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趋化因子,一种CX3C趋化因子,在单核细胞系THP-1中主要作为一种黏附分子发挥作用。

Fractalkine, a CX3C-chemokine, functions predominantly as an adhesion molecule in monocytic cell line THP-1.

作者信息

Umehara H, Goda S, Imai T, Nagano Y, Minami Y, Tanaka Y, Okazaki T, Bloom E T, Domae N

机构信息

Department of Internal Medicine, Osaka Dental University, Osaka, Kan Research Institute, Kyoto, Japan.

出版信息

Immunol Cell Biol. 2001 Jun;79(3):298-302. doi: 10.1046/j.1440-1711.2001.01004.x.

DOI:10.1046/j.1440-1711.2001.01004.x
PMID:11380684
Abstract

A newly identified CX3C-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 (CX3CR1), 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.

摘要

一种新发现的CX3C趋化因子,即fractalkine,在活化的内皮细胞上表达,在白细胞黏附和迁移中起重要作用。与单独使用纤连蛋白或细胞间黏附分子-1相比,将fractalkine与它们共同固定能增强表达fractalkine受体(CX3CR1)的THP-1细胞的黏附。这种黏附依赖于fractalkine,并且在阻断实验中得到证实。然而,与诱导强烈趋化反应的单核细胞趋化蛋白-1(MCP-1)相比,可溶性fractalkine在THP-1细胞中几乎不诱导趋化作用。此外,ECV304细胞上表达的膜形式的fractalkine降低了MCP-1介导的THP-1细胞趋化作用。这些结果表明,fractalkine可能作为单核细胞与内皮细胞之间的黏附分子发挥作用,而不是作为趋化因子。

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