Blood Group Antigens in Relation to Chemical and Structural Properties of the Red Cell Membrane

Vox Sanguinis ◽  
1968 ◽  
Vol 15 (2) ◽  
pp. 81-101 ◽  
Author(s):  
P. Zahler
Keyword(s):  
Cell Membrane ◽  
Structural Properties ◽  
Blood Group ◽  
Blood Group Antigens ◽  
Red Cell ◽  
Red Cell Membrane

scholarly journals Do Blood Group Antigens and the Red Cell Membrane Influence Human Immunodeficiency Virus Infection?

Cells ◽  
2020 ◽  
Vol 9 (4) ◽  
pp. 845
Author(s):  
Glenda M. Davison ◽  
Heather L. Hendrickse ◽  
Tandi E. Matsha
Keyword(s):  
Human Immunodeficiency Virus ◽  
Cell Membrane ◽  
Hiv Infection ◽  
Blood Group ◽  
Human Populations ◽  
Blood Group Antigens ◽  
Red Cell ◽  
Red Cell Membrane ◽  
Geographical Regions ◽  
Immunodeficiency Virus

The expression of blood group antigens varies across human populations and geographical regions due to natural selection and the influence of environment factors and disease. The red cell membrane is host to numerous surface antigens which are able to influence susceptibility to disease, by acting as receptors for pathogens, or by influencing the immune response. Investigations have shown that Human Immunodeficiency Virus (HIV) can bind and gain entry into erythrocytes, and therefore it is hypothesized that blood groups could play a role in this process. The ABO blood group has been well studied. However, its role in HIV susceptibility remains controversial, while other blood group antigens, and the secretor status of individuals, have been implicated. The Duffy antigen is a chemokine receptor that is important in the inflammatory response. Those who lack this antigen, and type as Duffy null, could therefore be susceptible to HIV infection, especially if associated with neutropenia. Other antigens including those in the Rh, Lutheran and OK blood group systems have all been shown to interact with HIV. More recently, experiments show that cells which overexpress the Pk antigen appear to be protected against infection. These reports all demonstrate that red cell antigens interact and influence HIV infection. However, as the red cell membrane is complex and the pathogenesis of HIV multi-factorial, the role of blood group antigens cannot be studied in isolation.

scholarly journals Kell blood group antigens are part of a 93,000-dalton red cell membrane protein.

1986 ◽  
Vol 261 (20) ◽  
pp. 9521-9525
Author(s):  
C M Redman ◽  
G Avellino ◽  
S R Pfeffer ◽  
T K Mukherjee ◽  
M Nichols ◽  
...  
Keyword(s):  
Cell Membrane ◽  
Membrane Protein ◽  
Blood Group ◽  
Blood Group Antigens ◽  
Red Cell ◽  
Red Cell Membrane ◽  
Cell Membrane Protein

Modelling the structure of the red cell membraneThis paper is one of a selection of papers published in a Special Issue entitled CSBMCB 53rd Annual Meeting — Membrane Proteins in Health and Disease, and has undergone the Journal’s usual peer review process.

2011 ◽  
Vol 89 (2) ◽  
pp. 200-215 ◽  
Author(s):  
Nicholas M. Burton ◽  
Lesley J. Bruce
Keyword(s):  
Cell Membrane ◽  
Cell Function ◽  
Protein Complexes ◽  
Peer Review Process ◽  
Homology Modelling ◽  
Extensive Study ◽  
Blood Group Antigens ◽  
Red Cell ◽  
Oligomeric State ◽  
Red Cell Membrane

The red cell membrane has long been the focus of extensive study. The macromolecules embedded within the membrane carry the blood group antigens and perform many functions including the vital task of gas exchange. Links between the intramembrane macromolecules and the underlying cytoskeleton stabilize the biconcave morphology of the red cell and allow deformation during microvascular transit. Much is now known about the proteins of the red cell membrane and how they are organised. In many cases we have an understanding of which proteins are expressed, the number of each protein per cell, their oligomeric state(s), and how they are collected in large multi-protein complexes. However, our typical view of these structures is as cartoon shapes in schematic figures. In this study we have combined knowledge of the red cell membrane with a wealth of protein structure data from crystallography, NMR, and homology modelling to generate the first, tentative models of the complexes which link the membrane to the cytoskeleton. Measurement of the size of these complexes and comparison with known cytoskeletal distance parameters suggests the idea of interaction between the membrane complexes, which may have profound implications for understanding red cell function and deformation.

