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Nucleic Acids Research, 1990, Vol. 18, No. 19 5829-5836
© 1990

MOLECULAR BIOLOGY

The mechanism of production of multiple mRNAs for human glycophorin A

Jawed Hamid and Alfred T.H. Burness*

Faculty of Medicine, Memorial University of Newfoundland St John's, Newfoundland A1B 3V6, Canada

* To whom correspondence should be addressed

Received April 16, 1990. Revised August 29, 1990. Accepted August 29, 1990.

The major sialoglycoprotein in the human red cell surface membrane, glycophorin A is encoded by a single gene. However, this gene gives rise to three species of glycophorin A mRNA of sizes about 1.0, 1.7 and 2.8 kilobases in reticulocytes, foetal liver cells and erythroleukaemic K562 cells. In an investigation of how the three mRNAs originated, we showed by primer extension analysis that all three mRNAs in K562 cells had identical 5' termini and, by nucleotide sequencing of correlated cDNAs, that they had identical coding regions, except for the well-known glycophorin AM polymorphism. However, we found also by sequencing the cDNAs that the mRNAs apparently differed from each other in the lengths of their 3' untranslated regions. This was confirmed by Northern blot analysis which also provided evidence that the three mRNAs originated by use of different polyadenylation signals of which seven were found in the longest cDNA we analyzed.


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