ADHESION OF HUMAN NEUTROPHILS TO AND ACTIVATION BY TYPE-I COLLAGEN INVOLVING A BETA-2 INTEGRIN

被引：70

作者：

MONBOISSE, JC ^{[1
]}

GARNOTEL, R ^{[1
]}

RANDOUX, A ^{[1
]}

DUFER, J ^{[1
]}

BOREL, JP ^{[1
]}

机构：

[1] INST JEAN GODINOI,HEMATOL LAB,F-51056 REIMS,FRANCE

来源：

JOURNAL OF LEUKOCYTE BIOLOGY | 1991年 / 50卷 / 04期

关键词：

POLYMORPHONUCLEAR LEUKOCYTES; MONOCLONAL ANTIBODIES; FIBRONECTIN;

D O I：

10.1002/jlb.50.4.373

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

We previously demonstrated that the alpha-1(l) polypeptide chain of collagen can bind and activate polymorphonuclear neutrophils (PMN). In the present experiments, performed in culture grade 96-well plastic plates coated with collagen, fibronectin, or other proteins, adhesion was assessed by staining the adhering cells after 30 min with crystal violet and measuring absorbance at 560 nm, and activation of PMNs was assessed by measuring the amount of O2 formed. Adhesion occurred at 17 and 37-degrees-C but activation at 37-degrees-C only. Monoclonal antibody anti-CD 18 inhibited adhesion, showing that the receptor of collagen l on PMNs is a beta-2 integrin. On the other hand, adhesion of PMNs to fibronectin was inhibited by monoclonal antibodies to CD18 and to CD11b.

引用

页码：373 / 380

页数：8

共 19 条

[1] LEUKOCYTE ADHESION DEFICIENCY - AN INHERITED DEFECT IN THE MAC-1, LFA-1, AND P150,95 GLYCOPROTEINS [J].