CD95 is a 45 kD single chain type I glycoprotein also known as Fas, APO-1, and TNFRSF6. It is a member of the TNF receptor superfamily. CD95 is expressed on T and B lymphocytes, monocytes, neutrophils, and fibroblasts. CD95 expression is upregulated by activation. The extracellular region of CD95 binds to CD178 (Fas ligand). CD178 binding to CD95 induces apoptosis and has been shown to play a role in the maintenance of peripheral tolerance.
CD99 is a type I single chain transmembrane protein devoid of N-linked glycosylation sites encoded by the pseudoautosomal gene MIC2. CD99 has an apparent molecular weight of 32 kD and is widely expressed on a variety of tissues. CD99 is highly expressed on thymocytes, T cells, and T cell leukemias and lymphomas. However, it is absent on some B cell lines, fetal B cells, eosinophils, granulocytes and the NK-cell line YT. CD99 is involved in spontaneous rosette formation with erythrocytes and may also be involved in other T-cell and hematopoietic cell adhesion pathways. CD99 has been reported to activate a caspase-independent death pathway in T cells under some conditions. CD99 interacts with a number of proteins including ferritin heavy chain 1, karyopherin beta 1, TRIP13, cyclophilin A, annexin II, and ubiquitin-conjugating enzyme E2H.
CD9 is a 24 kD type III transmembrane protein also known as tetraspanin, MRP-1 and DRAP-24. It is a member of the tetraspan family (spanning the membrane four times) found on platelets, B cell progenitors, activated lymphocytes, granulocytes, endothelial cells and epithelial cells. CD9 induces adhesion, platelet aggregation, and B cell development. CD9 has been shown to associate with CD63, CD81, CD82, and CD36 and to bind to β1 integrins.
MHC class I antigens associated with β2-microglobulin are expressed by all human nucleated cells. MHC class I molecules are involved in presentation of antigens to CD8+ T cells. They play an important role in cell-mediated immune responses and tumor surveillance.
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