Abstract
Secreted protein acidic and rich in cysteine (SPARC/osteonectin/BM-40) is a matricellular protein that functions in wound healing. Fibrinogen is a plasma protein involved in many aspects of wound healing, such as inflammation, fibrosis and thrombosis. In this study, the binding of SPARC to both native and plasmin-cleaved fibrinogen under physiological conditions was examined by the use of a surface plasmon resonance (SPR) biosensor. We show that SPARC binds to plasmin-cleaved fibrinogen, but not to native fibrinogen. SPARC binds to both fibrinogen fragments D and E fg D and fg E with similar dissociation constants (8.67 × 10- 8 M for Fg D and 1.61 × 10- 7 M for Fg E). Results from endothelial cell proliferation assays show that the binding of SPARC to Fg E suppressed the inhibition of proliferation by SPARC, whereas the binding of SPARC to Fg D did not influence the activity of SPARC on the cell cycle. The interaction of SPARC with fibrinogen fragments D and E, which are produced as a result of proteolytic activation of fibrinolysis, reveals potential storage sites in provisional extracellular matrix for SPARC during the wound healing process and indicates a regulatory role of SPARC in fibrinolysis and angiogenesis.
Original language | English (US) |
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Pages (from-to) | 20-26 |
Number of pages | 7 |
Journal | Matrix Biology |
Volume | 25 |
Issue number | 1 |
DOIs | |
State | Published - Jan 2006 |
Externally published | Yes |
Keywords
- Fibrinogen
- Fibrinolysis
- SPARC
- SPR
- Wound healing
ASJC Scopus subject areas
- Molecular Biology