FUNCTION OF THE UROKINASE RECEPTOR (CD87) IN NEUTROPHIL CHEMOTAXIS

被引：88

作者：

GYETKO, MR

SITRIN, RG

FULLER, JA

TODD, RF

PETTY, H

STANDIFORD, TJ

机构：

[1] ANN ARBOR VET AFFAIRS MED CTR, DEPT INTERNAL MED, DIV PULM & CRIT CARE MED, ANN ARBOR, MI USA

[2] ANN ARBOR VET AFFAIRS MED CTR, DEPT INTERNAL MED, DIV HEMATOL ONCOL, ANN ARBOR, MI USA

[3] UNIV MICHIGAN, MED CTR, ANN ARBOR, MI USA

[4] WAYNE STATE UNIV, DEPT BIOL SCI, DETROIT, MI 48202 USA

来源：

JOURNAL OF LEUKOCYTE BIOLOGY | 1995年 / 58卷 / 05期

关键词：

CELL MOVEMENT; COMPLEMENT RECEPTOR 3; SACCHARIDES; INTEGRINS;

D O I：

10.1002/jlb.58.5.533

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

During recruitment, leukocytes respond to chemotaxins and traverse matrix barriers, Urokinase-type plasminogen activator (uPA), bound to its receptor (uPAR; CD87) facilitates plasmin formation, which promotes matrix proteolysis. Polymerphonuclear leukocytes (PMNs) are critical to the inflammatory response and express both uPA and CD87. To determine whether uPA and CD87 are required for PMN chemotaxis, PMNs were pretreated with an anti-CD87 monoclonal antibody (mAb), a neutralizing anti-uPA mAb, or uPA, PMN chemotaxis was profoundly suppressed by the anti-CD87 mAb but was unaffected by anti-uPA mAb or uPA, The role CD81 plays in chemotaxis may be related to its ability to associate with CR3, CD87/CR3 coupling can be disrupted by specific saccharides. The same saccharides that disrupt CD87/CR3 coupling (NADG, D-mannose, and mannoside) inhibit PMN chemotaxis. We conclude that CD87 plays a crucial role in PMN chemotaxis in vitro that is independent of uPA enzyme activity but may be related to the ability of CD87 to interact with CR3.

引用

页码：533 / 538

页数：6