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.
Uemura
Y
Y
Department of Biochemical Engineering and Science, Kyushu Institute of Technology, Fukuoka, Japan.
Okamoto
K
K
D000818:Animals; D002417:Cattle; D002634:Chemotaxis, Leukocyte / Q000187:drug effects / Q000502:physiology*; D006152:Cyclic GMP / Q000378:metabolism* / Q000502:physiology; D017869:Cyclic GMP-Dependent Protein Kinases / Q000378:metabolism*; D004549:Elastin / Q000502:physiology*; D004789:Enzyme Activation; D006868:Hydrolysis; D008970:Molecular Weight; D009000:Monocytes / Q000166:cytology* / Q000187:drug effects; D009240:N-Formylmethionine Leucyl-Phenylalanine / Q000494:pharmacology; D010070:Oxalates; D019815:Oxalic Acid; D010446:Peptide Fragments; D015398:Signal Transduction
D010070:Oxalates; D010446:Peptide Fragments; D009240:N-Formylmethionine Leucyl-Phenylalanine; D004549:Elastin; D019815:Oxalic Acid; D017869:Cyclic GMP-Dependent Protein Kinases; D006152:Cyclic GMP