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Revisiting the antifibrinolytic effect of carboxypeptidase N: novel structure and regulation Open Access

Descriptions

Other title
Subject/Keyword
CPN inhibitor
fibrinolysis
clot lysis
fibrinogen
carboxypeptidase N
hemostasis
plasminogen activation
(DD)E
lysine
inflammation
Type of item
Thesis
Degree grantor
University of Alberta
Author or creator
Swanson, Pascale Libront
Supervisor and department
Schulz, Richard (Pediatrics)
Bajzar, Laszlo (Pediatrics)
Examining committee member and department
Michalak, Marek (Biochemistry)
Department
Medical Sciences - Pediatrics
Specialization

Date accepted
2010-07-09T19:30:06Z
Graduation date
2010-11
Degree
Master of Science
Degree level
Master's
Abstract
Carboxypeptidase N (CPN) is a plasma carboxypeptidase that was discovered in the 1960s as a regulator of inflammation and vascular tone. Through the removal of carboxy-terminal basic residues, CPN alters the activity or binding specificity of inflammatory mediators and vasoactive peptides. CPN shares significant homology with carboxypeptidases known to mediate antifibrinolysis through the removal of basic residues from fibrin clots, which would otherwise stimulate fibrinolysis. Despite the similarity of these enzymes, CPN is generally regarded as lacking a role in fibrinolysis. This thesis demonstrates that CPN is indeed a capable antifibrinolytic enzyme, and that the antifibrinolytic activity of CPN was previously undisclosed due to the presence of a circulating CPN inhibitor, which is likely the free CPN2 subunit. This inhibitor is described for the first time here. Furthermore, potential mechanisms of inhibition and mechanisms of enhancing activity of CPN are proposed based upon the additional structural characterization of CPN presented here.
Language
English
Rights
License granted by Pascale Swanson (pascales@ualberta.ca) on 2010-07-09T17:10:14Z (GMT): Permission is hereby granted to the University of Alberta Libraries to reproduce single copies of this thesis and to lend or sell such copies for private, scholarly or scientific research purposes only. Where the thesis is converted to, or otherwise made available in digital form, the University of Alberta will advise potential users of the thesis of the above terms. The author reserves all other publication and other rights in association with the copyright in the thesis, and except as herein provided, neither the thesis nor any substantial portion thereof may be printed or otherwise reproduced in any material form whatsoever without the author's prior written permission.
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