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

D. Belin, J. D. Vassalli, C. Combepine, F. Godeau, Y. Nagamine, E. Reich, H. P. Kocher, Robert Duvoisin

Research output: Contribution to journalArticle

154 Citations (Scopus)

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.

Original languageEnglish (US)
Pages (from-to)225-232
Number of pages8
JournalEuropean Journal of Biochemistry
Volume148
Issue number2
DOIs
StatePublished - 1985
Externally publishedYes

Fingerprint

Cloning
Urokinase-Type Plasminogen Activator
Organism Cloning
Nucleotides
Complementary DNA
Base Pairing
Proteolysis
Glycosylation
3T3 Cells
Periplasm
Plasminogen Activators
Enzymes
Protein Sorting Signals
Gene Library
Bacteria
Plasmids
Peptide Hydrolases
Swine
Tissue
Amino Acids

ASJC Scopus subject areas

  • Biochemistry

Cite this

Cloning, nucleotide sequencing and expression of cDNAs encoding mouse urokinase-type plasminogen activator. / Belin, D.; Vassalli, J. D.; Combepine, C.; Godeau, F.; Nagamine, Y.; Reich, E.; Kocher, H. P.; Duvoisin, Robert.

In: European Journal of Biochemistry, Vol. 148, No. 2, 1985, p. 225-232.

Research output: Contribution to journalArticle

Belin, D. ; Vassalli, J. D. ; Combepine, C. ; Godeau, F. ; Nagamine, Y. ; Reich, E. ; Kocher, H. P. ; Duvoisin, Robert. / Cloning, nucleotide sequencing and expression of cDNAs encoding mouse urokinase-type plasminogen activator. In: European Journal of Biochemistry. 1985 ; Vol. 148, No. 2. pp. 225-232.
@article{ef853bf7a03a4b90b2b93409bc031279,
title = "Cloning, nucleotide sequencing and expression of cDNAs encoding mouse urokinase-type plasminogen activator",
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.",
author = "D. Belin and Vassalli, {J. D.} and C. Combepine and F. Godeau and Y. Nagamine and E. Reich and Kocher, {H. P.} and Robert Duvoisin",
year = "1985",
doi = "10.1111/j.1432-1033.1985.tb08829.x",
language = "English (US)",
volume = "148",
pages = "225--232",
journal = "FEBS Journal",
issn = "1742-464X",
publisher = "Wiley-Blackwell",
number = "2",

}

TY - JOUR

T1 - Cloning, nucleotide sequencing and expression of cDNAs encoding mouse urokinase-type plasminogen activator

AU - Belin, D.

AU - Vassalli, J. D.

AU - Combepine, C.

AU - Godeau, F.

AU - Nagamine, Y.

AU - Reich, E.

AU - Kocher, H. P.

AU - Duvoisin, Robert

PY - 1985

Y1 - 1985

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=0021914983&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0021914983&partnerID=8YFLogxK

U2 - 10.1111/j.1432-1033.1985.tb08829.x

DO - 10.1111/j.1432-1033.1985.tb08829.x

M3 - Article

C2 - 2985383

AN - SCOPUS:0021914983

VL - 148

SP - 225

EP - 232

JO - FEBS Journal

JF - FEBS Journal

SN - 1742-464X

IS - 2

ER -