CD59 is a widely expressed membrane regulatory protein, and its C-terminus is fixed on the cell surface via a GPI anchor. CD59 has different names due to its functions, such as homologous restriction factor-20, protectin and membrane inhibitor of reactive lysis (MIRL). The main physiological function of CD59 is to prevent the complement membrane attack complex (MAC) from lysing and destroying cells of the same species or its own, that is, homologous species restriction (HSR).
CD5, also known as Leu-1, is a type I transmembrane protein belonging to the scavenger receptor cysteine-rich (SRCR) superfamily. It is expressed on thymocytes, T cells and the B1a subpopulation of B cells. CD5 binds the C-type lectin, CD72, and modulates signaling through the antigen receptors on T and B cells. CD5 has been shown to provide either positive or negative co-stimulatory signals depending on cell type to regulate immune responses.
CD5 is a 67 kD protein, also known as Lyt-1, Ly-1, T1, Tp67, or Ly-12. It is a member of the scavenger receptor cysteine-rich protein superfamily (SRCR) and primarily expressed on thymocytes, T cells, and B-1 cells. Although mature α/β T cells express high levels of CD5, very few γ/δ T cells express this antigen. The interaction of CD5 with CD72, gp35-37, TCR, or BCR is involved in T and B cell activation.
This gene encodes a cell surface adhesion molecule that belongs to a family of adhesion/homing receptors. The encoded protein contains a C-type lectin-like domain, a calcium-binding epidermal growth factor-like domain, and two short complement-like repeats. The gene product is required for binding and subsequent rolling of leucocytes on endothelial cells, facilitating their migration into secondary lymphoid organs and inflammation sites. Single-nucleotide polymorphisms in this gene have been associated with various diseases including immunoglobulin A nephropathy. Alternatively spliced transcript variants have been found for this gene.
Calcium-dependent lectin that mediates cell adhesion by binding to glycoproteins on neighboring cells.Mediates the adherence of lymphocytes to endothelial cells of high endothelial venules in peripheral lymph nodes. Promotes initial tethering and rolling of leukocytes in endothelia.
Ca2+-dependent receptor for myeloid cells that binds to carbohydrates on neutrophils and monocytes. Mediates the interaction of activated endothelial cells or platelets with leukocytes. The ligand recognized is sialyl-Lewis X. Mediates rapid rolling of leukocyte rolling over vascular surfaces during the initial steps in inflammation through interaction with SELPLG.
The protein encoded by this gene is a member of the transmembrane 4 superfamily, also known as the tetraspanin family. Most of these members are cell-surface proteins that are characterized by the presence of four hydrophobic domains. The proteins mediate signal transduction events that play a role in the regulation of cell development, activation, growth and motility. The encoded protein is a cell surface glycoprotein that is known to complex with integrins. It may function as a blood platelet activation marker. Deficiency of this protein is associated with Hermansky-Pudlak syndrome. Also this gene has been associated with tumor progression. Alternative splicing results in multiple transcript variants encoding different protein isoforms.
CD64 is a 72 kD single chain type I glycoprotein also known as FcγRI and FcRI. CD64 is a member of the immunoglobulin superfamily and is expressed on monocytes/macrophages, dendritic cells, and mast cells. The expression can be upregulated by IFN-γ stimulation. CD64 binds IgG immune complex. It plays a role in antigen capture, phagocytosis of IgG/antigen complexes, and antibody-dependent cellular cytotoxicity (ADCC).
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