Cloning and functional expression of the T cell activation antigen CD26

T. Tanaka, D. Camerini, B. Seed, Y. Torimoto, N. H. Dang, J. Kameoka, H. N. Dahlberg, S. F. Schlossman, C. Morimoto

Research output: Contribution to journalArticlepeer-review

210 Citations (Scopus)


A cDNA encoding the T cell activation Ag CD26 was isolated from human PHA- activated T cells by using an expression cloning method. The nucleotide sequence obtained predicts a protein of 766 amino acids of type II membrane topology, with six amino acids in the cytoplasmic region. The predicted amino acid sequence of the Ag was 85% homologous to that of the dipeptidyl peptidase IV enzyme isolated from rat liver. Derivatives of the human leukemic T cell line Jurkat transfected with a CD26 expression plasmid were established. Characterization of the CD26 Ag expressed by the transfected Jurkat cells revealed that the Ag could be immunoprecipitated as a 110-kDa molecule similar to that found on peripheral blood T cells and that the Ag had dipeptidyl peptidase IV activity. Functional analysis of these Jurkat transfectants showed that cross-linking of the CD26 and CD3 Ag with their respective antibodies resulted in enhanced intracellular calcium mobilization and IL-2 production. These results provide direct evidence that the CD26 Ag plays a role in T cell activation.

Original languageEnglish
Pages (from-to)481-486
Number of pages6
JournalJournal of Immunology
Issue number2
Publication statusPublished - 1992

ASJC Scopus subject areas

  • Immunology and Allergy
  • Immunology


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