Cloning, nucleotide sequencing and expression of cDNAs encoding mouse urokinase-type plasminogen activator.
Controlled extracellular proteolysis is catalyzed in part by the secretion of plasminogen activators. As a step in the study of the expression of these enzymes in mouse tissues, we have isolated five cDNAs encoding the mouse urokinase-type plasminogen activator from a cDNA library prepared with size-selected mRNA from MSV-transformed 3T3 cells. The longest cDNA insert contains the entire coding region of mouse urokinase, 58 base pairs of the 5' non-coding region, and the entire 3' non-coding region, which is 942 base pairs long. The deduced protein sequence, which starts with a signal peptide of 20 amino acids, shows extensive homology to that of human and porcine urokinase. However, in contrast to these enzymes, mouse urokinase contains no N-glycosylation site. Bacteria harbouring one of the recombinant plasmids synthesize and secrete into their periplasm a protease indistinguishable from mouse urokinase.
Belin
D
D
Vassalli
J D
JD
Combépine
C
C
Godeau
F
F
Nagamine
Y
Y
Reich
E
E
Kocher
H P
HP
Duvoisin
R M
RM
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D003001:Cloning, Molecular; D004247:DNA / Q000302:isolation & purification*; D004251:DNA Transposable Elements; D005786:Gene Expression Regulation; D051379:Mice; D009693:Nucleic Acid Hybridization; D010960:Plasminogen Activators / Q000235:genetics*; D014568:Urokinase-Type Plasminogen Activator / Q000235:genetics*
D004251:DNA Transposable Elements; D004247:DNA; D010960:Plasminogen Activators; D014568:Urokinase-Type Plasminogen Activator