A proenzyme form of human urokinase.
T C Wun,L Ossowski,E Reich +2 more
TLDR
It is concluded that the HEp 3 protein is a proenzyme that can be converted to active two-chain urokinase by plasmin, probably by a single proteolytic nick in the polypeptide chain.About:
This article is published in Journal of Biological Chemistry.The article was published on 1982-06-25 and is currently open access. It has received 335 citations till now. The article focuses on the topics: Plasmin & Urokinase.read more
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Book ChapterDOI
Plasminogen activators, tissue degradation, and cancer.
Keld Danø,Peter A. Andreasen,J Grøndahl-Hansen,Peter Marcus Kristensen,L.S. Nielsen,L. Skriver +5 more
TL;DR: This chapter describes two types of plasminogen activators—namely, the urokinase-type plasMinogen activator (u-PA) and the tissue- type plasmineg activator(t-PA), which are essentially different gene products.
Journal ArticleDOI
A cellular binding site for the Mr 55,000 form of the human plasminogen activator, urokinase.
TL;DR: The results demonstrate the presence of a membrane receptor for Uk on monocytes and show a hitherto unknown function for the A chain of Uk: binding of secreted enzyme to its receptor results in Uk acting as a membrane protease.
Journal ArticleDOI
Antibodies to plasminogen activator inhibit human tumor metastasis
Liliana Ossowski,Edward Reich +1 more
TL;DR: Antibody treatment delayed the onset of pulmonary metastasis, indicating that plasminogen activator is required during early stages of the process.
Journal ArticleDOI
Urokinase-type plasminogen activator: proenzyme, receptor, and inhibitors
TL;DR: Findings show that u-PA is synthesized and released from mammalian cells as a proenzyme with little or no activity (pro-u-PA), that cells possess a specific binding site for u- PA and pro-u -PA, and that they can also synthesize different rapidly acting, high affinity inhibitors of PAs.
Journal ArticleDOI
The receptor-binding sequence of urokinase. A biological function for the growth-factor module of proteases.
Ettore Appella,Elizabeth A. Robinson,Ullrich Sj,M P Stoppelli,Angelo Corti,Giovanni Cassani,Francesco Blasi +6 more
TL;DR: The area within ATF responsible for specific receptor binding has now been identified by the ability of different synthetic peptides corresponding to different regions of the amino terminus of uPA to inhibit receptor binding of 125I-labeled ATF.
References
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Journal ArticleDOI
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
TL;DR: Using an improved method of gel electrophoresis, many hitherto unknown proteins have been found in bacteriophage T4 and some of these have been identified with specific gene products.
Journal ArticleDOI
Fluorometric assay of proteins in the nanogram range
TL;DR: The reagent fluorescamine has been used for the fluorometric assay of proteins based on their content of free amino groups and its applications to the monitoring of proteins during enzyme purification are described.
Journal ArticleDOI
A study of proteases and protease-inhibitor complexes in biological fluids.
A Granelli-Piperno,E Reich +1 more
TL;DR: The respective results show that the plasminogen activators in urine and cell culture media are generally of lower molecular weight than those in plasma, and that proteases bound to α2-macroglobulin recover the ability to attack macromolecular substrates after exposure to sodium dodecyl sulfate while retaining the electrophoretic mobility of the protease inhibitor complex.
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Radioiodination of proteins in single polyacrylamide gel slices. Tryptic peptide analysis of all the major members of complex multicomponent systems using microgram quantities of total protein.
TL;DR: This technique has compared the tryptic peptides of all the major protein components of Moloney and Rauscher leukemia viruses using only 50 to 100 microgram of total protein from each virus.
Journal ArticleDOI
Fibrinolysis associated with oncogenic transformation. Partial purification and characterization of the cell factor, a plasminogen activator.
TL;DR: The cell factor that is involved in tumor-associated fibrinolysis has been partially purified from the supernatant fluid of transformed chicken embryo fibroblast cultures and is an arginine-specific protease that acts as a plasminogen activator.