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Fibronectin fibrillogenesis: a paradigm for extracellular matrix assembly
J E Schwarzbauer1, J L Sechler
1Department of Molecular Biology Princeton University Princeton, NJ 08544-1014, USA. jschwarzbauer@molbio.princeton.edu.
Current Opinion in Cell Biology
|October 6, 1999
Summary
Fibronectin and laminin matrix assembly are cell-mediated processes. Recent studies reveal insights into fibronectin assembly mechanisms and extracellular matrix control of cell functions.
Area of Science:
- Cell biology
- Biochemistry
- Extracellular matrix research
Background:
- Fibronectin matrix assembly is a complex, regulated process.
- Understanding extracellular matrix (ECM) assembly is crucial for cell function.
- Previous research focused on individual components of ECM assembly.
Purpose of the Study:
- To provide new insights into fibronectin matrix assembly mechanisms.
- To explore the role of fibronectin domains, integrins, and cytoskeleton.
- To investigate the common pathways in extracellular matrix assembly.
Main Methods:
- Analysis of fibronectin domains.
- Investigation of integrin and cytoskeletal contributions.
- Examination of fibronectin fibril architecture.
Main Results:
- New insights into fibronectin assembly mechanisms were gained.
- The contribution of fibronectin domains, integrins, and cytoskeleton to assembly was clarified.
- Fibronectin matrix assembly is a regulated, stepwise process.
Conclusions:
- A common cell-mediated pathway for extracellular matrix assembly is emerging.
- Fibronectin and laminin polymerization share common assembly mechanisms.
- ECM assembly pathways significantly influence cell functions.