TY - JOUR
T1 - Critical role for conversion of Glu-plasminogen to Lys-plasminogen for optimal stimulation of plasminogen activation on cell surfaces
AU - Miles, Lindsey A.
AU - Castellino, Francis J.
AU - Gong, Yun
N1 - Funding Information:
Research in the authors' laboratories was supported by National Institutes of Health grants HL38272 and HL45934 (to L.A.M.), and HL13423 (to F.J.C.); and American Heart grant-in-aid 9650636N (to L.A.M.).
PY - 2003/1
Y1 - 2003/1
N2 - When Glu-plasminogen, the native circulating form of the zymogen, is bound to cell surfaces, its activation is markedly enhanced compared with the reaction in solution. This results in localization of the broad-spectrum proteolytic activity of plasmin on cell surfaces. The cell-associated plasmin plays a key role in fibrinolysis, cell migration, and prohormone processing. It is well established that the localization of plasminogen and plasminogen activators on cell surfaces promotes the enhanced plasminogen activation on the cell surface. The focus of this article is to review recent studies demonstrating that the conversion of Glu-plasminogen to the more readily activated Lys-plasminogen derivative is necessary for optimal stimulation of plasminogen activation on the cell surface, and that the interaction of Glu-plasminogen with cells serves to increase processing of Glu-plasminogen to Lys-plasminogen, thereby enhancing plasminogen activation on the cell surface.
AB - When Glu-plasminogen, the native circulating form of the zymogen, is bound to cell surfaces, its activation is markedly enhanced compared with the reaction in solution. This results in localization of the broad-spectrum proteolytic activity of plasmin on cell surfaces. The cell-associated plasmin plays a key role in fibrinolysis, cell migration, and prohormone processing. It is well established that the localization of plasminogen and plasminogen activators on cell surfaces promotes the enhanced plasminogen activation on the cell surface. The focus of this article is to review recent studies demonstrating that the conversion of Glu-plasminogen to the more readily activated Lys-plasminogen derivative is necessary for optimal stimulation of plasminogen activation on the cell surface, and that the interaction of Glu-plasminogen with cells serves to increase processing of Glu-plasminogen to Lys-plasminogen, thereby enhancing plasminogen activation on the cell surface.
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U2 - 10.1016/S1050-1738(02)00190-1
DO - 10.1016/S1050-1738(02)00190-1
M3 - Review article
C2 - 12554097
AN - SCOPUS:12244293338
SN - 1050-1738
VL - 13
SP - 21
EP - 30
JO - Trends in Cardiovascular Medicine
JF - Trends in Cardiovascular Medicine
IS - 1
ER -