The CD99 signal enhances Fas‐mediated apoptosis in the human leukemic cell line, Jurkat

FEBS Letters

Jung, Kyeong Cheon³  Kim, Nam Hyun²  Park, Seong Hoe¹  Bae, Youngmee²  Park, Weon Seo² 

[1] Department of Pathology, College of Medicine, and Research Division for Human Life Science, Seoul National University, Yongon-dong 28, Chongno-gu, Seoul 110-799, South Korea;Department of Pathology, Kangwon National University College of Medicine, 192-1 Hyoja-dong, Chunchon 200-701, Kangwon-do, South Korea;Department of Pathology, Hallym University College of Medicine, 1 Okchon-dong, Chunchon 200-702, Kangwon-do, South Korea

关键词: Apoptosis;    Caspase;    CD99;    Epitope;    Fas aggregation;    7-AAD;    7-aminoactinomycin D;    AMC;    aminomethylcoumarin;    DiOC6;    3;    3′-dihexyloxacarbocyanine iodide;    FasL;    Fas ligand;    HRP;    horseradish peroxidase;    2-ME;    2-mercaptoethanol;    mAbs;    monoclonal antibodies;    PBS;    phosphate-buffered saline;    Δψ m;    mitochondrial membrane potential;   

DOI  :  10.1016/S0014-5793(03)01224-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The CD99 antigen has been implicated in various cellular processes, including apoptosis in T cells. Previously, we reported two monoclonal antibodies that recognize different epitopes of the CD99 molecule, named DN16 and YG32. In this study, we investigated the role of each CD99 epitope in T cell apoptosis. Unlike the DN16 epitope, CD99 ligation via the YG32 epitope failed to induce T cell death. Surprisingly, however, the YG32 signal enhanced Fas-mediated apoptosis in Jurkat T cells. Augmentation of Fas-mediated apoptosis by YG32 ligation was inhibited by treatment with either of the caspase inhibitors z-VAD-fmk or z-IETD-fmk, and YG32 ligation appeared to induce Fas oligomerization. These results suggest that each CD99 epitope plays a distinct role in T cell biology, especially in T cell apoptosis.

【 授权许可】

Unknown