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An alternatively spliced variant of mRNA for the human receptor for urokinase plasminogen activator
Author(s) -
Pyke C.,
Eriksen J.,
Solberg H.,
Nielsen B.Schnack,
Kristensen P.,
Lund L.R.,
Dano K.
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)81763-p
Subject(s) - urokinase receptor , messenger rna , microbiology and biotechnology , complementary dna , alternative splicing , chemistry , rapid amplification of cdna ends , plasminogen activator , receptor , biology , gene , biochemistry , genetics , molecular cloning
Using 3′ RACE (rapid amplification of cDNA ends), we have isolated a cDNA variant for the receptor for human urokinase plasminogen activator (uPAR). The deduced protein includes the amino‐terminal ligand binding domain in uPAR, but lacks the carboxy‐terminal membrane attachment by a glycolipid anchor. Genomic DNA analysis showed that the uPAR mRNA variant is generated by alternative splicing. The new variant mRNA is expressed in various human cell lines and tissues and both variants are up‐regulated by phorbol ester in A549 cells. We propose that the alternatively spliced uPAR mRNA encodes a soluble uPA binding protein, the possible function of which is discussed.