The Role of Proteases in Fibronectin Matrix Remodeling in Thyroid Epithelial Cell Monolayer Cultures
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Luigi Nezi
Abstract
Fischer rat thyroid (FRT) cells organize a matrix of extracellular fibronectin (FN) fibrils, which undergoes extensive remodeling according to cell culture confluence. In nonconfluent cells FN forms a fibrillar array associated with the ventral cell surface. However, basal FN is progressively removed in confluent cultures and substituted by nonfibrillar FN deposits at lateral cell domains in regions of cellcell contacts. FRT cells secrete and expose on the plasma membrane the tissuetype plasminogen activator and, in serumfree cultures, plasminogen induces a rapid loss of FN fibrils. Incubation with plasmin inhibitors greatly reduces this effect. FRT cells also express annexin II, a plasminogen receptor, suggesting that plasmin activity is associated with the pericellular enviroment. This is in agreement with the observation that a great reduction in FN degradation is observed if the cells are preincubated with carboxypeptidase B, which prevents plasminogen binding to the cells. A gelatinolytic activity with a molecular weigth equivalent to MMP-2 has been demonstrated by zymography of culture media, and the presence of MMP-2 and MT1-MMP on the cell plasma membrane has been detected by immunofluorescence. These results indicate that in the FN remodeling process, occurring during FRT epithelium maturation, both plasmindependent (tPA activated) and plasminindependent proteolytic activities are involved.
Copyright © 2002 by Walter de Gruyter GmbH & Co. KG
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Articles in the same Issue
- Non-Enzymatic Activities of Proteases: From Scepticism to Reality
- The Urokinase Plasminogen Activator Receptor in the Regulation of the Actin Cytoskeleton and Cell Motility
- The Molecular Basis for Anti-Proteolytic and Non-Proteolytic Functions of Plasminogen Activator Inhibitor Type-1: Roles of the Reactive Centre Loop, the Shutter Region, the Flexible Joint Region and the Small Serpin Fragment
- Nervous System Pathology: The Fibrin Perspective
- Post-Transcriptional Regulation of Gene Expression in the Plasminogen Activation System
- Role of Myofibroblasts at the Invasion Front
- Transmodulation of Cell Surface Regulatory Molecules via Ectodomain Shedding
- The Plasminogen Activating System in Periodontal Health and Disease
- Apolipoprotein(a): Structure-Function Relationship at the Lysine-Binding Site and Plasminogen Activator Cleavage Site
- Anti-Invasive Effects of Green Tea Polyphenol EpiGalloCatechin-3-Gallate (EGCG), a Natural Inhibitor of Metallo and Serine Proteases
- Inhibition of Receptor-Dependent Urokinase Signaling by Specific Ser to Glu Substitutions
- Activation of p38 MAP-Kinase and Caldesmon Phosphorylation Are Essential for Urokinase-Induced Human Smooth Muscle Cell Migration
- Growth Factor-Dependent Proliferation and Invasion of Muscle Satellite Cells Require the Cell-Associated Fibrinolytic System
- The Col-1 Module of Human Matrix Metalloproteinase-2 (MMP-2): Structural/Functional Relatedness between Gelatin-Binding Fibronectin Type II Modules and Lysine-Binding Kringle Domains
- Random Peptide Bacteriophage Display as a Probe for Urokinase Receptor Ligands
- Plasmin Produces an E-Cadherin Fragment That Stimulates Cancer Cell Invasion
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- Induction of Fibronectin mRNA by Urokinase- and Tissue-Type Plasminogen Activator in Human Skin Fibroblasts: Differential Role of u-PA and t-PA at the Fibronectin Protein Level
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- UVA Light Stimulates the Production of Cathepsin G and Elastase-Like Enzymes by Dermal Fibroblasts: A Possible Contribution to the Remodeling of Elastotic Areas in Sun-Damaged Skin
- uPA-Silica-Particles (SP-uPA): A Novel Analytical System to Investigate uPA-uPAR Interaction and to Test Synthetic uPAR Antagonists as Potential Cancer Therapeutics
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- Osteopontin Modulates Prostate Carcinoma Invasive Capacity through RGD-Dependent Upregulation of Plasminogen Activators
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