Molecular organization of glycophorin A: Implications for membrane interactions

Welsh, E. Jane; Thom, David; Morris, Edwin R.; Rees, David A.

doi:10.1002/bip.360241210

Cited by 26 publications

(8 citation statements)

References 56 publications

(5 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Glycophorin A has been extensively studied as a model membrane protein (12). It contains 131 amino acids organized into an extracellular, transmembrane and intracellular domain containing about 72, 20 and 39 amino acids, respectively (13).…”

Section: Introductionmentioning

confidence: 99%

The mechanism of production of multiple mRNAs for human glycophorin A

Hamid

Burness

1990

Nucl Acids Res

View full text Add to dashboard Cite

The major sialoglycoprotein in the human red cell surface membrane, glycophorin A is encoded by a single gene. However, this gene gives rise to three species of glycophorin A mRNA of sizes about 1.0, 1.7 and 2.8 kilobases in reticulocytes, foetal liver cells and erythroleukaemic K562 cells. In an investigation of how the three mRNAs originated, we showed by primer extension analysis that all three mRNAs in K562 cells had identical 5' termini and, by nucleotide sequencing of correlated cDNAs, that they had identical coding regions, except for the well-known glycophorin AM-AN polymorphism. However, we found also by sequencing the cDNAs that the mRNAs apparently differed from each other in the lengths of their 3' untranslated regions. This was confirmed by Northern blot analysis which also provided evidence that the three mRNAs originated by use of different polyadenylation signals of which seven were found in the longest cDNA we analyzed.

show abstract

Section: Introductionmentioning

confidence: 99%

The mechanism of production of multiple mRNAs for human glycophorin A

Hamid

Burness

1990

Nucl Acids Res

View full text Add to dashboard Cite

show abstract

“…Numbers denote amino acid residues. The model of Glycophorin A is drawn from Welsh et al [182]. et al [23] report that 78% of O-glycans on Glycophorins are in the form of disialotetrasaccharides, 17% monosialotrisaccharides, and 5% in the form of novel trisialylpentasaccharides.…”

Section: Structure Function and Antigens Of Glycophorins A And Bmentioning

confidence: 99%

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

Anstee¹

1990

Vox Sanguinis

View full text Add to dashboard Cite

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.

show abstract

“…This could be because, close to saturation, not all binding results in intercomplex cross-linking. The relationship between antibody binding and immobilization is in any case likely to be complex as band 3 and probably glycophorin exist in oligomeric states in the membrane (Reithmeier, 1993;Welsh et al, 1985). R1.3 produces significantly less immobilization than the other antibodies.…”

Section: Discussionmentioning

confidence: 99%

Loss of rotational mobility of band 3 proteins in human erythrocyte membranes induced by antibodies to glycophorin A

Che

Cherry

1995

Biophysical Journal

View full text Add to dashboard Cite

The effect of antibodies to glycophorin A on the rotational diffusion of band 3 in human erythrocyte membranes was investigated by transient dichrosim. Three antibodies that recognize different epitopes on the exofacial domain of glycophorin A all strongly reduce the rotational mobility of band 3. The effect is at most only weakly dependent on the distance of the epitope from the membrane surface. The degree of immobilization obtained with two of the antibodies, BRIC14 and R18, is very similar to that produced by antibodies to band 3 itself. Similar results were obtained with membranes stripped of skeletal proteins. Fab fragments and an antibody to glycophorin C had no effect on band 3 rotational mobility. These results rule out a mechanism whereby band 3 rotational immobilization results from enhanced interactions with the membrane skeleton that are mediated by a conformational change in glycophorin A. Rather, they strongly indicate that the antibodies to glycophorin A cross-link existing band 3-glycophorin A complexes that have lifetimes that are long compared with the millisecond time scale of the transient dichroism measurements.

show abstract

Molecular organization of glycophorin A: Implications for membrane interactions

Cited by 26 publications

References 56 publications

The mechanism of production of multiple mRNAs for human glycophorin A

The mechanism of production of multiple mRNAs for human glycophorin A

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

Loss of rotational mobility of band 3 proteins in human erythrocyte membranes induced by antibodies to glycophorin A

Contact Info

Product

Resources

About