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  • http://hdl.handle.net/10048/1215
  • Revisiting the antifibrinolytic effect of carboxypeptidase N: novel structure and regulation
  • Swanson, Pascale Libront
  • en
  • carboxypeptidase N
    fibrinolysis
    inflammation
    clot lysis
    plasminogen activation
    (DD)E
    fibrinogen
    lysine
    CPN inhibitor
    hemostasis
  • Jul 9, 2010 7:30 PM
  • Thesis
  • en
  • Adobe PDF
  • 11370168 bytes
  • 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.
  • Master's
  • Master of Science
  • Medical Sciences - Pediatrics
  • Fall 2010
  • Bajzar, Laszlo (Pediatrics)
    Schulz, Richard (Pediatrics)
  • Michalak, Marek (Biochemistry)

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