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