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Cloning, nucleotide sequencing and expression of cDNAs encoding mouse urokinase-type plasminogen activator

Godeau, F.
Nagamine, Y.
Reich, E.
Kocher, H. P.
Duvoisin, R. M.
Published in European journal of biochemistry. 1985, vol. 148, no. 2, p. 225-232
Abstract 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.
Keywords Amino Acid SequenceAnimalsBase SequenceCloning, MolecularDNA/ isolation & purificationDNA Transposable ElementsGene Expression RegulationMiceNucleic Acid HybridizationPlasminogen Activators/ geneticsUrokinase-Type Plasminogen Activator/ genetics
PMID: 2985383
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BELIN, Dominique et al. Cloning, nucleotide sequencing and expression of cDNAs encoding mouse urokinase-type plasminogen activator. In: European journal of biochemistry, 1985, vol. 148, n° 2, p. 225-232. doi: 10.1111/j.1432-1033.1985.tb08829.x https://archive-ouverte.unige.ch/unige:8635

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Deposited on : 2010-07-12

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