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RGD and other recognition sequences for integrins
1La Jolla Cancer Research Center, Burnham Institute, California 92037, USA.
Annual Review of Cell and Developmental Biology
|January 1, 1996
Summary
The Arg-Gly-Asp (RGD) sequence is key for cell adhesion, mediating interactions with integrins. RGD peptides and mimics offer therapeutic potential for diseases like cancer and thrombosis.
Area of Science:
- Biochemistry
- Cell Biology
- Biotechnology
Background:
- Proteins with Arg-Gly-Asp (RGD) sites and their integrin receptors are crucial for cell adhesion.
- The RGD sequence is present in many adhesive proteins, recognized by nearly half of known integrins.
Purpose of the Study:
- To explore the role of RGD sequences and integrins in cell adhesion and related biological processes.
- To investigate the potential of RGD peptides and mimics in biological research and drug development.
Main Methods:
- Utilizing synthetic peptides containing the RGD sequence to mimic natural ligand binding.
- Designing selective RGD-directed integrin binders through peptide cyclization and RGD mimic synthesis.
Main Results:
- Insolubilized RGD peptides promote cell adhesion, while soluble peptides inhibit it.
- Selective RGD-integrin binding reagents can be synthesized for targeted applications.
Conclusions:
- RGD peptides and mimics are valuable tools for studying integrin functions in cell migration, growth, differentiation, and apoptosis.
- RGD-based drug design holds promise for treating diseases including thrombosis, osteoporosis, and cancer.