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 ◽  
...  
Transfusion ◽  
1987 ◽  
Vol 27 (1) ◽  
pp. 61-63 ◽  
Author(s):  
SF Parsons ◽  
G Mallinson ◽  
PA Judson ◽  
DJ Anstee ◽  
MJ Tanner ◽  
...  

1987 ◽  
Vol 244 (3) ◽  
pp. 735-741 ◽  
Author(s):  
S Moore ◽  
C Green

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.


Cells ◽  
2020 ◽  
Vol 9 (4) ◽  
pp. 845
Author(s):  
Glenda M. Davison ◽  
Heather L. Hendrickse ◽  
Tandi E. Matsha

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.


1986 ◽  
Vol 261 (20) ◽  
pp. 9521-9525
Author(s):  
C M Redman ◽  
G Avellino ◽  
S R Pfeffer ◽  
T K Mukherjee ◽  
M Nichols ◽  
...  

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