scholarly journals Human erythrocyte acetylcholinesterase bears the Yta blood group antigen and is reduced or absent in the Yt(a-b-) phenotype

Blood ◽  
1993 ◽  
Vol 81 (3) ◽  
pp. 815-819 ◽  
Author(s):  
N Rao ◽  
CF Whitsett ◽  
SM Oxendine ◽  
MJ Telen
Keyword(s):  
Membrane Protein ◽  
Blood Group ◽  
Erythrocyte Membrane ◽  
Human Erythrocyte ◽  
Blood Cells ◽  
Phosphatidyl Inositol ◽  
Blood Group Antigen ◽  
Blood Group Antigens ◽  
Relationship Of ◽  
The Relationship

Abstract The Cartwright (Yt) blood group antigens have previously been shown likely to reside on a phosphatidylinositol-linked erythrocyte membrane protein. In this study, an unusual individual whose red blood cells (RBCs) were of the previously unreported Yt(a-b-) phenotype were used, along with normal Yt(a+) cells, to investigate serologically and biochemically the relationship of the Yta antigen to known phosphatidylinositol-linked erythrocyte proteins. Yt(a-b-) RBCs expressed normal amounts of various phosphatidyl-inositol-linked proteins except acetylcholinesterase. Further, human anti-Yta reacted with acetylcholinesterase in immunoprecipitation and immunoblotting studies. Thus, acetylcholinesterase is now identified as the protein bearing the Yt blood group antigens.

Human erythrocyte acetylcholinesterase bears the Yta blood group antigen and is reduced or absent in the Yt(a-b-) phenotype

Blood ◽  
1993 ◽  
Vol 81 (3) ◽  
pp. 815-819
Author(s):  
N Rao ◽  
CF Whitsett ◽  
SM Oxendine ◽  
MJ Telen
Keyword(s):  
Membrane Protein ◽  
Blood Group ◽  
Erythrocyte Membrane ◽  
Human Erythrocyte ◽  
Blood Cells ◽  
Phosphatidyl Inositol ◽  
Blood Group Antigen ◽  
Blood Group Antigens ◽  
Relationship Of ◽  
The Relationship

The Cartwright (Yt) blood group antigens have previously been shown likely to reside on a phosphatidylinositol-linked erythrocyte membrane protein. In this study, an unusual individual whose red blood cells (RBCs) were of the previously unreported Yt(a-b-) phenotype were used, along with normal Yt(a+) cells, to investigate serologically and biochemically the relationship of the Yta antigen to known phosphatidylinositol-linked erythrocyte proteins. Yt(a-b-) RBCs expressed normal amounts of various phosphatidyl-inositol-linked proteins except acetylcholinesterase. Further, human anti-Yta reacted with acetylcholinesterase in immunoprecipitation and immunoblotting studies. Thus, acetylcholinesterase is now identified as the protein bearing the Yt blood group antigens.

scholarly journals Structural relationships between human erythrocyte sialoglycoproteins β and γ and abnormal sialoglycoproteins found in certain rare human erythrocyte variants lacking the Gerbich blood-group antigen(s)

1987 ◽  
Vol 244 (1) ◽  
pp. 123-128 ◽  
Author(s):  
M E Reid ◽  
D J Anstee ◽  
M J A Tanner ◽  
K Ridgwell ◽  
G T Nurse
Keyword(s):  
Blood Group ◽  
Erythrocyte Membrane ◽  
Human Erythrocyte ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Blood Group Antigen ◽  
Human Erythrocyte Membrane ◽  
Diffuse Band ◽  
Structural Relationships ◽  
Normal Erythrocyte

The human erythrocyte membrane sialoglycoproteins beta and gamma are important for the maintenance of the discoid shape of the normal erythrocyte. In this paper we show that the human erythrocyte sialoglycoproteins beta and gamma (hereafter called beta and gamma) are structurally related. Rabbit antisera produced against purified beta and beta 1 and rendered specific to the cytoplasmic portion of these proteins also react with the cytoplasmic portion of gamma. Some human anti-Gerbich (Ge) sera react with the extracellular portion of both beta and gamma. This reactivity is shown to be directed towards a common epitope on beta and gamma. However, most anti-Ge sera do not react with beta, but react with an extracellular epitope only present on gamma. All individuals who lack the Ge antigens lack beta and gamma. In some cases abnormal sialoglycoproteins are present in the erythrocytes, and these are shown to be structurally related to beta and gamma. Rabbit antisera raised against the purified abnormal sialoglycoprotein from a Ge-negative erythrocyte type reacted with the cytoplasmic portion of both beta and gamma. Unlike normal beta and gamma, the abnormal sialoglycoproteins found in Ge-negative erythrocytes migrate as a diffuse band on SDS/polyacrylamide-gel electrophoresis. Studies using endoglycosidases suggest that the diffuse nature of these bands results from carbohydrate heterogeneity and that the abnormal sialoglycoproteins contain N-glycosidically linked oligosaccharides with repeating lactosamine units. Such polylactosamine chains are not present on normal beta or gamma.

