The <scp>MNS</scp> glycophorin variant <scp>GP</scp>.Mur affects differential erythroid expression of Rh/Rh<scp>AG</scp> transcripts

Hsu, Kate; Kuo, Mei-Shin; Yao, Ching-Che; Cheng, Huey-Chuan; Lin, Hui‐Ju; Chan, Y.-S.; Lin, Min

doi:10.1111/vox.12555

Cited by 7 publications

(6 citation statements)

References 36 publications

(43 reference statements)

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“…This suggests that GP.Mur/band 3-associated structural features could further facilitate NO scavenge by intraerythrocytic Hb ( Figure 3A ). Band 3 protein complexes differ between GP.Mur and non-GP.Mur in two aspects: ( 1 ) there are more band 3 molecules on the GP.Mur+ RBCs; ( 2 ) GP.Mur+ band 3 complexes are structurally distinguishable from non-GP.Mur ( 18 , 25 – 27 ). In particular, AQP1 and band 3 interact more strongly in GP.Mur+ than in non-GP.Mur RBCs ( 26 ).…”

Section: Discussionmentioning

confidence: 99%

“…The structural-functional hallmarks of GP.Mur+ red cells are enhanced band 3 expression (18) and altered band 3 complex structure with other membrane proteins on the red cell surface (21,(24)(25)(26). GP.Mur+ red cells present stronger band 3-AQP1 interaction (18,26), contain reduced amount of RhAG and consequently altered band 3-Rh/RhAG macrocomplex organization (25,27), and are more resilient physically in the osmolarity-fragility test (18). These presumably could affect band 3 interaction with submembranous deoxy Hb and metHb (28) and/or result in differential NOx processing, vasodilation, and blood pressure setting.…”

Section: Introductionmentioning

confidence: 99%

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Comodulation of NO-Dependent Vasodilation by Erythroid Band 3 and Hemoglobin: A GP.Mur Athlete Study

Hsu

Liu

Tseng

et al. 2021

Front. Cardiovasc. Med.

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GP.Mur, a red blood cell (RBC) hybrid protein encoded by glycophorin B-A-B, increases expression of erythroid band 3 (Anion Exchanger-1, SLC4A1). GP.Mur is extremely rare but has a prevalence of 1–10% in regions of Southeast Asia. We unexpectedly found slightly higher blood pressure (BP) among healthy Taiwanese adults with GP.Mur. Since band 3 has been suggested to interact with hemoglobin (Hb) to modulate nitric oxide (NO)-dependent hypoxic vasodilation during the respiratory cycle, we hypothesized that GP.Mur red cells could exert differentiable effects on vascular tone. Here we recruited GP.Mur-positive and GP.Mur-negative elite male college athletes, as well as age-matched, GP.Mur-negative non-athletes, for NO-dependent flow-mediated dilation (FMD) and NO-independent dilation (NID). The subjects were also tested for plasma nitrite and nitrate before and after arterial occlusion in FMD. GP.Mur+ and non-GP.Mur athletes exhibited similar heart rates and blood pressure, but GP.Mur+ athletes showed significantly lower FMD (4.8 ± 2.4%) than non-GP.Mur athletes (6.5 ± 2.1%). NO-independent vasodilation was not affected by GP.Mur. As Hb controls intravascular NO bioavailability, we examined the effect of Hb on limiting FMD and found it to be significantly stronger in GP.Mur+ subjects. Biochemically, plasma nitrite levels were directly proportional to individual band 3 expression on the red cell membrane. The increase of plasma nitrite triggered by arterial occlusion also showed small dependency on band 3 levels in non-GP.Mur subjects. By the GP.Mur comparative study, we unveiled comodulation of NO-dependent vasodilation by band 3 and Hb, and verified the long-pending role of erythroid band 3 in this process.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Comodulation of NO-Dependent Vasodilation by Erythroid Band 3 and Hemoglobin: A GP.Mur Athlete Study

Hsu

Liu

Tseng

et al. 2021

Front. Cardiovasc. Med.

