Plasmin-induced proteolysis of tenascin-C: modulation by T lymphocyte-derived urokinase-type plasminogen activator and effect on T lymphocyte adhesion, activation, and cell clustering
Détails
ID Serval
serval:BIB_194DA513D1BC
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
Plasmin-induced proteolysis of tenascin-C: modulation by T lymphocyte-derived urokinase-type plasminogen activator and effect on T lymphocyte adhesion, activation, and cell clustering
Périodique
Journal of Immunology
ISSN
0022-1767 (Print)
Statut éditorial
Publié
Date de publication
02/1997
Volume
158
Numéro
3
Pages
1051-60
Notes
Journal Article
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S. --- Old month value: Feb 1
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S. --- Old month value: Feb 1
Résumé
Proteolysis and remodeling of the extracellular matrix occur physiologically in processes such as tissue morphogenesis and repair and may participate in the regulation of complex cell functions, including proliferation and differentiation. While matrix degradation appears to be relevant to T lymphocyte migration through tissues, little is known about whether degraded matrix affects T lymphocyte function. We have studied the interaction between T lymphocytes and tenascin-C (TN-C), a matrix protein we have previously reported to inhibit T lymphocyte activation, in the context of plasmin-induced degradation. Here we report that plasmin efficiently cleaves TN-C. Peripheral blood T lymphocytes stimulated with phorbol ester, anti-CD28, or anti-CD3 Ab, induce, within 24 to 48 h, a strong plasminogen-dependent proteolysis of TN-C. We demonstrate that stimulated T lymphocytes activate plasminogen by secreting the urokinase-type plasminogen activator (u-PA). Plasminogen activation by T lymphocyte-derived u-PA occurs efficiently in fluid phase in the absence of cells. We investigate the consequences of plasmin-induced proteolysis on three of the effects of TN-C in relation to lymphocyte functions. Plasmin proteolysis converts TN-C from a nonadhesive into an adhesive substrate for T lymphocytes and abolishes its aggregating activity on PBMC. In contrast, the inhibitory effect of TN-C on T lymphocyte activation remains unaffected. These observations demonstrate that stimulated T lymphocytes induce plasminogen-dependent proteolysis of TN-C by secreting u-PA and suggest that proteolysis of TN-C may represent a mechanism by which to regulate some of its effects on T lymphocyte functions.
Mots-clé
Cell Adhesion
Cell Aggregation
Cells, Cultured
Enzyme Activation
Fibronectins/metabolism
Gene Expression Regulation, Enzymologic
Humans
Lymphocyte Activation
Plasmin/*metabolism
Plasminogen/metabolism
RNA, Messenger/genetics
T-Lymphocytes/cytology/*enzymology
Tenascin/*metabolism
Urinary Plasminogen Activator/genetics/*metabolism
Pubmed
Web of science
Création de la notice
28/01/2008 9:36
Dernière modification de la notice
20/08/2019 13:50