Related Experiment Videos
Matrix valency regulates integrin-mediated lymphoid adhesion via Syk kinase
D G Stupack1, E Li, S A Silletti
1Department of Immunology, The Scripps Research Institute, La Jolla, California 92037, USA.
The Journal of Cell Biology
|February 26, 1999
Summary
Lymphoid cells adhere to polymerized extracellular matrix (ECM) proteins, activating Syk kinase. This interaction regulates cell adhesion and retention within tissues.
Area of Science:
- Immunology
- Cell Biology
- Biochemistry
Background:
- Lymphocytes accumulate in tumor, wound, and inflammatory tissues, which contain polymerized extracellular matrix (ECM) proteins like fibrin and fibronectin.
- Nonactivated lymphocytes adhere to polymerized ECM proteins but not to monomeric forms without prior activation.
Purpose of the Study:
- To investigate the mechanism of nonactivated lymphoid cell adhesion to ECM proteins.
- To explore the role of Syk kinase and antigen receptors in this adhesion process.
Main Methods:
- Studied lymphoid cell adhesion to various forms of ECM proteins (polymerized vs. monomeric).
- Investigated the role of integrin spacing and Syk kinase activation in adhesion.
- Examined the effect of antigen receptor signaling on ECM adhesion.
Main Results:
- Lymphoid cell adhesion to polymerized ECM proteins triggers activation of Syk kinase within podosomes.
- Activation of Syk kinase, either by antigen or through a mutant, promotes adhesion to monomeric ECM proteins.
- A cooperative signaling interaction between integrins and antigen receptors regulates lymphoid cell adhesion and retention in the ECM.
Conclusions:
- Lymphoid cell adhesion to the ECM is a regulated process involving integrin and antigen receptor signaling.
- Syk kinase plays a crucial role in mediating lymphocyte adhesion and retention within remodeling tissue environments.