Alternative Splicing of a Novel Glycophorin Allele GPHe(GL) Generates Two Protein Isoforms in the Human Erythrocyte Membrane

The Henshaw antigen (synonym: He or MNS6) is carried by an altered form of glycophorin B (GPB), but the molecular basis for its variable expression or quantitative polymorphism remains largely undefined. We report here the identification and analysis of a novel glycophorin He allele, GPHe(GL), which...

Full description

Saved in:
Bibliographic Details
Published in:Blood 1997-07, Vol.90 (1), p.391-397, Article 391
Main Authors: HUANG, C.-H, BLUMENFELD, O. O, REID, M. E, CHEN, Y, DANIELS, G. L, SMART, E
Format: Article
Language:English
Subjects:
Alleles
Alternative Splicing
Amino Acid Sequence
Antigens
Base Sequence
Biological and medical sciences
Blood group antigens
DNA, Complementary - analysis
DNA, Complementary - genetics
Erythrocyte Membrane - metabolism
Fundamental and applied biological sciences. Psychology
Fundamental immunology
Glycophorins - genetics
Glycophorins - metabolism
Humans
Molecular immunology
Molecular Sequence Data
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:The Henshaw antigen (synonym: He or MNS6) is carried by an altered form of glycophorin B (GPB), but the molecular basis for its variable expression or quantitative polymorphism remains largely undefined. We report here the identification and analysis of a novel glycophorin He allele, GPHe(GL), which gives rise to the expression of two protein isoforms in the erythrocyte membrane. In addition to the nucleotide changes defining the epitopic sequence of He, a single C-to-G nucleotide transversion in exon V coding for the membrane domain was found to cause aberrant RNA splicings by creating a new acceptor splice site. In addition, a T-to-G transversion at -6 position of the acceptor splice site for exon IV was identified. Both full-length and truncated transcripts of GPHe(GL) were detected as the result of partial activation of the new acceptor splice site and partial inactivation of the normal splice sites. The full-length cDNA encoded He, S, and U antigens, whereas the three truncated ones lacked either the sequence for S and U antigens or a large portion of the membrane domain or both. The GPB gene on the other chromosome was apparently normal and its transcript encoded N, s, and U antigens. These results correlate alternative RNA splicing with the expression of two GPHe isoforms and thus delineate a new mechanism for the phenotypic diversity of membrane glycophorins.
ISSN:0006-4971
1528-0020
DOI:10.1182/blood.V90.1.391