Secreted protein acidic and rich in cysteine (SPARC/osteonectin/BM-40) binds to fibrinogen fragments D and E, but not to native fibrinogen

Hua Wang, Gail Workman, Shengfu Chen, Thomas H. Barker, Buddy D. Ratner, E. Helene Sage, Shaoyi Jiang

Research output: Contribution to journalArticle

12 Citations (Scopus)

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 languageEnglish (US)
Pages (from-to)20-26
Number of pages7
JournalMatrix Biology
Volume25
Issue number1
DOIs
StatePublished - Jan 2006
Externally publishedYes

Fingerprint

Osteonectin
Fibrinogen
Cysteine
Wound Healing
Fibrinolysin
Fibrinolysis
Proteins
Surface Plasmon Resonance
Biosensing Techniques
Extracellular Matrix
Blood Proteins
Cell Cycle
Thrombosis
Fibrosis
Endothelial Cells
Cell Proliferation
Inflammation
fibrinogen fragment E

Keywords

  • Fibrinogen
  • Fibrinolysis
  • SPARC
  • SPR
  • Wound healing

ASJC Scopus subject areas

  • Molecular Biology

Cite this

Secreted protein acidic and rich in cysteine (SPARC/osteonectin/BM-40) binds to fibrinogen fragments D and E, but not to native fibrinogen. / Wang, Hua; Workman, Gail; Chen, Shengfu; Barker, Thomas H.; Ratner, Buddy D.; Sage, E. Helene; Jiang, Shaoyi.

In: Matrix Biology, Vol. 25, No. 1, 01.2006, p. 20-26.

Research output: Contribution to journalArticle

Wang, Hua ; Workman, Gail ; Chen, Shengfu ; Barker, Thomas H. ; Ratner, Buddy D. ; Sage, E. Helene ; Jiang, Shaoyi. / Secreted protein acidic and rich in cysteine (SPARC/osteonectin/BM-40) binds to fibrinogen fragments D and E, but not to native fibrinogen. In: Matrix Biology. 2006 ; Vol. 25, No. 1. pp. 20-26.
@article{eba952e4b10447169c2bd09a51e99f6b,
title = "Secreted protein acidic and rich in cysteine (SPARC/osteonectin/BM-40) binds to fibrinogen fragments D and E, but not to native fibrinogen",
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.",
keywords = "Fibrinogen, Fibrinolysis, SPARC, SPR, Wound healing",
author = "Hua Wang and Gail Workman and Shengfu Chen and Barker, {Thomas H.} and Ratner, {Buddy D.} and Sage, {E. Helene} and Shaoyi Jiang",
year = "2006",
month = "1",
doi = "10.1016/j.matbio.2005.09.004",
language = "English (US)",
volume = "25",
pages = "20--26",
journal = "Matrix Biology",
issn = "0945-053X",
publisher = "Elsevier",
number = "1",

}

TY - JOUR

T1 - Secreted protein acidic and rich in cysteine (SPARC/osteonectin/BM-40) binds to fibrinogen fragments D and E, but not to native fibrinogen

AU - Wang, Hua

AU - Workman, Gail

AU - Chen, Shengfu

AU - Barker, Thomas H.

AU - Ratner, Buddy D.

AU - Sage, E. Helene

AU - Jiang, Shaoyi

PY - 2006/1

Y1 - 2006/1

N2 - 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.

AB - 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.

KW - Fibrinogen

KW - Fibrinolysis

KW - SPARC

KW - SPR

KW - Wound healing

UR - http://www.scopus.com/inward/record.url?scp=31344473092&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=31344473092&partnerID=8YFLogxK

U2 - 10.1016/j.matbio.2005.09.004

DO - 10.1016/j.matbio.2005.09.004

M3 - Article

C2 - 16263253

AN - SCOPUS:31344473092

VL - 25

SP - 20

EP - 26

JO - Matrix Biology

JF - Matrix Biology

SN - 0945-053X

IS - 1

ER -