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Post-transcriptional regulation of gene expression in the plasminogen activation system.
No full textThe urokinase-mediated plasminogen activation (PA) system has been shown to play a key role in cell migration and tissue invasion by regulating both cell-associated proteolysis and cell-cell and cell-matrix interactions. The expression and activity of the components of this complex system are strictly regulated. The control of the expression occurs both at transcriptional and post-transcriptional levels. This review is focused on the post-transcriptional regulation of gene expression of all components of the PA system
Il Recettore dell’attivatore del plasminogeno di tipo urochinasi in cellule tiroidee: caratterizzazione e funzione
No full textPost-transcriptional regulation of gene expression in the plasminogen activation system.
No full textThe urokinase-mediated plasminogen activation (PA) system has been shown to play a key role in cell migration and tissue invasion by regulating both cell-associated proteolysis and cell-cell and cell-matrix interactions. The expression and activity of the components of this complex system are strictly regulated. The control of the expression occurs both at transcriptional and post-transcriptional levels. This review is focused on the post-transcriptional regulation of gene expression of all components of the PA system
Urokinase-type plasminogen-activator receptor associates to a cell surface molecule in monocytic cells.
No full textThe monocyte-like THP-1 cells express on their surface the urokinase-type plasminogen activator receptor (uPA-R). This receptor, chemically cross-linked to its possible ligands, migrates, in SDS PAGE, slower than the uPA-R expressed on
the epithelial thyroid cell line TAD-2, cross-linked to the same ligands. The different migration corresponds to a difference in molecular weight of 15 kDa.
Similar results were obtained with peripheral monocytes and primary cultures of thyroid cells. The molecular weight of the native receptor is about 50 kDa and appears to be identical in these two cell types. Such results suggest that, in monocytic cells, uPA-R associates to a 15 kDa molecule. This molecule is probably linked to the cell surface by a glyco-phospho-inositol anchor since, by phospholipase-C treatment, it is co-eluted with the urokinase-type plasminogen activator receptor from THP-1 cells
Urokinase-type plasminogen activator/type-2 plasminogen activator inhibitor complexes are not internalized upon binding to the urokinase- type-plasminogen- activator receptor in THP-1 cells.
No full textUrokinase-type plasminogen-activator receptor associates to a cell surface molecule in monocytic cells.
No full textThe monocyte-like THP-1 cells express on their surface the urokinase-type plasminogen activator receptor (uPA-R). This receptor, chemically cross-linked to its possible ligands, migrates, in SDS PAGE, slower than the uPA-R expressed on
the epithelial thyroid cell line TAD-2, cross-linked to the same ligands. The different migration corresponds to a difference in molecular weight of 15 kDa.
Similar results were obtained with peripheral monocytes and primary cultures of thyroid cells. The molecular weight of the native receptor is about 50 kDa and appears to be identical in these two cell types. Such results suggest that, in monocytic cells, uPA-R associates to a 15 kDa molecule. This molecule is probably linked to the cell surface by a glyco-phospho-inositol anchor since, by phospholipase-C treatment, it is co-eluted with the urokinase-type plasminogen activator receptor from THP-1 cells
Soluble and cleaved forms of the urokinase-receptor: degradation products or active molecules?
No full textThe urokinase-mediated plasminogen activation (PA) system is involved in many physiological and pathological events that include cell migration and tissue remodelling, such as embryogenesis, ovulation, inflammation, wound healing, angiogenesis, and tumor invasion and metastasis. The urokinase receptor (uPAR) is a key molecule of this system and can bind extracellular and cell membrane molecules such as urokinase (uPA), vitronectin (VN), integrins and chemotaxis receptors. These multiple interactions can be modulated by the shedding or the cleavage of the cell membrane receptor. Indeed, cleaved forms of uPAR, lacking the N-terminal D1 domain, have been detected on the surface of cells and in tissues, while soluble forms have been found in biological fluids. Cleaved and soluble forms could represent the intermediary products of the uPAR metabolism or active molecules with precise and distinct functional roles. Here, we review the data concerning the in vitro and in vivo identification of these uPAR forms, their origin and functions, and the role that uPAR shedding and cleavage could play in biological processes
Processing of complex between urokinase and its type-2 inhibitor on the cell-surface: a possible regulatory mechanism of urokinase activity.
No full textProcessing of complex between urokinase and its type-2 inhibitor on the cell-surface: a possible regulatory mechanism of urokinase activity.
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