Activated thrombin-activatable fibrinolysis inhibitor (TAFIa) attenuates breast cancer cell metastatic behaviors through inhibition of plasminogen activation and extracellular proteolysis

Authors

Zainab Ali Bazzi, University of WindsorFollow
Danielle Lanoue, University of WindsorFollow
Mouhanned El-Youssef, Universty of WindsorFollow
Rocco Romagnuolo, University of Windsor
Janice Tubman, University of WindsorFollow
Dora Cavallo-Medved, University of WindsorFollow
Lisa A. Porter, University of WindsorFollow
Michael B. Boffa, University of Windsor

Document Type

Article

Publication Date

5-24-2016

Publication Title

BMC Cancer

Volume

16

Issue

1

First Page

1

Last Page

12

Abstract

Thrombin activatable fibrinolysis inhibitor (TAFI) is a plasma zymogen, which can be converted to activated TAFI (TAFIa) through proteolytic cleavage by thrombin, plasmin, and most effectively thrombin in complex with the endothelial cofactor thrombomodulin (TM). TAFIa is a carboxypeptidase that cleaves carboxyl terminal lysine and arginine residues from protein and peptide substrates, including plasminogen-binding sites on cell surface receptors. Carboxyl terminal lysine residues play a pivotal role in enhancing cell surface plasminogen activation to plasmin. Plasmin has many critical functions including cleaving components of the extracellular matrix (ECM), which enhances invasion and migration of cancer cells. We therefore hypothesized that TAFIa could act to attenuate metastasis.

DOI

10.1186/s12885-016-2359-1

Recommended Citation

Bazzi, Zainab Ali; Lanoue, Danielle; El-Youssef, Mouhanned; Romagnuolo, Rocco; Tubman, Janice; Cavallo-Medved, Dora; Porter, Lisa A.; and Boffa, Michael B., "Activated thrombin-activatable fibrinolysis inhibitor (TAFIa) attenuates breast cancer cell metastatic behaviors through inhibition of plasminogen activation and extracellular proteolysis" (2016). BMC Cancer, 16, 1, 1-12.
https://scholar.uwindsor.ca/biologypub/104