Elastin-derived peptide induces monocyte chemotaxis by increasing intracellular cyclic GMP level and activating cyclic GMP dependent protein kinase.

An elastin-derived peptide with an average molecular mass of 25 kDa was shown to induce monocyte chemotaxis at the optimal concentration of 10(-1) micrograms/ml. Homologous deactivation test showed that monocytes exposed to the elastin-derived peptide at 10(-1) micrograms/ml lost their chemotactic responsiveness when reexposed to the same stimulus. In conjunction with chemotactic response to the elastin-derived peptide, intracellular guanosine 3', 5'-monophosphate (cGMP) levels were enhanced but intracellular adenosine 3', 5'-monophosphate (cAMP) levels were not. The monocyte migration induced by the elastin-derived peptide was inhibited by cGMP dependent protein kinase (PKG) inhibitor, but not by cAMP dependent protein kinase inhibitor and protein kinase C inhibitor. These results suggest that the elastin-derived peptide induces monocyte chemotaxis by increasing the level of cGMP, followed by activating PKG.