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Thromb Haemost 2001; 86(06): 1555-1562
DOI: 10.1055/s-0037-1616762
Review Article
Schattauer GmbH

Extracellular Signal-regulated Kinase (ERK) Activation Is Required for GP Ibα-dependent Endothelial Cell Migration[*]

Jie Lian
1   Cardeza Foundation for Hematologic Research, Jefferson Medical College of Thomas Jefferson University, Philadelphia, PA
,
Cezary Marcinkiewicz
2   Sol Sherry Thrombosis Research Center, Department of Physiology, Temple University, School of Medicine, Philadelphia, PA, USA
,
Stefan Niewiarowski
2   Sol Sherry Thrombosis Research Center, Department of Physiology, Temple University, School of Medicine, Philadelphia, PA, USA
,
Dorothy A. Beacham
1   Cardeza Foundation for Hematologic Research, Jefferson Medical College of Thomas Jefferson University, Philadelphia, PA
2   Sol Sherry Thrombosis Research Center, Department of Physiology, Temple University, School of Medicine, Philadelphia, PA, USA
› Author AffiliationsThis work was supported in part by the National Institutes of Health R29HL-51415 (DAB), the National American Heart Association 96011230 (DAB), PA/DE Affiliate of the American Heart Association 440515-431 (SN) and an Initial Investigator Award (CM).
Further Information

Publication History

Received 12 February 2001

Accepted after resubmission 07 August 2001

Publication Date:
12 December 2017 (online)

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Summary

The GP Ib 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 Ibα, and echistatin inhibited αvβ3 binding. Albo A, B and echistatin inhibited EC migration on vWF and vWF/collagen. Albo B or the anti-GP Ibα monoclonal antibody (mAb) 1b1 did not affect the migration of smooth muscle cells or fibroblasts, which lack GP Ib. 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 1b1 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 αvβ3, EC GP Ibα initiates ERK activation, and regulates ERK-induced EC migration on vWF.

Keywords

Endothelial cell - migration - extracellular signal-regulated kinase - snake venom

* Dedicated to Stefan Niewiarowski, MD, PhD, 1926-2001.


 

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