Extracellular signal-regulated kinase (ERK) activation is required for GP lbα-dependent endothelial cell migration

被引：4

作者：

Lian, J

Marcinkiewicz, C

Niewiarowski, S

Beacham, DA

机构：

[1] Temple Univ, Sch Med, Sol Sherry Thrombosis Res Ctr, Dept Physiol, Philadelphia, PA 19140 USA

[2] Thomas Jefferson Univ, Jefferson Med Coll, Cardeza Fdn Hematol Res, Philadelphia, PA USA

来源：

THROMBOSIS AND HAEMOSTASIS | 2001年 / 86卷 / 06期

关键词：

endothelial cell; migration; extracellular signal-regulated kinase; snake venom;

D O I：

10.1055/s-0037-1616762

中图分类号：

R5 [内科学];

学科分类号：

1002 ; 100201 ;

摘要：

The GP lb complex can participate in endothelial cell (EC) migration on von Willebrand factor (vWF) or the mixed matrix of vWF and type I collagen (vWF/collagen). In this study, viper venom proteins alboaggregin (albo) A or B blocked GP Ib alpha, and echistatin inhibited alphav beta3 binding. Albo A. B and echistatin inhibited EC migration on vWF and vWF/collagen. Albo B or the anti-GP Ib alpha monoclonal antibody (mAb) Ib1 did not affect the migration of smooth muscle cells or fibroblasts, which lack GP lb. EC also migrate on albo A- or albo B-coated dishes. PD98059. which blocks ERK activation, abolished EC migration on vWF, vWF/collagen, collagen or albo B. Soluble albo A or Ib1 dramatically inhibited ERK activation during EC migration on vWF or albo B. Echistatin inhibited ERK activation on vWF and vitronectin (VN), but not albo B. Thus. in addition to alphav beta3, EC GP Ib alpha initiates ERK activation, and regulates ERK-induced EC migration on vWF.

引用

页码：1555 / 1562

页数：8

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