Binding of carboxypeptidase N to fibrinogen and fibrin

Biochemical and Biophysical Research Communications

Volumn 427, Issue 2, 2012, Pages 421-425

  Talens, S ^a   Lebbink, J H G ^a   Malfliet, J J M C ^a   Demmers, J A A ^a   Uitte de Willige, S ^a   Leebeek, F W G ^a   Rijken, D C ^a  

^a ERASMUS MEDICAL CENTER   (Netherlands)

Author keywords

Carboxypeptidase N; Coagulation; Fibrinogen; Fibrinolysis

Indexed keywords

APROTININ; ARGININE CARBOXYPEPTIDASE; CALCIUM CHLORIDE; FIBRIN; FIBRINOGEN; THROMBIN;

AMINO ACID SEQUENCE; ARTICLE; BLOOD CLOT; COVALENT BOND; HUMAN; ISOELECTRIC POINT; MASS SPECTROMETRY; MOLECULAR WEIGHT; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN FUNCTION; PROTEIN PROCESSING; SURFACE PLASMON RESONANCE; TWO DIMENSIONAL GEL ELECTROPHORESIS; WESTERN BLOTTING;

BLOOD COAGULATION; FIBRIN; FIBRINOGEN; FIBRINOLYSIS; HUMANS; LYSINE CARBOXYPEPTIDASE; PROTEIN BINDING; SURFACE PLASMON RESONANCE;

EID: 84867882712     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2012.09.081     Document Type: Article

References (18)

1. Weisel J.W. Fibrinogen and fibrin. Adv. Protein Chem. 2005, 70:247-299.
2. Lord S.T. Fibrinogen and fibrin: scaffold proteins in hemostasis. Curr. Opin. Hematol. 2007, 14:236-241.
3. Wolberg A.S. Plasma and cellular contributions to fibrin network formation structure and stability. Haemophilia 2010, 16(Suppl. 3):7-12.
4. Rijken D.C., Lijnen H.R. New insights into the molecular mechanisms of the fibrinolytic system. J. Thromb. Haemost. 2009, 7:4-13.
5. Erdos E.G., Sloane E.M. An enzyme in human blood plasma that inactivates bradykinin and kallidins. Biochem. Pharmacol. 1962, 11:585-592.
6. Bokisch V.A., Muller-Eberhard H.J. Anaphylatoxin inactivator of human plasma: its isolation and characterization as a carboxypeptidase. J. Clin. Invest. 1970, 49:2427-2436.
7. Skidgel R.A., Erdos E.G. Structure and function of human plasma carboxypeptidase N the anaphylatoxin inactivator. Int. Immunopharmacol. 2007, 7:1888-1899.
8. Levin Y., Skidgel R.A., Erdos E.G. Isolation and characterization of the subunits of human plasma carboxypeptidase N (kininase i). Proc. Natl. Acad. Sci. USA 1982, 79:4618-4622.
9. Quagraine M.O., Tan F., Tamei H., Erdos E.G., Skidgel R.A. Plasmin alters the activity and quaternary structure of human plasma carboxypeptidase N. Biochem. J. 2005, 388:81-91.
10. Talens S., Leebeek F.W., Demmers J.A., Rijken D.C. Identification of fibrin clot-bound plasma proteins. PLoS One 2012, 7:e41966.
11. Walker J.B., Binette T.M., Mackova M., Lambkin G.R., Mitchell L., Bajzar L. Proteolytic cleavage of carboxypeptidase N markedly increases its antifibrinolytic activity. J. Thromb. Haemost. 2008, 6:848-855.
12. Rijken D.C., Dirkx S.P., Luider T.M., Leebeek F.W. Hepatocyte-derived fibrinogen-related protein-1 is associated with the fibrin matrix of a plasma clot. Biochem. Biophys. Res. Commun. 2006, 350:191-194.
13. Howes J.M., Richardson V.R., Smith K.A., Schroeder V., Somani R., Shore A., Hess K., Ajjan R., Pease R.J., Keen J.N., Standeven K.F., Carter A.M. Complement C3 is a novel plasma clot component with anti-fibrinolytic properties. Diab. Vasc. Dis. Res. 2012, 9:216-225.
14. Willemse J.L., Chen D., Hendriks D.F. Major carboxypeptidase N deficiency. Clin. Chim. Acta 2008, 389:181-182.
15. Mathews K.P., Curd J.G., Hugli T.E. Decreased synthesis of serum carboxypeptidase N (SCPN) in familial SCPN deficiency. J. Clin. Immunol. 1986, 6:87-91.
16. Bouma B.N., Marx P.F., Mosnier L.O., Meijers J.C. Thrombin-activatable fibrinolysis inhibitor (TAFI, plasma procarboxypeptidase B, procarboxypeptidase R, procarboxypeptidase U). Thromb. Res. 2001, 101:329-354.
17. Plow E.F., Allampallam K., Redlitz A. The plasma carboxypeptidases and the regulation of the plasminogen system. Trends Cardiovasc. Med. 1997, 7:71-75.
18. Walker J.B., Bajzar L. The intrinsic threshold of the fibrinolytic system is modulated by basic carboxypeptidases but the magnitude of the antifibrinolytic effect of activated thrombin-activable fibrinolysis inhibitor is masked by its instability. J. Biol. Chem. 2004, 279:27896-27904.