High Frequency Antigens of Human Erythrocyte Membrane Sialoglycoproteins, V.Characterization of the Gerbich Blood Group Antigens: Ge2 and Ge3

1987 ◽  
Vol 368 (2) ◽  
pp. 1375-1384 ◽  
Author(s):  
Wolfgang DAHR ◽  
Siegrid KIEDROWSKI ◽  
Dominique BLANCHARD ◽  
Patricia HERMAND ◽  
John J. MOULDS ◽  
...  
Keyword(s):  
Blood Group ◽  
Erythrocyte Membrane ◽  
Human Erythrocyte ◽  
High Frequency ◽  
Blood Group Antigens ◽  
Human Erythrocyte Membrane

scholarly journals Two individuals with elliptocytic red cells apparently lack three minor erythrocyte membrane sialoglycoproteins

1984 ◽  
Vol 218 (2) ◽  
pp. 615-619 ◽  
Author(s):  
D J Anstee ◽  
S F Parsons ◽  
K Ridgwell ◽  
M J A Tanner ◽  
A H Merry ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Blood Group ◽  
Erythrocyte Membrane ◽  
Human Erythrocyte ◽  
Blood Group Antigen ◽  
Red Cells

We have studied the erythrocytes of two individuals (P. L. and K. W.) who lack the Gerbich (Ge) blood-group antigen. The erythrocytes of P. L. and K. W. were not reactive with two monoclonal antibodies (NBTS/BRIC 4 and NBTS/BRIC 10) which reacted with normal erythrocytes. The membranes of P. L. and K. W. erythrocytes appeared to lack three minor sialoglycoproteins (beta, beta 1 and gamma). These three minor sialoglycoproteins were found to be associated with the cytoskeletons of normal erythrocytes. Approx. 10% of the erythrocytes of P. L. and K. W. were frankly elliptocytic. We suggest that one or more of the minor sialoglycoproteins may play a part in maintaining the discoid shape of the human erythrocyte.

scholarly journals Blood Group Susceptibility towardsCOVID-19 and Other Diseases

2021 ◽  
Vol 3 (2) ◽  
pp. 171-176
Author(s):  
Renuka Sharma ◽  
Manpreet Kaur ◽  
Manpreet Kaur ◽  
Neeru ◽  
Neha Yadav ◽  
...  
Keyword(s):  
Blood Group ◽  
Respiratory Diseases ◽  
Large Family ◽  
Future Research ◽  
Abo Blood Group ◽  
Blood Group System ◽  
Blood Group Antigens ◽  
Group System ◽  
Relationship Of ◽  
The Relationship

COVID – 19 is a global pandemic caused by a coronavirus named SARS CoV -2. A large family of viruses that causes severe respiratory diseases known as Coronavirus (CoVs) show symptoms such as common cold and range to more rare and severe respiratory diseases such SARAS i.e Severe Acute Respiratory Syndrome and MERS i.e Middle East Respiratory Syndrome detected for the first time in 2003 and 2012, respectively. It is expected to be a zoonotic virus transmitted via bats categorically, from genus Rhinolophus and closely related animals to humans. As this life threatening pandemic started from the Wuhan city of China, and the examination about this disease is still in continuity. It is very important to explore all possible scientific key points regarding this disease to eradicate such a dangerous issue from the society and to save the human race on earth. Literature available till now confirmed that the ABO blood group system showed significant relationship with various diseases. Now, scientific communities were working on different aspects of COVID-19 disease. But by keeping in mind about the severity of this disease and the relationship of blood group system of humans with infectious disease we conducted this study. Present review is designed to explore the relationship of COVID-19 alongwith other disease with the ABO blood group and Von Willebrand Factor. This study will provide information about the scientific evidences regarding the role of blood group antigens in prognosis of COVID-19 alongwith other disease and this can be significant for future research.

scholarly journals Abnormal minor human erythrocyte membrane sialoglycoprotein (β) in association with the rare blood-group antigen Webb (Wb)

1985 ◽  
Vol 232 (1) ◽  
pp. 289-291 ◽  
Author(s):  
M E Reid ◽  
M A Shaw ◽  
G Rowe ◽  
D J Anstee ◽  
M J Tanner
Keyword(s):  
Blood Group ◽  
Erythrocyte Membrane ◽  
Human Erythrocyte ◽  
Blood Group Antigen ◽  
Human Erythrocyte Membrane ◽  
Similar Treatment ◽  
Altered Form ◽  
Glycophorin C

