Open AccessMedicineBiologyChemistry

T. Imaizumi, T. Matsumiya, K. Fujimoto, K. Okamoto, X. Cui, U. Ohtaki, H. Yoshida, K. Satoh

2000.10.1TOHOKU JOURNAL OF EXPERIMENTAL MEDICINE

DOI: 10.1620/tjem.192.127

tlooto Summary

The enhanced expression of fractalkine is found in human umbilical vein endothelial cells stimulated with interferon-γ (IFN-γ) and this may play an important role in immune responses by eliciting a traffic of mononuclear cells through the vascular wall.

Abstract

CX3CL1/Fractalkine, a CX3C chemokine, is a potent agonist for the chemotaxis and adhesion of monocytes and lymphocytes. It was first identified as a membrane protein in endothelial cells activated with IL-1 or TNF-α. We have found the enhanced expression of fractalkine in human umbilical vein endothelial cells stimulated with interferon-γ (IFN-γ). Pretreatment of the cells with cycloheximide did not inhibit the expression of fractalkine mRNA. The majority of fractalkine protein was found in the cell lysate, and an antibody-blocking experiment disclosed that fractalkine contributes to the adhesion of mononuclear cells to endothelial monolayers stimulated with IFN-γ. Vascular endothelial cells produce fractalkine in response to IFN-γ, and this may play an important role in immune responses by eliciting a traffic of mononuclear cells through the vascular wall.

Citation format

IMAIZUMI, T., et al. Interferon-γ stimulates the expression of cx3cl1/fractalkine in cultured human endothelial cells. TOHOKU JOURNAL OF EXPERIMENTAL MEDICINE, 2000, 192: 127–139.