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Biosynthesis and processing of fibronectin in NIL.8 hamster cells
The Journal of Biological Chemistry
|December 10, 1979
Summary
Newly synthesized fibronectin rapidly dimerizes and is secreted as a dimer. This dimeric fibronectin undergoes carbohydrate processing and aggregation, becoming insoluble at the cell surface.
Area of Science:
- Biochemistry
- Cell Biology
- Glycobiology
Background:
- Fibronectin is a crucial extracellular matrix glycoprotein.
- Its synthesis and post-translational modifications are key to its function.
Purpose of the Study:
- To investigate the intracellular processing and secretion of fibronectin.
- To characterize the early post-translational modifications and assembly of fibronectin.
Main Methods:
- Metabolic labeling of cells to track fibronectin synthesis.
- Use of endoglycosidase H to analyze carbohydrate structures.
- Assessment of fibronectin solubility and aggregation.
Main Results:
- Fibronectin is initially synthesized as a monomer with high-mannose type glycans.
- Monomers dimerize intracellularly, and dimers are rapidly secreted.
- Secreted fibronectin exhibits complex-type glycans, indicating processing.
- Cell surface fibronectin transitions from soluble to insoluble forms and aggregates.
Conclusions:
- Fibronectin undergoes rapid intracellular dimerization and glycosylation processing.
- Secretion and cell surface association involve complex glycan modifications and aggregation.
- These processes are critical for fibronectin's extracellular matrix integration.