Individuals whose erythrocytes are positive for the rare blood-group antigen Webb (Wb) have an altered form of the minor sialoglycoprotein beta (synonyms glycophorin C and glycoconnectin). This altered sialoglycoprotein beta (beta Wb) has an Mr about 2700 lower than that of normal sialoglycoprotein beta. Treatment of normal sialoglycoprotein beta with endo-beta-N-acetylglucosaminidase F decreased its Mr by about 3600, but similar treatment of sialoglycoprotein beta Wb had no effect. These results suggest the possibility that sialoglycoprotein beta Wb lacks the N-glycosidically linked oligosaccharide found on normal sialoglycoprotein beta.

scholarly journals cDNA cloning of a 30 kDa erythrocyte membrane protein associated with Rh (Rhesus)-blood-group-antigen expression

1990 ◽  
Vol 271 (3) ◽  
pp. 821-825 ◽  
Author(s):  
N D Avent ◽  
K Ridgwell ◽  
M J A Tanner ◽  
D J Anstee
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Membrane Protein ◽  
Blood Group ◽  
Erythrocyte Membrane ◽  
British Library ◽  
Cdna Clones ◽  
Blood Group Antigens ◽  
Hydrophobic Membrane ◽  
Pcr Products

The Rh-blood-group antigens (often described as Rhesus antigens) are associated with erythrocyte membrane proteins of approx. 30 kDa. We have determined the N-terminal 54 amino acid residues of the 30 kDa Rh D polypeptide (D30 polypeptide). We used primers based on these sequence data and the polymerase chain reaction (PCR) on human reticulocyte cDNA and genomic DNA to clone two types of PCR product of identical size. The two PCR products had related translated amino acid sequences between the 3′ ends of the primers, one of which was identical with that found for the D30 polypeptide. We designate the two related mRNA species which gave rise to the PCR products as Rh30A and Rh30B, the latter corresponding to the D30 polypeptide. We have isolated cDNA clones for the Rh30A protein which encode a hydrophobic membrane protein of 417 amino acids. The Rh30A protein has the same N-terminal 41 amino acids as the D30 polypeptide, but beyond this point the sequence differs, but is clearly related. The Rh30A protein probably corresponds to the R6A32 polypeptide, another member of the Rh 30 kDa family of proteins, which may carry the C/c and/or E/e antigens. Hydropathy analysis suggests that the Rh30A protein has up to 12 transmembrane domains. Three of these domains are bordered by a novel cysteine-containing motif, which might signal substitutions at these cysteine residues. Information which supplements this paper (amino-acid-sequence-analysis histograms) is reported in Supplementary Publication SUP 50160 (4 pages), which has been deposited at the British Library Document Supply Centre, Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1990) 265, 5.

scholarly journals Isolation of cDNA clones for a 50 kDa glycoprotein of the human erythrocyte membrane associated with Rh (rhesus) blood-group antigen expression

1992 ◽  
Vol 287 (1) ◽  
pp. 223-228 ◽  
Author(s):  
K Ridgwell ◽  
N K Spurr ◽  
B Laguda ◽  
C MacGeoch ◽  
N D Avent ◽  
...  
Keyword(s):  
Amino Acid ◽  
Membrane Proteins ◽  
Amino Acid Sequence ◽  
Blood Group ◽  
Erythrocyte Membrane ◽  
Human Erythrocyte ◽  
Cdna Clones ◽  
Blood Group Antigens ◽  
Human Erythrocyte Membrane ◽  
Degenerate Primers

The Rh blood-group antigens are associated with human erythrocyte membrane proteins of approx. 30 kDa (the Rh30 polypeptides). Heterogeneously glycosylated membrane proteins of 50 and 45 kDa (the Rh50 glycoproteins) are coprecipitated with the Rh30 polypeptides on immunoprecipitation with anti-Rh-specific mono- and poly-clonal antibodies. We have isolated cDNA clones representing a member of the Rh50 glycoprotein family (the Rh50A glycoprotein). We used PCR with degenerate primers based on the N-terminal amino acid sequence of the Rh50 glycoproteins and human genomic DNA as a template and cloned and sequenced three types of PCR product of the expected size. Two of these products, Rh50A and Rh50B, gave the same translated amino acid sequence which corresponded to the expected Rh50 glycoprotein sequence but had only 75% DNA sequence similarity. The third product (Rh50C) contained a single base deletion, and the translated amino acid sequence contained an in-frame stop codon. We have isolated cDNA clones containing the full coding sequence of the Rh50A glycoprotein. This sequence predicts that it is a 409-amino acid N-glycosylated membrane protein with up to 12 transmembrane domains. The Rh50A glycoprotein shows clear similarity to the Rh30A protein in both amino acid sequence and predicted topology. Our results are consistent with the Rh30 and Rh50 groups of proteins being different subunits of an oligomeric complex which is likely to have a transport or channel function in the erythrocyte membrane. We mapped the Rh50A gene to human chromosome 6p21-qter, showing that genetic differences in the Rh30 rather than the Rh50 genes specify the major polymorphic forms of the Rh antigens.

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