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Collagen‐binding motif peptide, a cleavage product of osteopontin, stimulates human neutrophil chemotaxis via pertussis toxin‐sensitive G protein‐mediated signaling
Author(s) -
Kim Mi-Kyoung,
Kim Sang Doo,
Lee Ha Young,
Lee Sun Young,
Shim Jae Woong,
Yun Jeanho,
Kim Jong-Min,
Min Do Sik,
Yoo Young Hyun,
Bae Yoe-Sik
Publication year - 2008
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2008.09.023
Subject(s) - pertussis toxin , chemotaxis , peptide , formyl peptide receptor , osteopontin , microbiology and biotechnology , protein kinase a , chemistry , signal transduction , receptor , kinase , biology , biochemistry , g protein , immunology
The collagen‐binding motif (CBM) peptide, a cleavage product of osteopontin (OPN), stimulated intracellular calcium increase in human neutrophils. CBM peptide‐stimulated calcium was inhibited by pertussis toxin (PTX), suggesting the influence of PTX‐sensitive G‐proteins. In addition CBM peptide stimulated the chemotactic migration of human neutrophils and human monocytes. CBM peptide‐induced neutrophil chemotaxis was completely inhibited by PTX, once again indicating the influence of G i proteins. CBM peptide was also found to induce mitogen activated protein kinase activation. CBM peptide‐induced neutrophil chemotaxis was mediated by p38 kinase as well as an extracellular signal‐regulated protein kinase. Taken together, the results suggest that a cleavage product of OPN, CBM peptide, initiates immune responses by inducing neutrophil trafficking via certain PTX‐sensitive cell surface receptors.