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“…For example, in the MNS blood group system, the antibody recognition reaction is obviously temperature-dependent. As a consequence, antibodies known as cold antibodies do not agglutinate with their corresponding erythrocytes at 37°C, meaning that temperature control is required when doing test in the laboratory [20][21] . In addition to temperature, blood group antibodies are also different in dependence on complement.…”

Section: The Complexity Of Blood Group Antibodiesmentioning

confidence: 99%

Overview of the diversity of erythrocyte blood group antigens

Yang¹,

Feng²

2020

Blood and Genomics

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During the differentiation and maturation of erythrocytes, the surface molecules of erythrocytes are gradually expressed and stabilized. These molecules are to be antigenic in addition to their functions of maintaining cell membrane structural stability, material transport and exchange of cells and signal transmission between cells. The antigenic molecules on the erythrocyte surface are called erythrocyte blood group antigens. The blood group antigens and their corresponding blood group antibodies in vivo are important indicators for clinical blood transfusion and organ transplantation, and also form the basis for research on blood group related diseases. Three hundred and sixty-eight erythrocyte blood group antigens have been confirmed so far, which are classified into 39 blood group systems, 5 blood group collections and 2 blood group series. Based on the diversity of blood group antigens and their composition of glycolipids, glycoproteins and other molecules, this study mainly reviews the classification, molecular structure, antibody response and gene regulation of blood group antigens, and explains the main reasons for the diversity of blood group antigens.

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“…On the red cell membrane, GP.Mur oligomerizes with glycophorin A and band 3, and supports band 3 expression [ 5 ]. GP.Mur+ band 3 complexes are unique in (i) stronger association with AQP1 [ 11 ] and (ii) differential structural organization with Rh/RhAG complexes [ 12 , 13 ]. AQP1 is a gated water channel that functions in response to changes of osmolarity [ 14 , 15 ].…”

Section: Introductionmentioning

confidence: 99%

Different Involvement of Band 3 in Red Cell Deformability and Osmotic Fragility—A Comparative GP.Mur Erythrocyte Study

Kuo

Chuang

Cheng

et al. 2021

Cells

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GP.Mur is a clinically important red blood cell (RBC) phenotype in Southeast Asia. The molecular entity of GP.Mur is glycophorin B-A-B hybrid protein that promotes band 3 expression and band 3–AQP1 interaction, and alters the organization of band 3 complexes with Rh/RhAG complexes. GP.Mur+ RBCs are more resistant to osmotic stress. To explore whether GP.Mur+ RBCs could be structurally more resilient, we compared deformability and osmotic fragility of fresh RBCs from 145 adults without major illness (47% GP.Mur). We also evaluated potential impacts of cellular and lipid factors on RBC deformability and osmotic resistivity. Contrary to our anticipation, these two physical properties were independent from each other based on multivariate regression analyses. GP.Mur+ RBCs were less deformable than non-GP.Mur RBCs. We also unexpectedly found 25% microcytosis in GP.Mur+ female subjects (10/40). Both microcytosis and membrane cholesterol reduced deformability, but the latter was only observed in non-GP.Mur and not GP.Mur+ normocytes. The osmotic fragility of erythrocytes was not affected by microcytosis; instead, larger mean corpuscular volume (MCV) increased the chances of hypotonic burst. From comparison with GP.Mur+ RBCs, higher band 3 expression strengthened the structure of RBC membrane and submembranous cytoskeletal networks and thereby reduced cell deformability; stronger band 3–AQP1 interaction additionally supported osmotic resistance. Thus, red cell deformability and osmotic resistivity involve distinct structural–functional roles of band 3.

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The MNS glycophorin variant GP.Mur affects differential erythroid expression of Rh/RhAG transcripts

Cited by 7 publications

References 36 publications

Comodulation of NO-Dependent Vasodilation by Erythroid Band 3 and Hemoglobin: A GP.Mur Athlete Study

Comodulation of NO-Dependent Vasodilation by Erythroid Band 3 and Hemoglobin: A GP.Mur Athlete Study

Overview of the diversity of erythrocyte blood group antigens

Different Involvement of Band 3 in Red Cell Deformability and Osmotic Fragility—A Comparative GP.Mur Erythrocyte Study

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