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Elastin‐derived peptide induces monocyte chemotaxis by increasing intracellular cyclic GMP level and activating cyclic GMP dependent protein kinase
Author(s) -
Uemura Yuko,
Okamoto Kouji
Publication year - 1997
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549700201061
Subject(s) - chemotaxis , intracellular , peptide , elastin , protein kinase a , cyclic adenosine monophosphate , monocyte , chemistry , cyclic guanosine monophosphate , kinase , guanosine , biochemistry , protein kinase c , microbiology and biotechnology , biology , receptor , nitric oxide , immunology , genetics , organic chemistry
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 μg/ml. Homologous deactivation test showed that monocytes exposed to the elastin‐derived peptide at 10‐1 μg/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.
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