International Immunology, Vol. 11, No. 11, 1731-1738,
November 1999
© 1999 Japanese Society for Immunology
Antigen-induced TCRCD3 down-modulation does not require CD3
or CD3
cytoplasmic domains, necessary in response to anti-CD3 antibody
Centre d'Immunologie INSERM-CNRS de Marseille-Luminy, Case 906, 13288 Marseilles, Cedex 9, France
Correspondence to: C. Boyer
We studied cytotoxic T lymphocyte (CTL) clones expressing cytoplasmic domain-deleted CD3
and CD3
chains. These cells retained efficient antigen-specific cytolysis. Because the cytoplasmic domains of native CD3
and CD3
chains contain a dileucine-based and a tyrosine-based motif thought to be important for receptor endocytosis, we compared TCRCD3 down-modulation on the CTL clones expressing or not these domains. We found that antigen-induced TCRCD3 down-modulation was not dependent on either the CD3
or CD3
cytoplasmic domains. This contrasts with phorbol ester- and anti-CD3 mAb (soluble or plastic-coated)-induced TCRCD3 down-modulation, that are respectively dependent on CD3
and on either CD3
or CD3
cytoplasmic domains, suggesting that differences may exist between the mechanisms of TCRCD3 down-modulation in response to the three stimuli. TCRCD3 down-modulation in response to antigen was demonstrated by confocal microscopy to be associated with TCRß chain internalization, whether CD3
and CD3
were native or truncated. Inhibition by the protein tyrosine kinase inhibitor PP1 of TCRCD3 down-modulation in response to antigen was also similar whether CD3
and CD3
cytoplasmic domains were present or not. These properties of receptor down-modulation are discussed with respect to the requirements for TCR engagement on antigen-presenting cells.
Keywords: cellcell interactions, cytotoxic T lymphocyte, protein kinases, rodent, TCR
Transmitting editor: M. M. Davis
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