PLASMINOGEN RECEPTORS IN THE MEDIATION OF PERICELLULAR PROTEOLYSIS

被引:49
作者
PLOW, EF [1 ]
MILES, LA [1 ]
机构
[1] Scripps Res Inst, RES INST, COMM VASC BIOL, LA JOLLA, CA 92037 USA
来源
CELL DIFFERENTIATION AND DEVELOPMENT | 1990年 / 32卷 / 03期
关键词
PLASMINOGEN; PERICELLULAR PROTEOLYSIS;
D O I
10.1016/0922-3371(90)90042-U
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
A wide variety of cells bind plasminogen with very high capacity, with similar affinity and recognize the same structural features within the plasminogen molecule. As a consequence of binding to cell surfaces, plasminogen is more readily activated to plasmin. Plasmin remains cell-bound where it can degrade matrix constituents and is protected from inactivation by alpha-2-antiplasmin. Thus, the functional consequence of plasminogen binding to cells is pericellular proteolysis, permitting cell migration. Both proteins and nonprotein cell-surface constituents function as plasminogen binding sites. Gangliosides exhibit the appropriate properties of the non-protein plasminogen receptors.
引用
收藏
页码:293 / 298
页数:6
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