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S Chang, ME Reid, J Conboy, YW Kan and N Mohandas
Cell and Molecular Biology Division, Lawrence Berkeley Laboratory,
University of California 94720.
Human erythrocyte glycophorin C plays a functionally important role in
maintaining erythrocyte shape and regulating membrane mechanical stability.
Immunochemical and serologic studies have identified a number of
glycophorin C variants that include the Yus, Gerbich, and Webb phenotypes.
We report here the molecular characterization of these variants.
Amplification of glycophorin C mRNA from the Yus phenotype, using two
oligonucleotide primers that span the coding domain, generated a 338-bp
fragment compared with a 395-bp fragment generated by amplification of
normal glycophorin C mRNA. Sequencing of the mutant 338-bp fragment
identified a 57-bp deletion that corresponds to exon 2 of the glycophorin C
gene. Similar analysis showed deletion of 84-bp exon 3 in the Gerbich
phenotype. In contrast to the generation of shorter than normal DNA
fragments from mRNA amplification in the Yus and Gerbich phenotypes,
amplification of mRNA from the Webb phenotype generated a normal-sized
fragment. Sequencing of this DNA fragment showed an A----G substitution at
nucleotide 23 of the coding sequence, resulting in the substitution of
asparagine by serine. This modification accounts for the altered
glycosylation of glycophorin C seen in this phenotype. These results have
enabled us to characterize glycophorin C variants in three different
phenotypes that involve deletions of exons 2 and 3 of the glycophorin C
gene, as well as a point mutation in exon 1 that results in altered
glycosylation of this protein.
This article has been cited by other articles:
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| Copyright © 1991 by American Society of Hematology Online ISSN: 1528-0020 | |||||||||
