CD24 is a 35-45 kD protein also known as Heat Stable Antigen (HSA), Ly-52, or Nectadrin. It is a GPI-linked sialoglycoprotein expressed on lymphocytes, granulocytes, epithelial cells, thymocytes, monocytes, erythrocytes, and dendritic cells. CD24 expression varies during T and B cell differentiation and is a useful marker for delineating various lymphocyte developmental stages. CD24 serves as an adhesion or costimulatory molecule involved in T and B lymphocyte activation and differentiation by homophilic binding or binding to CD62P.
CD25 is a 55 kD glycoprotein, also known as the low affinity IL-2Rα, Ly-43, p55, or Tac. It is expressed on activated T and B cells, thymocyte subset, pre-B cells, and T regulatory cells. In association with CD122 (IL-2Rβ) and CD132(common γ chain), CD25 forms the high affinity signaling IL-2 receptor.
B and T lymphocyte attenuator (BTLA) is an Ig superfamily coinhibitory receptor with structural similarity to programmed cell death 1 (PD-1) and CTLA-4. BTLA is expressed on B cells, T cells, macrophages, dendritic cells, NKT cells, and NK cells. Engagement of BTLA by its ligand Herpes Virus Entry Mediator (HVEM) is critical for negatively regulating immune response. The absence of BTLA with HVEM inhibitory interactions leads to increased experimental autoimmune encephalomyelitis severity, enhanced rejection of partially mismatched allografts, an increased CD8+ memory T cell population, increased severity of colitis, and reduced effectiveness of T regulatory cells. BTLA plays an important role in the induction of peripheral tolerance of both CD4+ and CD8+ T cells in vivo. Tolerant T cells have significant up-regulated expression of BTLA compared with effector and naive T cells. BTLA may cooperate with CTLA-4 and PD-1 to control T cell tolerance and autoimmunity. It has been reported that BTLA may regulate T cell function through binding to B7-H4.
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