scholarly journals The human Kell blood group binds the erythroid 4.1R protein: new insights into the 4.1R-dependent red cell membrane complex

2015 ◽  
Vol 171 (5) ◽  
pp. 862-871 ◽  
Author(s):  
Slim Azouzi ◽  
Emmanuel Collec ◽  
Narla Mohandas ◽  
Xiuli An ◽  
Yves Colin ◽  
...  
Keyword(s):  
Cell Membrane ◽  
Blood Group ◽  
Red Cell ◽  
Red Cell Membrane ◽  
Membrane Complex ◽  
Cell Membrane Complex

Evidence that the Lub blood group antigen is located on red cell membrane glycoproteins of 85 and 78 kd

Transfusion ◽  
1987 ◽  
Vol 27 (1) ◽  
pp. 61-63 ◽  
Author(s):  
SF Parsons ◽  
G Mallinson ◽  
PA Judson ◽  
DJ Anstee ◽  
MJ Tanner ◽  
...  
Keyword(s):  
Cell Membrane ◽  
Blood Group ◽  
Blood Group Antigen ◽  
Red Cell ◽  
Membrane Glycoproteins ◽  
Red Cell Membrane

scholarly journals The identification of specific Rhesus-polypeptide-blood-group-ABH-active-glycoprotein complexes in the human red-cell membrane

1987 ◽  
Vol 244 (3) ◽  
pp. 735-741 ◽  
Author(s):  
S Moore ◽  
C Green
Keyword(s):  
Cell Membrane ◽  
Blood Group ◽  
Immune Complexes ◽  
Polyacrylamide Gel Electrophoresis ◽  
Red Cells ◽  
Red Cell ◽  
Red Cell Membrane ◽  
Blood Group A ◽  
Group A ◽  
Blood Group Abh

1. RhD,c and E immune complexes isolated from 3H- and 125I-surface-radiolabelled and unlabelled intact human red cells were analysed by SDS/polyacrylamide-gel electrophoresis. 2. Apparent Mr values of 31,900 for RhD polypeptide and 33,100 for Rhc,E polypeptide were obtained under both reducing and non-reducing conditions. Glycosylation of RhD,c and E polypeptides was not detected. 3. RhD,c and E immune complexes also contain a glycoprotein component. RhD glycoprotein (apparent Mr 45,000-100,000) is distinct from Rhc,E glycoprotein(s) (apparent Mr 35,000-65,000). Rh (Rhesus) glycoprotein carbohydrate moieties are susceptible to endo-beta-galactosidase digestion and carry blood-group-ABH determinants. This suggests the presence of polylactosaminoglycan-type structures. 4. Rh glycoproteins are not present in Rh immune complexes as a result of non-specific adsorption of membrane glycoproteins during the membrane-solubilization phase of immune-complex isolation because RhD immune complexes isolated from a 1:1 (v/v) mixture of Acde/cde and OcDE/cDE red cells do not contain blood-group-A-active glycoprotein. 5. Blood-group-A immune complexes isolated from group-A red cells of the appropriate Rh phenotypes contain the 31,900- and 33,100-apparent-Mr Rh polypeptides. 6. It was concluded from the above evidence that non-covalent Rh-glycoprotein-Rh-polypeptide complexes exist in the native red-cell membrane. 7. The 31,900- and 33,100-apparent-Mr Rh polypeptides are absent from blood-group-A immune complexes isolated from regulator type Rhnull cells (donor A.L.), but are replaced by a 33,800-apparent-Mr Rhnull-specific polypeptide (Rhnull polypeptide). It is suggested that Rhnull polypeptide is an aberrant product of the Rh gene complex.

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