Surface properties of a fibronectin derived peptide that regulates tyrosine phosphorylation

Abstract

The role of fibronectin (FN) and substrates, created from FN-derived peptides, in cell-surface interaction was examined. A relationship between substrate mediated intracellular protein tyrosine phosphorylation and cell adhesion was also found using human primary blood derived macrophages. Using western blot analysis, it was found that ∼30 kDa proteins from these macrophages were influenced by surface-bound G3PHSRNG resulting in a reduced tyrosine phosphorylation in the presence of protein kinase C9PKC) inhibitor. The substrate association was shown to allow subsequent interactions that are likely related to its unique ability to influence tyrosine phosphorylation in the presence of PKC inhibitor.