Inhibition of cell adhesion to glycoproteins of the extracellular matrix by peptides corresponding to serum amyloid A

摘要: Synthetic peptides related to amino acid residues 29–42 of human serum amyloid A (SAA), Tyr-Ile-Gly-Ser-Asp-Lys-Tyr-Phe-His-Ala-Arg-Gly-Asn-Tyr, were found inhibit the adhesion T-lymphocytes and mouse M4 melanoma cells surfaces coated with major cell adhesive glycoproteins extracellular matrix, laminin or fibronectin. Correspondingly inhibitory activity was manifested by entire 14-residue peptide, its YIGSD laminin-related domain, RGN, fibronectin-related domain. Intact recombinant SAA (rSAA) 1–76 fragment, an (AA) protein, also inhibited adhesion. The did not collagen ADP-induced aggregation platelets. Proteolysis lysosomal enzymes originating from neutrophils led generation specific peptide segments some which pertain It is suggested that acute-phase protein might be involved, either directly via fragments, in inhibition inflammatory reactions metastatic processes depend on integrin possibly other extracellular-matrix-specific receptors mediated recognition interactions immobilized components blood-vessel walls.