An alternatively spliced variant of mRNA for the human receptor for urokinase plasminogen activator.
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.
Finsen Laboratory, Rigshospitalet, Copenhagen, Denmark.
C
C
Pyke
J
J
Eriksen
H
H
Solberg
B S
BS
Nielsen
P
P
Kristensen
L R
LR
Lund
K
K
Danø
D000595:Amino Acid Sequence; D001483:Base Sequence; D004247:DNA / Q000235:genetics; D005784:Gene Amplification; D014644:Genetic Variation; D006801:Humans; D008969:Molecular Sequence Data; D016133:Polymerase Chain Reaction; D014176:Protein Biosynthesis; D012326:RNA Splicing; D012333:RNA, Messenger / Q000235:genetics*; D011956:Receptors, Cell Surface / Q000737:chemistry / Q000235:genetics*; D055293:Receptors, Urokinase Plasminogen Activator; D012260:Ribonucleases
C524898:PLAUR protein, human; D012333:RNA, Messenger; D011956:Receptors, Cell Surface; D055293:Receptors, Urokinase Plasminogen Activator; D004247:DNA; D012260:Ribonucleases