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Mitogenic properties of major extracellular proteins
J P Lévesque1, A Hatzfeld, J Hatzfeld
1Laboratoire de Biologie Cellulaire et Moléculaire des Facteurs de Croissance (Centre National de la Recherche Scientifique), Höpital Paul-Brousse, Villejuif, France.
Immunology Today
|August 1, 1991
Summary
Major plasma and extracellular matrix proteins possess multiple functions. These proteins bind distinct receptors, suggesting common evolutionary origins for cell adhesion molecules and growth factors.
Area of Science:
- Biochemistry
- Cell Biology
- Evolutionary Biology
Background:
- Plasma and extracellular matrix proteins are multifunctional.
- Some proteins, like fibrinogen and C3, contain domains that bind to both adhesion and mitogenic receptors.
Purpose of the Study:
- To review adhesion and mitogenic receptors that interact with distinct domains of extracellular matrix proteins.
- To explore the evolutionary origins of cell adhesion molecules and related proteins.
Main Methods:
- Literature review of scientific publications.
- Analysis of protein domain functions and receptor interactions.
- Discussion of evolutionary hypotheses.
Main Results:
- Extracellular matrix proteins exhibit dual-binding capabilities for different receptor types.
- Evidence suggests distinct domains on proteins like fibrinogen and C3 bind specific receptors.
- The review highlights the potential for shared ancestry among various cell signaling molecules.
Conclusions:
- Multifunctional extracellular matrix proteins play key roles in cell signaling.
- The distinct domain binding supports complex cellular communication pathways.
- Common ancestral genes may underlie the evolution of cell adhesion molecules, extracellular matrix proteins, and growth factor systems.