The immunoglobulin-like transcript (ILT) family (also named leukocyte Ig-like receptors (LIR) and monocyte/macrophage Ig-like receptors (MIR)) can be activating and inhibitory immunoreceptors. ILTs are expressed on many leukocyte subsets and regulators of immune responses . ILTs share significant homology with killer cell Ig-like receptors (KIR). Except ILT-6, all ILT family members are type I transmembrane proteins having two or four extracellular Ig-like domains . ILT2 is expressed on most monocytes,dendritic cells,and mature B cells. ILT2 is also expressed on small percentages of T-cells and NK cells. ILT2 can prevents cellular activation.
Members of the immunoglobulin-like transcript (ILT) family are activating and inhibitory immunoreceptors whose genes are located same locus that encodes killer cell Ig-like receptors (KIR). Leukocyte Immunoglobulin-Like Receptor Subfamily B Member 2 (LIR-2) is a type I transmembrane protein. LIR-2 is expressed primarily on monocytes and dendritic cells (DC). Human LIR-2 is produced as a 598 amino acino acid precursor including a 21 aa signal sequence, a 440 aa extracellular domain (ECD), a 21 aa transmenbrane segment, and a 116 aa cytoplasmic domain. LIR-2 binds to Classical MHCI proteins. Ligation of LIR-2 incluces Tyr phosphorylation within its cytoplasmic ITIMs, a requirement for association with SHP-1. LIR-2 mediates tolerogenic DC-induced CD4+ T cell energy in vitro and in vivo.
Lymphocyte function-associated antigen 3 (LFA-3/CD58) is a single-pass type I membrane protein. CD58 is widely expressed on hematopoietic and non-hematopoietic human tissue and has been found on leukocytes; erythrocytes; endothelial cells; epithelial cells and fibroblasts of human origin. It is a Ligand of the T-lymphocyte CD2 glycoprotein. This interaction is important in mediating thymocyte interactions with thymic epithelial cells; antigen-independent and -dependent interactions of T-lymphocytes with target cells and antigen-presenting cells and the T-lymphocyte rosetting with erythrocytes. In addition; the LFA-3/CD2 interaction may prime response by both the CD2+ and LFA-3+ cells.
CD53 is a member of the transmembrane 4 superfamily, also called the tetraspanin family. Most of these members are cell-surface proteins that are characterized by the presence of four hydrophobic domains. These proteins mediate signal transduction events that play a role in the regulation of cell development, activation, growth and motility. CD53 is a cell surface glycoprotein that is known to complex with integrins. Familial deficiency of CD53 gene has been linked to an immunodeficiency associated with recurrent infectious diseases caused by bacteria, fungi and viruses. CD53 contributes to the transduction of CD2-generated signals in T cells and natural killer cells and has been suggested to play a role in growth regulation.
Human Fatty Acid-Binding Protein 1 (FABP1) is a cytoplasm protein, which belongs to the calycin superfamily and Fatty-acid binding protein (FABP) family. Fatty acid binding proteins are a family of small, highly conserved, cytoplasmic proteins that bind long-chain fatty acids. FABP1 forms a beta-barrel structure that accommodates hydrophobic ligands in its interior. FABP1 can bind free fatty acids and their coenzyme A derivatives, bilirubin, and some other small molecules in the cytoplasm, so it can be involved in intracellular lipid transport.
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