Activated protein C enhances tPA-catalyzed Glu-plasminogen activation in the presence of poly-D-lysine [2]

Thrombosis and Haemostasis

Volumn 92, Issue 4, 2004, Pages 891-892

  Hryszko, Tomasz ^a,b   Urano, Tetsumei ^a  

^a HAMAMATSU UNIVERSITY SCHOOL OF MEDICINE   (Japan)

^b MEDICAL UNIVERSITY OF BIALYSTOK   (Poland)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATED PROTEIN C; FIBRIN; GLUTAMIC ACID; PLASMIN; PLASMINOGEN; POLY DEXTRO LYSINE; PROTEIN S; TISSUE PLASMINOGEN ACTIVATOR;

CATALYSIS; CONTROLLED STUDY; FIBRINOLYSIS; HYDROLYSIS; LETTER; PHENOMENOLOGY; PLASMINOGEN ACTIVATION; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN MODIFICATION; SEQUENCE ANALYSIS; STATISTICAL SIGNIFICANCE;

EID: 6344258862     PISSN: 03406245     EISSN: None     Source Type: Journal    
DOI: 10.1055/s-0037-1614198     Document Type: Letter

References (3)

1. Miles LA, Castellino FJ, Gong Y. Critical role for conversion of glu-plasminogen to lys-plasminogen for optimal stimulation of plasminogen activation on cell surfaces. Trends Cardiovasc Med 2003; 13: 21-30.
2. Urano T, Castellino F, Ihara H, et al. Activated protein C attenuates coagulation-associated over-expression of fibrinolytic activity by suppressing the thrombin-dependent inactivation of PAI-1. J Thromb Haemost 2003; 1: 2615-20.
3. Petersen LC, Suenson E. Trinitrobenzoylated poly(D-lysine) as a stimulator of interactions between plasminogen, plasmin, and tissue-type plasminogen activator. Biochim Biophys Acta 1986; 883: 313-25.