Dissociation of the αIIbβ3-Integrin by EGTA Stimulates the Tyrosine Kinase pp72 without Inducing Platelet Activation

This publication has 33 references indexed in Scilit:

• Integrin αIIbβ3-mediated Translocation of CDC42Hs to the Cytoskeleton in Stimulated Human Platelets
  Published by Elsevier ,1995
• Platelet Shape Change Induced by Thrombin Receptor Activation: RAPID STIMULATION OF TYROSINE PHOSPHORYLATION OF NOVEL PROTEIN SUBSTRATES THROUGH AN INTEGRIN- AND Ca 2+-INDEPENDENT MECHANISM
  Published by Elsevier ,1995
• Ligand and cation binding are dual functions of a discrete segment of the integrin β3 subunit: Cation displacement is involved in ligand binding
  Cell, 1994
• Involvement of Protein-Tyrosine Kinase p72syk in Collagen-Induced Signal Transduction in Platelets
  European Journal of Biochemistry, 1994
• Calcium mobilisation controls tyrosine protein phosphorylation independently of the activation of protein kinase C in human platelets
  FEBS Letters, 1994
• Adhesive ligand binding to integrin alpha IIb beta 3 stimulates tyrosine phosphorylation of novel protein substrates before phosphorylation of pp125FAK
  The Journal of cell biology, 1993
• Alpha IIb beta 3 integrin dissociation induced by EDTA results in morphological changes of the platelet surface-connected canalicular system with differential location of the two separate subunits.
  The Journal of cell biology, 1993
• Integrin-dependent phosphorylation and activation of the protein tyrosine kinase pp125FAK in platelets.
  The Journal of cell biology, 1992
• Dissociation of the glycoprotein IIb-IIIa complex in isolated human platelet membranes
  Biochimica et Biophysica Acta (BBA) - Biomembranes, 1982
• Involvement of divalent cations in the complex between the platelet glycoproteins IIb and IIIa
  Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1982