6533b7d1fe1ef96bd125cbf8
RESEARCH PRODUCT
Enzymatic Activity of CD26 (Dipeptidylpeptidase IV) is not Required for Its Signalling Function in T Cells
Martin HegenBernhard FleischerHans-ulrich DemuthKlaus NeubertRosula HugAlfred BarthHans-willi Mittrückersubject
Antigens Differentiation T-LymphocyteDipeptidyl Peptidase 4T-LymphocytesT cellCD3ImmunologyBiologyLymphocyte ActivationCell LineMiceTumor Cells CulturedmedicineAnimalsHumansImmunology and AllergyCytotoxic T cellDipeptidyl-Peptidases and Tripeptidyl-PeptidasesT-cell receptorProteolytic enzymesHematologyTransfectionT lymphocyteCytotoxicity Tests ImmunologicCell biologymedicine.anatomical_structureBiochemistrybiology.proteinInterleukin-2Clone (B-cell biology)Signal Transductiondescription
Abstract CD26 is a proteolytic enzyme (dipeptidylpeptidase IV) expressed on the T cell surface that defines an alternative activation signal for human T lymphocytes. Crosslinking of CD26 via monoclonal antibodies triggers proliferation and cytotoxicity in preactivated T cells. In this study, we used highly specific competitive and irreversible inhibitors of dipeptidylpeptidase IV to study the role of the enzymatic activity in activation of CD26- transfected T cells as well as of CD26-expressing normal human T cell clones. These inhibitors at concentrations that blocked up to 95% of the enzymatic activity, did not specifically inhibit T cell activation neither via TCR/CD3 nor via CD26 itself. This demonstrates that the enzymatic activity of CD26 is not required for its T cell activating properties.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 1993-12-01 | Immunobiology |