Cytometry · 1998 · 23 citations · 27 references
Life SciencesImmunologyOncologyCancer ImmunologyImmunopathologyTumor ImmunologyT Cell BiologyTumor AntigensBiomolecular Binding AffinityDipeptidyl PeptidasesEnzymatic Activity MarkersFlow Cytometry ImmunophenotypingNeoplastic DiseaseNeoplastic ProgressionPeptidase Activity
The transmembrane serine aminopeptidase dipeptidyl peptidase IV (DPP IV) (also known as CD26) participates in several immunological functions and has a binding affinity for several molecules, including collagen, which may be an integral mechanism for T cells to traverse endothelial barriers. Since CD26 is phenotypically expressed in certain T-cell malignancies, this study utilized a novel four-color cytofluorographic procedure to measure DPP IV enzymatic activity concurrently with the expression of other surface markers in an aggressive hepatosplenic T-cell lymphoma. Immunophenotypic analysis by flow cytometry revealed the tumor to be CD2+, CD3+, CD5-, CD7+, TcR-gamma/delta+, CD4-, CD8+/-, CD56+, and CD11c+. The CD26 molecule was also expressed, and DPP IV activity was present, with the maximal activity detectable after 10 min of incubation. These results represent the initial description of enzymatically active CD26 in a T-cell malignancy, and raise the possibility that this molecule may be a participant in the pathogenetic mechanisms utilized by the neoplastic cells.
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Direct Association of Adenosine Deaminase with a T Cell Activation Antigen, CD26
Junichi Kameoka, Toshiaki Tanaka, Yoshihisa Nojima et al. · Science · 1993 · 508 citations
Emile Jf, M-L Boulland, Corinne Haïoun et al. · Blood · 1996 · 203 citations · Full text
Life Sciences, Hematology, Oncology +12