{"title":"纤溶酶原受体介导细胞周围蛋白水解","authors":"Edward F. Plow , Lindsey A. Miles","doi":"10.1016/0922-3371(90)90042-U","DOIUrl":null,"url":null,"abstract":"<div><p>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 α<sub>2</sub>-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.</p></div>","PeriodicalId":77508,"journal":{"name":"Cell differentiation and development : the official journal of the International Society of Developmental Biologists","volume":"32 3","pages":"Pages 293-298"},"PeriodicalIF":0.0000,"publicationDate":"1990-12-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0922-3371(90)90042-U","citationCount":"61","resultStr":"{\"title\":\"Plasminogen receptors in the mediation of pericellular proteolysis\",\"authors\":\"Edward F. Plow , Lindsey A. Miles\",\"doi\":\"10.1016/0922-3371(90)90042-U\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>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 α<sub>2</sub>-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.</p></div>\",\"PeriodicalId\":77508,\"journal\":{\"name\":\"Cell differentiation and development : the official journal of the International Society of Developmental Biologists\",\"volume\":\"32 3\",\"pages\":\"Pages 293-298\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1990-12-11\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1016/0922-3371(90)90042-U\",\"citationCount\":\"61\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Cell differentiation and development : the official journal of the International Society of Developmental Biologists\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/092233719090042U\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Cell differentiation and development : the official journal of the International Society of Developmental Biologists","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/092233719090042U","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Plasminogen receptors in the mediation of pericellular proteolysis
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 α2-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.