Related Experiment Videos
Cross-talk between insulin receptor and integrin alpha5 beta1 signaling pathways
A Guilherme1, K Torres, M P Czech
1Program in Molecular Medicine and Department of Biochemistry and Molecular Biology, University of Massachusetts Medical Center, Worcester, Massachusetts 01605, USA.
The Journal of Biological Chemistry
|August 29, 1998
Summary
Insulin enhances cell adhesion by activating alpha5beta1 integrins, which in turn amplifies insulin receptor signaling. This synergy between insulin receptor and integrin pathways promotes cell adhesion.
Area of Science:
- Cell Biology
- Biochemistry
- Molecular Signaling
Background:
- Cell surface integrins mediate cell adhesion and initiate signaling pathways.
- Insulin signaling regulates various cellular processes.
Purpose of the Study:
- To investigate the role of alpha5beta1 integrins in insulin-stimulated cell adhesion.
- To elucidate the synergistic interaction between insulin receptor and integrin signaling.
Main Methods:
- Utilized Chinese hamster ovary cells expressing insulin receptors (CHO-T).
- Assessed cell adhesion on fibronectin matrix using GRGDSP peptide and wortmannin.
- Employed anti-alpha5beta1 integrin antibody (PB-1) to block integrin function.
- Measured insulin receptor and insulin receptor substrate (IRS)-1 tyrosine phosphorylation.
Main Results:
- Insulin treatment significantly increased CHO-T cell adhesion to fibronectin.
- This effect was blocked by GRGDSP peptide and PI 3-kinase inhibitor wortmannin.
- Activating alpha5beta1 integrins potentiated insulin-induced tyrosine phosphorylation of insulin receptor and IRS-1.
- Integrin activation enhanced PI 3-kinase recruitment to IRS-1.
Conclusions:
- Insulin activates alpha5beta1 integrin-mediated cell adhesion.
- Alpha5beta1 integrin signaling enhances insulin receptor kinase activity and IRS-1/PI 3-kinase complex formation.
- Insulin receptor and alpha5beta1 integrin signaling act synergistically to promote cell adhesion.