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Fractalkine, a CX 3 C‐chemokine, functions predominantly as an adhesion molecule in monocytic cell line THP‐1
Author(s) -
Umehara Hisanori,
Goda Seiji,
Imai Toshio,
Nagano Yutaka,
Minami Yasuhiro,
Tanaka Yoshiya,
Okazaki Toshiro,
Bloom Eda T,
Domae Naochika
Publication year - 2001
Publication title -
immunology and cell biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.999
H-Index - 104
eISSN - 1440-1711
pISSN - 0818-9641
DOI - 10.1046/j.1440-1711.2001.01004.x
Subject(s) - thp1 cell line , chemokine , cell adhesion molecule , microbiology and biotechnology , cell culture , line (geometry) , chemistry , biology , immunology , inflammation , mathematics , genetics , geometry
A newly identified CX 3 C‐chemokine, fractalkine, expressed on activated endothelial cells plays an important role in leucocyte adhesion and migration. Co‐immobilized fractalkine with fibronectin or intercellular adhesion molecule‐1 enhanced adhesion of THP‐1 cells, which express the fractalkine receptor (CX 3 CR1), compared with that observed for each alone. That adherence was fractalkine‐dependent and was confirmed in blocking studies. However, soluble fractalkine induced little chemotaxis in THP‐1 cells in comparison to monocyte chemotactic protein‐1 (MCP‐1), which induced a strong chemotactic response. Moreover, the membrane form of fractalkine expressed on ECV304 cells reduced MCP‐1 mediated chemotaxis of THP‐1 cells. These results indicate that fractalkine may function as an adhesion molecule between monocytes and endothelial cells rather than as a chemotactic factor.