Expression of the Rh/RhAG complex is reduced in Mi.III erythrocytes

Hsu, Kate; Lee, T.-Y.; Chao, Hsueh-Ping; Chan, Y.-S.; Lin, Yen–Chun; Lin, Min

doi:10.1111/j.1423-0410.2011.01535.x

Cited by 9 publications

(14 citation statements)

References 44 publications

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“…a). These differences in RhAG transcript levels among GYP*Mur ho , GYP*Mur het and the negative control were similar to our previous findings in RhAG protein expression: compared to the negative control, RhAG protein is significantly reduced in homozygous GYP*Mur RBCs, but not in heterozygous GYP*Mur RBCs .…”

Section: Resultssupporting

confidence: 90%

“…In the ‘band 3‐central macrocomplex’, we hypothesized that GPB likely serves as a structural linker, as GPB and its homologous counterpart GPA form heterodimer, and is a component of the Rh/RhAG complex . Our hypothesis is based on previous findings in GYP*Mur ho RBCs that lack GPB: Rh/RhAG protein expression is reduced, and band 3 expression increased . When the linker GPB is replaced by glycophorin B‐A‐B hybrid GP.Mur, the consequences could be as follows: (1) reduction in the number of band 3 macrocomplexes and increase in the number of band 3/GPA dimer, (2) changes in the structural organization of the band 3‐central macrocomplexes, or (3) both.…”

Section: Introductionmentioning

confidence: 98%

“…When the linker GPB is replaced by glycophorin B‐A‐B hybrid GP.Mur, the consequences could be as follows: (1) reduction in the number of band 3 macrocomplexes and increase in the number of band 3/GPA dimer, (2) changes in the structural organization of the band 3‐central macrocomplexes, or (3) both. As expression of U antigen that requires both RhAG and GPB is diminished in GYP*Mur ho RBCs, the interface structure between RhAG and GP.Mur is expected to differ from the interface between RhAG and GPB .…”

Section: Introductionmentioning

confidence: 99%

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

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Section: Resultssupporting

confidence: 90%

Section: Introductionmentioning

confidence: 98%

Section: Introductionmentioning

confidence: 99%

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

et al. 2017

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“…Moreover, the significant differences in FLIM-FRET in Mi.III vs. non-Mi.III membrane reflected their structural differences in band 3 complex organization ( Fig. 3) (20,39).…”

Section: Aqp1-band 3 Physical Interaction Measured By Flim-fretmentioning

confidence: 99%

Adaptable interaction between aquaporin‐1 and band 3 reveals a potential role of water channel in blood CO₂transport

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Human CO respiration requires rapid conversion between CO and HCO Carbonic anhydrase II facilitates this reversible reaction inside red blood cells, and band 3 [anion exchanger 1 (AE1)] provides a passage for HCO flux across the cell membrane. These 2 proteins are core components of the CO transport metabolon. Intracellular HO is necessary for CO/HCO conversion. However, abundantly expressed aquaporin 1 (AQP1) in erythrocytes is thought not to be part of band 3 complexes or the CO transport metabolon. To solve this conundrum, we used Förster resonance energy transfer (FRET) measured by fluorescence lifetime imaging (FLIM-FRET) and identified interaction between aquaporin-1 and band 3 at a distance of 8 nm, within the range of dipole-dipole interaction. Notably, their interaction was adaptable to membrane tonicity changes. This suggests that the function of AQP1 in tonicity response could be coupled or correlated to its function in band 3-mediated CO/HCO exchange. By demonstrating AQP1 as a mobile component of the CO transport metabolon, our results uncover a potential role of water channel in blood CO transport and respiration.-Hsu, K., Lee, T.-Y., Periasamy, A., Kao, F.-J., Li, L.-T., Lin, C.-Y., Lin, H.-J., Lin, M. Adaptable interaction between aquaporin-1 and band 3 reveals a potential role of water channel in blood CO transport.

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“…Therefore, Mi. [21]. As Mi.III expression affects the interface between RhAG and GPB ⁄ Gp.Mur and the interface between band 3 and GPA ⁄ Gp.Mur, conceivably band 3 and the Rh complex are structurally linked by oligomerization of GPA and GPB ⁄ Gp.Mur.…”

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confidence: 98%

Physiological Implications of Miltenberger blood group antigen subtype III (Mi.III)

Hsu

2011

ISBT Science Series

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In Taiwan, Miltenberger blood group antigen subtype III (Mi.III) is the second most important blood group antigen following ABO. Mi.III presumably evolved from homologous recombination between GYPA and GYPB, and expresses a hybrid configuration of glycophorin B-A-B and the Mur antigen in the crossover region.GPA and GPB oligomerize on the erythrocyte cell membrane. GPA also forms protein complexes with band 3 and facilitates band 3 expression. GPB is believed not to involve in the GPA-band 3 interaction. In Mi.III+ blood, half or all GPB is replaced with the glycophorin BAB hybrid, Gp.Mur. We previously showed that upon heterologous expression in HEK-293 cells, Gp. On the other hand, GPB is a component of the Rh protein complex, and has been shown to assist the surface expression of RhAG. Because GPB is half or completely replaced by Gp.Mur in Mi.III+ RBCs, we also examined if the expression of the Rh complexes could be affected in Mi.III. We found that homologous Mi.III RBCs exhibit reduced levels of RhAG and Rh antigens. The functions of Rh polypeptides and RhAG in erythrocytes are unclear, but RhAG in other species might function as gas channels for physiologically important molecules such as CO 2 , NH 3 , NO, and ⁄ or O 2 . Thus, substitution of GPB with Gp.Mur in Mi.III+ RBCs affects the structure of the band 3 ⁄ Rh-associated macrocomplex, and is expected to affect functional coordination within the metabolon of O 2 ⁄ CO 2 gas exchange as well.

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Expression of the Rh/RhAG complex is reduced in Mi.III erythrocytes

Abstract: Substitution of GPB with Gp.Mur significantly reduced the expression of Rh antigen and RhAG on the Mi.III(+/+) erythrocyte membrane. The Mi.III phenotype is predicted to induce considerable structural variations within the band 3/Rh-associated macrocomplexes.

Cited by 9 publications

References 44 publications

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

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

Adaptable interaction between aquaporin‐1 and band 3 reveals a potential role of water channel in blood CO₂transport

Physiological Implications of Miltenberger blood group antigen subtype III (Mi.III)

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Expression of the Rh/RhAG complex is reduced in Mi.III erythrocytes

Abstract: Substitution of GPB with Gp.Mur significantly reduced the expression of Rh antigen and RhAG on the Mi.III(+/+) erythrocyte membrane. The Mi.III phenotype is predicted to induce considerable structural variations within the band 3/Rh-associated macrocomplexes.

Cited by 9 publications

References 44 publications

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

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

Adaptable interaction between aquaporin‐1 and band 3 reveals a potential role of water channel in blood CO2transport

Physiological Implications of Miltenberger blood group antigen subtype III (Mi.III)

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Adaptable interaction between aquaporin‐1 and band 3 reveals a potential role of water channel in blood CO₂transport