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Leukotactin‐1/CCL15‐induced chemotaxis signaling through CCR1 in HOS cells
Author(s) -
Ko Jesang,
Kim In Sik,
Jang Sung-Wuk,
Lee Young Han,
Shin Soon Young,
Min Do Sik,
Na Doe Sun
Publication year - 2002
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/s0014-5793(02)02465-1
Subject(s) - chemotaxis , protein kinase c , microbiology and biotechnology , signal transduction , chemistry , receptor , biology , biochemistry
Leukotactin‐1 (Lkn‐1)/CCL15 is a recently cloned CC‐chemokine that binds to the CCR1 and CCR3. Although Lkn‐1 has been known to function as a chemoattractant for neutrophils, monocytes and lymphocytes, its cellular mechanism remains unclear. To understand the mechanism of Lkn‐1‐induced chemotaxis signaling, we examined the chemotactic activities of human osteogenic sarcoma cells expressing CCR1 in response to Lkn‐1 using inhibitors of signaling molecules. Inhibitors of G i /G o protein, phospholipase C (PLC) and protein kinase Cδ (PKCδ) inhibited the chemotactic activity of Lkn‐1 indicating that Lkn‐1‐induced chemotaxis signal is transduced through G i /G o protein, PLC and PKCδ. The activities of PLC and PKCδ were also enhanced by Lkn‐1 stimulation. Chemotactic activity of Lkn‐1 was inhibited by the treatment of cycloheximide and actinomycin D suggesting that newly synthesized proteins are needed for chemotaxis. Nuclear factor‐κB (NF‐κB) inhibitor reduced chemotactic activity of Lkn‐1. DNA binding activity of NF‐κB was also enhanced by Lkn‐1 stimulation. These results suggest that Lkn‐1 transduces the signal through G i /G o protein, PLC, PKCδ, NF‐κB and newly synthesized proteins for chemotaxis.