Sialic acid-binding Ig-like lectin 9(Siglec 9) is expressed by peripheral blood leukocytes (neutrophils and monocytes but not eosinophils); and found in liver; fetal liver; bone marrow; placenta; spleen and in lower levels in skeletal muscle; fetal brain and so on. It is a putative adhesion molecule that mediates sialic-acid dependent binding to cells. It also binds to alpha-2;3- or alpha-2;6-linked sialic acid. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface.
Signal Regulatory Protein α (SIRPα) is a monomeric approximately 90 kD type I transmembrane glycoprotein. The 504 amino acid human SIRPα contains two Ig-like C1-type domains and one Ig-like V-type domain. SIRPα can express in various tissues, mainly on brain and myeloid cells, including macrophages, neutrophils, dendritic and Langerhans cells. It also can detect in neurons, smooth muscle and endothelial cells. SIRPA is an immunoglobulin-like cell surface receptor for CD47. SIRPα acts as docking protein and induces translocation of PTPN6, PTPN11 and other binding partners from the cytosol to the plasma membrane. SIRPα shows adhesion of cerebellar neurons, neurite outgrowth and glial cell attachment. SIRPα engagement generally produces a negative regulatory signal; it may mediate negative regulation of phagocytosis, mast cell activation and dendritic cell activation
Signal Regulatory Protein α (SIRPα) is a monomeric approximately 90 kD type I transmembrane glycoprotein. The 504 amino acid human SIRPα contains two Ig-like C1-type domains and one Ig-like V-type domain. SIRPα can express in various tissues, mainly on brain and myeloid cells, including macrophages, neutrophils, dendritic and Langerhans cells. It also can detect in neurons, smooth muscle and endothelial cells. SIRPA is an immunoglobulin-like cell surface receptor for CD47. SIRPα acts as docking protein and induces translocation of PTPN6, PTPN11 and other binding partners from the cytosol to the plasma membrane. SIRPα shows adhesion of cerebellar neurons, neurite outgrowth and glial cell attachment. SIRPα engagement generally produces a negative regulatory signal; it may mediate negative regulation of phagocytosis, mast cell activation and dendritic cell activation.
Signal Transducer CD24 is a heavily and variably glycosylated GPI-linked sialoprotein. Human CD24 is expressed on B lineage cells and granulocytes, on epithelial, neuronal, and muscle cells, and on a range of tumor cells. CD24 expression is regulated during lineage development and with the activation of various cell types. Antibody crosslinking of CD24 enhances the induction of apoptosis in B and T lymphocytes which contributes to negative selection and the induction of immune tolerance. CD24 on antigen presenting cells cooperates with B7 molecules in the costimulation of T cells. CD24 associates in cis with Siglec10 and with the danger-associated molecules HMGB1, HSP70, or HSP90 which are released from necrotic or damaged cells. Formation of these ternary complexes fills a protective role: the resulting Siglec10 signaling inhibits inflammatory responses that are otherwise induced by extracellular DAMPs.
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