Wb, Lsa, Dha and Ana). Erythrocytes of the Ge and Yus phenotypes lack normal GPC and GPD molecules but express variant molecules (denoted GPC.Ge, GPC.Yus, respectively) that functionally substitute for normal GPC and GPD in the membrane. Leach phenotype cells lack GPC and GPD molecules and are elliptocytic in shape with a membrane that is less deformable than that of normal cells. The Lsa antigen is expressed on higher molecular-weight variants of GPC (GPC.Lsa) and GPD (GPD.Lsa). Wb, Dha and Ana antigens arise from point mutations in the GYPC gene and are expressed on GPC.Wb, GPC.Dha and GPD.Ana, respectively. The structure of each of the variant GPC and GPD molecules and the location of the Gerbich blood group system antigens is discussed. The GYPC gene, located on chromosome 2q14-q21, is 13.5 kb long and comprises four exons. Exons 1, 2 and most of exon 3 encode the N-terminal extracellular domain while the remainder of exon 3 and exon 4 encode transmembrane and cytoplasmic domains of GPC. Exons 2 and 3 are highly homologous, with less than 5% nucleotide divergence. The molecular basis of generation of variation GPC and GPD molecules, and the structure of the GYPC gene from different Leach phenotype individuals, is discussed.

show abstract

Section: Humanmentioning

confidence: 99%

Section: Molecular Basis Of Gpcge Gpc Yus and Gpcls"mentioning

confidence: 99%

Molecular basis of glycophorin C variants and their associated blood group antigens

Reid

Spring

1994

Transfusion Medicine

View full text Add to dashboard Cite

show abstract

“…This arose partly as a result of examining red cells with the rare Leach phenotype that were not agglutinated by a monoclonal antibody with Gespecificity. Subsequently, low frequency antigens Wb, Ls" and Dha have been located on the same gene products, either normal or abnormal forms (Reid ef al., 1985;MacDonald et al, 1990;Spring et al, 1990). The chance of these low frequency antigens occurring in informative families that lack the high frequency antigens is very small; so the genetic linkage has only been demonstrated by immunoblotting techniques.…”

Section: Mnss Blood G R O U P Antigensmentioning

confidence: 99%

Three decades of reference serology*

Giles

1991

Transfusion Medicine

View full text Add to dashboard Cite

I have tried to show that blood group serology developed rapidly out of necessity and demonstrated a high degree of polymorphism on red cells that was unmatched at that time in man. With new knowledge, these observations have proved to be accurate and informative and correlate well with subsequent biochemical and molecular studies on the antigenic structures, in spite of the fact that they were achieved by relatively simple technology. Serology still has the capacity to focus on points of interest and even to solve problems, albeit in conjunction with other modern and more sophisticated techniques. It provides a good discipline for any scientist to make unbiased and objective studies.

show abstract

“…Macdonald et al [90] have shown that the low-frequency antigen Ls" is associated with abnormal forms of Glycophorin C and Glycophorin D, both of which are larger than their normal counterpart. Analysis of genomic DNA from an individual heterozygous for Ls" suggests that the Glycophorin C gene of Ls(a+) individuals contains an additional exon 3 [ fig.…”

Section: Gerbich Antigensmentioning

confidence: 99%

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

Anstee

1990

Vox Sanguinis

120

View full text Add to dashboard Cite

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.

show abstract

Abnormal Beta and Gamma Sialoglycoprotein Associated with the Low-Frequency Antigen Ls

Cited by 6 publications

References 8 publications

Molecular basis of glycophorin C variants and their associated blood group antigens

Molecular basis of glycophorin C variants and their associated blood group antigens

Three decades of reference serology*

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

Contact Info

Product

Resources

About