International Immunology, Vol. 12, No. 7, 1051-1061,
July 2000
© 2000 Japanese Society for Immunology
Novel molecular mechanisms of dendritic cell-induced T cell activation
Department of Immunology, Windeyer Institute of Medical Sciences, UCL Medical School, 46 Cleveland Street, London W1P 6DB, UK
1 Department of Internal Medicine, University of Michigan, Ann Arbor, MI 48109, USA
2 Service d'Immunologie, Hospital Clinic, Barcelona 08036, Spain
3 Department of Immunology, University of Birmingham, Birmingham B15 2TT, UK
4 Institute of Clinical Pathology and Medical Research, Westmead Hospital, Westmead, NSW 2145 Australia
5 Institute of Molecular Genetics, Academy of Sciences of the Czech Republic, Prague, Czech Republic
6 Department of Transfusion Medicine, Kurume University, Kurume, Fukouka 830, Japan
7 University of Minnesota, Minnesota Medical School, University Hospital, Minneapolis, MN 55455, USA
8 National Centre of Infectious and Parasitic Diseases, 1504 Sofia, Bulgaria
9 Department of Internal Medicine, Division of Haematology/Oncology, University of Michigan Medical Centre, Ann Arbor, MI 48109-0374, USA
10 Immunotech, 13276 Marseille Cedex 9, France
Correspondence to: D. R. Katz
In this study we have re-examined the molecular mechanisms involved in activation of T cells by dendritic cells (DC). Human peripheral blood DC (PBDC) were derived by 2 h adhesion followed by 7 day culture in a combination of granulocyte macrophage colony stimulating factor and IL-4, and depletion of residual T and B cells. These PBDC were used to induce autologous T cell proliferation in a CD3-dependent response, and antibodies against CD11a/18 and CD86 were used as control inhibitors of accessory function. Antibodies against five of the cell surface molecules that we have recently identified on the surface of DC, CD13, CD87, CD98, CD147 and CD148, and an antibody which recognizes a molecule that has not as yet been identified, all inhibited the CD3-induced T cell proliferation. These findings were observed not only when antibodies were present throughout the culture, but also when they were prepulsed on to the surface of the DC, suggesting the inhibition was mediated via the antigen-presenting cells rather than the T cell. The same set of antibodies also inhibited an allospecific mixed lymphocyte reaction, confirming that the inhibitory effect was not dependent on the use of a CD3 antibody as the stimulating agent. All the antibodies of known specificity inhibited both CD4 and CD8 T cells equally. Unlike CD87, CD98 and CD147 antibodies, which inhibited activation of both CD45RA (naive) T cells and CD45RO (memory) T cells, CD13 and CD148 appeared to be involved in activation of naive cells only. The molecules identified in this study have not previously been demonstrated to play a role as accessory molecules on DC, the cells that are pivotal for immune induction. Therefore they may provide new potential targets for modulation of the immune response at the APC level.
Keywords: CD13, CD87, CD98, CD147, CD148, dendritic cell, T cell activation
Transmitting editor: M. Feldmann
CiteULike 
Connotea 
Del.icio.us What's this?
This article has been cited by other articles:
|
|
 |
|
  F. Gueler, S. Rong, M. Mengel, J.-K. Park, J. Kiyan, T. Kirsch, I. Dumler, H. Haller, and N. Shushakova Renal Urokinase-Type Plasminogen Activator (uPA) Receptor but not uPA Deficiency Strongly Attenuates Ischemia Reperfusion Injury and Acute Kidney Allograft Rejection J. Immunol., July 15, 2008; 181(2): 1179 - 1189. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 M. Alfalah, M. P. Krahn, G. Wetzel, S. von Horsten, C. Wolke, N. Hooper, T. Kalinski, S. Krueger, H. Y. Naim, and U. Lendeckel A Mutation in Aminopeptidase N (CD13) Isolated from a Patient Suffering from Leukemia Leads to an Arrest in the Endoplasmic Reticulum J. Biol. Chem., April 28, 2006; 281(17): 11894 - 11900. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 P. Mina-Osorio, L. H. Shapiro, and E. Ortega CD13 in cell adhesion: aminopeptidase N (CD13) mediates homotypic aggregation of monocytic cells J. Leukoc. Biol., April 1, 2006; 79(4): 719 - 730. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 D. Xu and M. E. Hemler Metabolic Activation-related CD147-CD98 Complex Mol. Cell. Proteomics, August 1, 2005; 4(8): 1061 - 1071. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
P. Mina-Osorio and E. Ortega Aminopeptidase N (CD13) functionally interacts with Fc{gamma}Rs in human monocytes J. Leukoc. Biol., June 1, 2005; 77(6): 1008 - 1017. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
G. Staffler, A. Szekeres, G. J. Schutz, M. D. Saemann, E. Prager, M. Zeyda, K. Drbal, G. J. Zlabinger, T. M. Stulnig, and H. Stockinger Selective Inhibition of T Cell Activation Via CD147 Through Novel Modulation of Lipid Rafts J. Immunol., August 15, 2003; 171(4): 1707 - 1714. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 J. Y. Cho, D. A. Fox, V. Horejsi, K. Sagawa, K. M. Skubitz, D. R. Katz, and B. Chain The functional interactions between CD98, {beta}1-integrins, and CD147 in the induction of U937 homotypic aggregation Blood, July 15, 2001; 98(2): 374 - 382. [Abstract] [Full Text] [PDF]
|
|