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

Details

Serval ID
serval:BIB_194DA513D1BC
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
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
Journal
Journal of Immunology
Author(s)
Gundersen  D., Tran-Thang  C., Sordat  B., Mourali  F., Ruegg  C.
ISSN
0022-1767 (Print)
Publication state
Published
Issued date
02/1997
Volume
158
Number
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
Abstract
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.
Keywords
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
Create date
28/01/2008 9:36
Last modification date
20/08/2019 13:50
Usage data