E. V. Parfenova

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Urokinase-type plasminogen activator (uPA) is a serine protease that converts the plasminogen zymogen into the enzymatically active plasmin. uPA is synthesized and secreted as the single-chain molecule (scuPA) composed of an N-terminal domain (GFD) and kringle (KD) and C-terminal proteolytic (PD) domains. Earlier, the structure of ATF (which consists of GFD(More)
We studied the effect of urokinase, its recombinant forms, and domain fragments on migration and proliferation of adipose tissue mesenchymal stromal cells (MSCs) and MMP secretion by these cells. Urokinase, but not its recombinant forms, slightly induced directed migration of MSCs. Spontaneous migration of MSCs increased under the action of urokinase or its(More)
In cultured fibroblasts, urokinase stimulated expression of MMP-9 and generation of ROS, while antioxidant ebselen abolished the stimulating effect of urokinase on MMP-9 expression. sTNF-α produced similar and more pronounced stimulating effect. The data showed that urokinase could regulate MMP-9 expression via ROS generation in fibroblasts, which can play(More)
Proteolytically inactive recombinant forms of urokinase (uPAHQ and amino-terminal fragment) inhibit spontaneous migration of endothelial cells; amino-terminal fragment also suppresses angiogenesis stimulated by basic fi broblast growth factor in vitro. These fi ndings suggest the possibility of using synthesized proteolytically inactive recombinant forms of(More)
The inhibitory effect of the non-hydrolyzable GTP analog Gpp (NH) p (10(-5)-10(-3) M) on the specific binding of some natural odorants (L-3H-amino acids, boar sex pheromone analog 5 alpha-3H-androstan-3-one) and sex hormones (17 beta-3H-estradiol, 3H-testosterone and 5 alpha-3H-dihydrotestosterone) to the olfactory receptors of some vertebrates (fish, frog,(More)
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