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The structure of the urokinase-type plasminogen activator receptor gene
JR Casey, JG Petranka, J Kottra, DE Fleenor and WF Rosse
Department of Pediatrics, Duke University Medical Center, Durham, NC 27710.
The cellular receptor for urokinase-type plasminogen activator (uPAR) is a
glycosylphosphatidylinositol (GPI)-anchored membrane protein that plays a
central role in pericellular plasminogen activation. It contains 313 amino
acid residues, including 28 cysteine residues in a pattern of three
homologous repeats. The cysteine residue pattern suggests that uPAR belongs
to a superfamily of proteins including CD59, murine Ly-6, and a variety of
elapid snake venom toxins. A novel 1.7-kb uPAR cDNA was isolated that is
missing exon 5 and that contains 380 bp not previously reported at the 5'
end. This cDNA was used to probe a human genomic library from which three
clones were isolated and analyzed. The uPAR gene consists of 7 exons spread
over 23 kb of genomic DNA. Exons 2, 4, and 6 code for homologous domains
within the mature protein, as do exons 3, 5, and 7; CD59-like homologous
pairs are encoded by exons 2-3, 4-5, and 6-7, respectively. The structure
of the gene for uPAR further confirms the relationship of this molecule to
the superfamily containing CD59, Ly-6, and the elapid snake venom toxins.
Volume 84,
Issue 4,
pp. 1151-1156,
08/15/1994
Copyright © 1994 by The American Society of Hematology
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