New Insights into the Role of Plg-RKT in Macrophage Recruitment

被引:35
作者
Miles, Lindsey A. [1 ]
Lighvani, Shahrzad [1 ]
Baik, Nagyung [1 ]
Parmer, Caitlin M. [2 ]
Khaldoyanidi, Sophia [3 ]
Mueller, Barbara M. [3 ]
Parmer, Robert J. [4 ,5 ]
机构
[1] Scripps Res Inst, Dept Cell & Mol Biol, La Jolla, CA 92037 USA
[2] Yale Univ, Dept Cell Mol & Dev Biol, New Haven, CT USA
[3] Torrey Pines Inst Mol Studies, San Diego, CA USA
[4] Univ Calif San Diego, Dept Med, La Jolla, CA 92093 USA
[5] Vet Adm San Diego Healthcare Syst, Dept Med, San Diego, CA USA
来源
INTERNATIONAL REVIEW OF CELL AND MOLECULAR BIOLOGY, VOL 309 | 2014年 / 309卷
关键词
TISSUE-PLASMINOGEN-ACTIVATOR; UROKINASE-CATALYZED ACTIVATION; HEYMANN NEPHRITIS AUTOANTIGEN; INDUCED BINDING-SITES; OMEGA-AMINO ACIDS; LYS-PLASMINOGEN; GLU-PLASMINOGEN; ALPHA-ENOLASE; SINGLE-CHAIN; HISTONE H2B;
D O I
10.1016/B978-0-12-800255-1.00005-3
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Plasminogen (PLG) is the zymogen of plasmin, the major enzyme that degrades fibrin clots. In addition to its binding and activation on fibrin clots, PLG also specifically interacts with cell surfaces where it is more efficiently activated by PLG activators, compared with the reaction in solution. This results in association of the broad-spectrum proteolytic activity of plasmin with cell surfaces that functions to promote cell migration. Here, we review emerging data establishing a role for PLG, plasminogen receptors and the newly discovered plasminogen receptor, Plg-R-KT, in macrophage recruitment in the inflammatory response, and we address mechanisms by which the interplay between PLG and its receptors regulates inflammation.
引用
收藏
页码:259 / 302
页数:44
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