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Characterization of lymphocyte fibronectin
D Hauzenberger1, N Martin, S Johansson
1Department of Clinical Immunology, Karolinska Institute, Huddinge Hospital, Sweden.
Experimental Cell Research
|February 1, 1996
Summary
Activated T-lymphocytes synthesize fibronectin, a gelatin-binding protein, while resting cells do not. This fibronectin production is regulated by cell activation signals and specific mRNA isoforms are expressed.
Area of Science:
- Immunology
- Molecular Biology
- Cell Biology
Background:
- Lymphocytes play crucial roles in immune responses.
- Fibronectin is a key extracellular matrix protein involved in cell adhesion and signaling.
- The synthesis and function of fibronectin in lymphocytes are not fully understood.
Purpose of the Study:
- To investigate fibronectin synthesis by human lymphocytes.
- To determine the regulation of fibronectin production in T-lymphocytes.
- To characterize the fibronectin isoforms expressed by T-cells.
Main Methods:
- In vitro culture of peripheral blood lymphocytes and T-cell lines.
- Detection of gelatin-binding molecules using Western blotting.
- Immunocytochemistry for fibronectin localization.
- RT-PCR to analyze fibronectin mRNA expression.
Main Results:
- Activated lymphocytes and T-cell lines synthesize a 500 kDa gelatin-binding molecule identified as fibronectin.
- Fibronectin synthesis is potentiated by Concanavalin A-mediated lymphocyte anchorage.
- Lymphocyte-derived fibronectin is primarily cell-associated.
- T-lymphocytes predominantly express fibronectin mRNA isoforms lacking the III CS exon, which encodes the LDV binding region.
Conclusions:
- T-lymphocytes synthesize fibronectin, and its production is regulated by cell activation signals.
- The expression of specific fibronectin mRNA isoforms in T-cells suggests unique functional roles.
- This study demonstrates fibronectin synthesis in T-lymphocytes, contributing to understanding lymphocyte-matrix interactions.