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Superfibronectin is a functionally distinct form of fibronectin
A Morla1, Z Zhang, E Ruoslahti
1Cancer Research Center, La Jolla Cancer Research Foundation, California 92037.
Nature
|January 13, 1994
Summary
A fibronectin fragment induces self-assembly into matrix-like fibrils, creating superfibronectin with enhanced adhesion and suppressed cell migration. This superfibronectin utilizes both integrin and distinct receptors for cell attachment.
Area of Science:
- Biochemistry
- Cell Biology
- Extracellular Matrix Research
Background:
- Fibronectin (FN) is a crucial extracellular matrix protein involved in development, wound healing, and cancer.
- In circulation, FN exists as a dimer, while in tissues, it forms disulfide-crosslinked fibrils.
Purpose of the Study:
- To investigate the role of a specific fibronectin fragment in mediating fibronectin self-assembly and function.
- To characterize the properties of the induced fibronectin form, termed 'superfibronectin'.
Main Methods:
- Utilized a fibronectin fragment from the first type-III repeat.
- Induced spontaneous disulfide crosslinking of fibronectin molecules.
- Assessed changes in fibronectin adhesion and cell migration properties.
- Investigated cell attachment mechanisms to native and superfibronectin.
Main Results:
- A fibronectin fragment induced spontaneous disulfide crosslinking, forming high molecular mass multimers resembling matrix fibrils.
- This process converted fibronectin into 'superfibronectin' with significantly enhanced adhesive properties.
- Superfibronectin suppressed cell migration.
- Cell attachment to superfibronectin involved both integrins and novel, distinct receptors.
Conclusions:
- A specific fibronectin fragment can trigger the formation of matrix-like fibronectin structures (superfibronectin).
- Superfibronectin exhibits distinct cell adhesion properties mediated by integrins and other receptors.
- Superfibronectin may represent a biologically relevant form of the natural matrix fibronectin.