Interleukin-9 (IL-9) is a secreted protein that belongs to the IL-7/IL-9 family.Mature mouse IL-9 shares 57% and 74% amino acid sequence identity with human and rat IL-9, respectively. IL-9 supports IL-2 independent and IL-4 independent growth of helper T-cells. IL-9 stimulates cell proliferation and prevents apoptosis. It functions through the IL-9 receptor (IL-9R), which activates different signal transducer and activator (STAT) proteins and thus connects this cytokine to various biological processes. IL-9 has been identified as a candidate gene for asthma. IL-9 is a determining factor in the pathogenesis of bronchial hyperresponsiveness.
ILDR2 is a member of the B7-like family of proteins that regulate T cell activity, is also a known endoplasmic reticulum molecule that regulates lipid homeostasis. The human ILDR2 lumenal domain shares a 99% and 98% homology with the mouse and rat respectively. The human gene encoding ILDR2 is located in a region on Chr1q23–25 that has been associated with type 2 diabetes. ILDR2 plays critical roles in hepatic clearance of lipoproteins and in lipid homeostasis. ILDR2 regulates human dendritic cells (DC2 cells, a subpopulation of polarized DCs that promotes Th2 differentiation). Recent publications reported that ILDR2 displayed negative regulatory functions on human and mouse T cells in various experimental systems. Fusion protein of ILDR2 lumenal domain with an Fc fragment, displays therapeutic effects in collagen-induced arthritis (CIA), a mouse model of rheumatoid arthritis (RA). ILDR2 represents a novel B7-like ligand that exerts negative immune modulation via interaction with a putative counterpart receptor expressed on activated T cells.
Integrin-linked kinase-associated serine/threonine phosphatase 2C, also known as ILKAP, is cytoplasm protein which belongs to thePP2C family. ILKAP contains onePP2C-like domain. ILKAP is widely expressed. Highest levels expressed in striated muscle. Much lower levels evident in various smooth muscle tissues. ILKAP may play a role in regulation of cell cycle progression via dephosphorylation of its substrates whose appropriate phosphorylation states might be crucial for cell proliferation. ILKAP selectively associates with integrin linked kinase (ILK), to modulate cell adhesion and growth factor signaling. ILKAP inhibits the ILK-GSK3B signaling axis and may play an important role in inhibiting oncogenic transformation. Integrin-linked kinase ( ILK ) plays key roles in a variety of cell functions, including cell proliferation, adhesion and migration. Within the cell, ILK localizes to multiple sites, including the cytoplasm, focal adhesion complexes that mediate cell adhesion to extracellular substrates, as well as cell-cell junctions in epidermal keratinocytes. Nuclear ILK can be rapidly exported into the cytoplasm through a CRM1-dependent pathway, and its export is enhanced by the type 2C protein phosphatase ILKAP. Nuclear localization of ILK in epidermal keratinocytes is associated with increased DNA synthesis, which is sensitive to inhibition by ILKAP.
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.
ILT6, also known as LILRA3, belongs to the ILT family. In human, the ILT gene family includes up to 11 members. The extracellular portion of all members includes at least two and usually four immuno-globulin domains. ILT-2 through 5 are all inhibitory members having variable numbers of cytoplasmic ITIM domains. ILT6 lacks a transmembrane domain. The function of ILT6 is currently unknown. however it is highly homologous to other LILR genes, and can bind human leukocyte antigen (HLA) class I. Therefore, if secreted, the ILT6 might impair interactions of membrane-bound LILRs (such as LILRB1, an inhibitory receptor expressed on effector and memory CD8 T cells) with their HLA ligands, thus modulating immune reactions and influencing susceptibility to disease.
Leukocyte immunoglobulin-like receptor subfamily A member 3 is also known as CD85 antigen-like family member E, Immunoglobulin-like transcript 6, ILT-6, Leukocyte immunoglobulin-like receptor 4, LIR-4 and Monocyte inhibitory receptor HM43/HM31. In humans, it is encoded by the LILRA3 gene. It acts as soluble receptor for class I MHC antigens. Binds both classical and non-classical HLA class I molecules but with reduced affinities compared to LILRB1 or LILRB2.It is detected in B-cells, natural killer (NK) cells, peripheral blood monocytes and lung.
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