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Induction of Intracellular Signals Through Binding of Adhesive Molecules

Activation of p125FAK Tyrosine Phosphorylation
  • Mascia Venturino
  • Cristina Olivo
  • Guido Tarone
  • Paola Defilippi
Part of the Methods in Molecular Biology book series (MIMB, volume 96)

Abstract

p125FAK tyrosine phosphorylation is a primary response to integrin stimulation. The first evidence that integrin occupancy by ligands induces tyrosine phosphorylation came from studies on the fibrinogen receptor αllbβ3 in platelets (1). Further work showed that both in normal and transformed cells several different integrin receptors can trigger tyrosine phosphorylation of intracellular proteins following interactions with matrix proteins or integrin receptor clustering by specific antibodies (2).

Keywords

Sodium Dodecyl Sulfate Tyrosine Phosphorylation Cluster Solution Laemmli Sample Buffer BioRad Protein Assay 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Humana Press Inc. 1999

Authors and Affiliations

  • Mascia Venturino
    • 1
  • Cristina Olivo
    • 1
  • Guido Tarone
    • 1
  • Paola Defilippi
    • 1
  1. 1.Sezione di Biologia, Dipartimento di Genetica, Biologia e Chimica MedicaUniversità di TorinoTorinoItaly

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