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Cloning of glycoprotein IIIa cDNA from human erythroleukemia cells and
localization of the gene to chromosome 17
JP Rosa, PF Bray, O Gayet, GI Johnston, RG Cook, KW Jackson, MA Shuman and RP McEver
U150 INSERM, Hopital Lariboisiere, Paris.
Platelet aggregation requires the binding of adhesive proteins such as
fibrinogen to the heterodimer of membrane glycoproteins IIb (GPIIb) and
IIIa (GPIIIa). Human erythroleukemia (HEL) cells synthesize both GPIIb and
GPIIIa. Using poly(A+) RNA purified from HEL cells, we constructed a cDNA
library in the lambda gt10 phage vector. This library was screened with a
38mer oligonucleotide derived from a platelet GPIIIa peptide, and three
overlapping cDNAs were isolated. The three inserts encompassed 3.5
kilobases (kb), including the entire coding region of mature GPIIIa (2,286
basepairs, bp) and 1.3 kb of 3' untranslated sequence. All 222 residues
determined directly from platelet GPIIIa tryptic peptides exactly matched
the HEL cell-deduced amino acid sequence. The HEL cell sequence matched a
previously reported endothelial cell cDNA sequence except for eight
nucleotides. Five of these nucleotide differences were silent changes
consistent with genetic polymorphisms. The other three differences resulted
in changes in the deduced amino acid sequence of GPIIIa; reexamination of
the endothelial cell cDNA sequence in these three areas revealed that it is
actually identical to the HEL cell sequence. The virtual identity of the
endothelial and HEL cell cDNA sequences provides direct evidence that
GPIIIa is a subunit common to cell-adhesion receptors present in more than
one cell type. We localized the gene for GPIIIa to chromosome 17, the same
chromosome to which we had previously mapped the gene for GPIIb.
Volume 72,
Issue 2,
pp. 593-600,
08/01/1988
Copyright © 1988 by The American Society of Hematology
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