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Published online before print June 12, 2006

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(Journal of Leukocyte Biology. 2006;80:350-358.)
© 2006 by Society for Leukocyte Biology

Release of surface-expressed lactoferrin from polymorphonuclear neutrophils after contact with CD4⁺T cells and its modulation on Th1/Th2 cytokine production

Ko-Jen Li^*, Ming-Chi Lu^*, Song-Chou Hsieh, Cheng-Han Wu, Hsin-Su Yu, Chang-Youh Tsai and Chia-Li Yu^,1

^* Department of Internal Medicine, Buddhist Tzu-Chi General Hospital Taipei Branch, Taiwan; Departments of
Internal Medicine and
Dermatology, National Taiwan University College of Medicine, Taipei; and
Section of Allergy, Immunology & Rheumatology, Veterans General Hospital-Taipei, Taiwan

¹Correspondence: Department of Internal Medicine, National Taiwan University Hospital, No. 7 Chung-Shan South Road, Taipei, Taiwan 100. E-mail: clyu{at}ha.mc.ntu.edu.tw

It is conceivable that a membrane component(s) is transferred from antigen-presenting cells to T cells after antigenic stimulation. However, it is not clear whether a certain membrane component(s) is transferred from polymorphonuclear neturophils (PMN) to T cells for immunomodulation. In the presence study, we cocultured two of the three autologous cells—PMN, CD4⁺T, and red blood cells (RBC)—homotypically or heterotypically for 1 h. Spontaneous membrane exchange between autologous PMN-PMN and PMN-CD4⁺T but not between CD4⁺T-CD4⁺T or RBC-CD4⁺T was observed with a confocal microscope. Loss of membrane exchange between two paraformaldehyde-fixed cells suggests that mutual membrane exchange is via cell–cell contact. Different combinations of cellular enzyme-linked immunosorbent assay for measuring the binding between fixed cells and biotinylated cell lysates showed the same tendency. To identify the molecule(s) mediating PMN-CD4⁺T binding, we compared the banding of biotinylated PMN lysates and the banding of plain PMN lysate probed by biotinylated CD4⁺T lysate in 10% sodium dodecyl sulfate-polyacrylamide gel electrophoresis. We found that a 75- to 80-kDa surface-expressed molecule on PMN exists constantly to mediate PMN-CD4⁺T binding. Peptide analysis disclosed that the molecule had 99.8% identity with lactoferrin (LF). The expression of LF on system lupus erythematosis (SLE)-PMN is less than normal PMN. PMN-CD4⁺T coculture increased LF expression on CD4⁺T. Normal PMN and human milk-derived LF suppressed interferon- (IFN-) but enhanced interleukin (IL)-10 production of anti-CD3+anti-CD28-activated, normal CD4⁺T. In contrast, coculture of SLE-PMN and autologous CD4⁺T suppressed IFN- and IL-10 production. These results suggest that the surface-expressed LF released from PMN after contact with autologous CD4⁺T modulated its T helper cell type 1 (Th1)/Th2 cytokine production. Decreased LF expression on SLE-PMN abnormally modulates Th1/Th2 production by CD4⁺T cells.

Key Words: systemic lupus erythematosus • interferon- • interleukin-10

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				G. de la Rosa, D. Yang, P. Tewary, A. Varadhachary, and J. J. Oppenheim Lactoferrin Acts as an Alarmin to Promote the Recruitment and Activation of APCs and Antigen-Specific Immune Responses J. Immunol., May 15, 2008; 180(10): 6868 - 6876. [Abstract] [Full Text] [PDF]