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

• Published in: Vox sanguinis Vol. 112; no. 7; pp. 671 - 677
• Main Authors: Hsu, K., Kuo, M.‐S., Yao, C.‐C., Cheng, H.‐C., Lin, H.‐J., Chan, Y.‐S., Lin, M.
• Format: Journal Article
• Language: English
• Published: England S. Karger AG 01.10.2017
• Subjects: Ankyrins; Blood transfusions; Erythroid cells; Erythroid Cells - metabolism; Glycophorin - blood; Glycophorin - genetics; Glycophorin - metabolism; Glycophorin B; Glycoproteins; GP.Mur (Miltenberger subtype III; Humans; Mi.III; Peripheral blood; Polypeptides; real‐time PCR; Reticulocytes; Reverse transcription; Rh polypeptides; Rh-Hr Blood-Group System - blood; Rh-Hr Blood-Group System - genetics; Rh-Hr Blood-Group System - metabolism; RhAG; RhCE (RhCcEe); RhD; Ribonucleic acid; RNA; RNA, Messenger - genetics; RNA, Messenger - metabolism; Taiwan; glycophorin B; Mi.III; RhCE (RhCcEe); RhAG; real-time PCR; Rh polypeptides; GP.Mur (Miltenberger subtype III; RhD
• ISSN: 0042-9007; 1423-0410; 1423-0410
• DOI: 10.1111/vox.12555

Background The band 3 macrocomplex (also known as the ankyrin‐associated complex) on the red cell membrane comprises two interacting subcomplexes: a band 3/glycophorin A subcomplex, and a Rh/RhAG subcomplex. Glycophorin B (GPB) is a component of the Rh/RhAG subcomplex that is also structurally associated with glycophorin A (GPA). Expression of glycophorin B‐A‐B hybrid GP.Mur enhances band 3 expression and is associated with lower levels of Rh‐associated glycoprotein (RhAG) and Rh polypeptides. The goal of this study was to determine whether GP.Mur influenced erythroid Rh/RhAG expression at the transcript level. Materials and Methods GP.Mur was serologically determined in healthy participants from Taitung County, Taiwan. RNA was extracted from the reticulocyte‐enriched fraction of peripheral blood, followed by reverse transcription and quantitative PCR for RhAG, RhD and RhCcEe. Results Quantification by real‐time PCR revealed significantly fewer RhAG and RhCcEe transcripts in the reticulocytes from subjects with homozygous GYP*Mur. Independent from GYP.Mur, both RhAG and RhD transcript levels were threefold or higher than that of RhCcEe. Also, in GYP.Mur and the control samples alike, direct quantitative associations were observed between the transcript levels of RhAG and RhD, but not between that of RhAG and RhCcEe. Conclusion Erythroid RhD and RhCcEe were differentially expressed at the transcript levels, which could be related to their different degrees of interaction or sensitivity to RhAG. Further, the reduction or absence of glycophorin B in GYP.Mur erythroid cells affected transcript expressions of RhAG and RhCcEe. Thus, GPB and GP.Mur differentially influenced Rh/RhAG expressions prior to protein translation.