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Published on: February 7, 2018
Recombinant human collagen XV regulates cell adhesion and migration.
Merja Hurskainen1, Florence Ruggiero, Pasi Hägg
1Oulu Centre for Cell-Matrix Research, Department of Medical Biochemistry and Molecular Biology, Institute of Biomedicine, University of Oulu, 90014 Oulu, Finland.
The Journal of Biological Chemistry
|December 31, 2009
Summary
Full-length collagen XV was produced and purified, revealing its molecular structure. This collagen binds to extracellular matrix proteins and inhibits fibrosarcoma cell adhesion and migration within fibronectin networks.
Area of Science:
- Biochemistry
- Molecular Biology
- Extracellular Matrix Research
Background:
- The C-terminal domain (restin) of collagen XV is studied, but the functions of the full-length protein remain unclear.
- Understanding full-length collagen XV is crucial for elucidating its biological roles.
Purpose of the Study:
- To produce, purify, and characterize full-length human collagen XV.
- To investigate the functional interactions of collagen XV with cells and extracellular matrix components.
- To generate a monoclonal antibody targeting the N-terminus of collagen XV.
Main Methods:
- Production of full-length human collagen XV in insect cells using baculovirus expression system.
- Purification from cell culture medium, yielding 15 mg/liter.
- Characterization using rotary shadowing electron microscopy and N-terminal antibody binding.
- Cell adhesion assays and solid-phase binding assays to assess interactions with extracellular matrix proteins and cell lines.
Main Results:
- Purified collagen XV is a trimeric, rod-like molecule (mean length 241.8 nm) with a globular N-terminal domain.
- Collagen XV does not support direct cell adhesion but binds to fibronectin, laminin, and vitronectin.
- It specifically interacts with the collagen/gelatin-binding domain of fibronectin and inhibits fibrosarcoma cell adhesion and migration in fibronectin-containing matrices.
Conclusions:
- Full-length collagen XV possesses distinct structural and binding properties.
- Collagen XV modulates cell behavior, specifically inhibiting fibrosarcoma cell adhesion and migration through interactions with the fibronectin network.
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