LIGHT , also known as TNFSF14 or CD258 , is a newly identified member of the TNF superfamily (TNFSF14) that is expressed by activated T lymphocytes , monocytes , granulocytes , spleen cells , and immature dendritic cells. TNFSF14 / LIGHT / CD258 is a type II transmembrane protein that is known to bind 2 membrane-bound TNFSF signaling receptors: HVEM , which is predominantly expressed by T cells , and lymphotoxin β receptor (LTβR) , which is expressed by stromal cells and nonlymphoid hematopoietic cells. TNFSF14 / LIGHT / CD258 also binds to a soluble non-signaling receptor , decoy receptor 3 (DcR3) , which can modulate the function of LIGHT in vivo. TNFSF14 / LIGHT / CD258 can also costimulate T cell responses via HVEM , which is constitutively expressed in most lymphocyte subpopulations , including CD4+ and CD8+ T cells. In addition , TNFSF14 / LIGHT / CD258 has been shown to suppress tumor formation in vivo and to induce tumor cell apoptosis via the up-regulation of intercellular adhesion molecule 1 and an increased lymphocyte adhesion to cancer cells. Thus , TNFSF14 / LIGHT / CD258 is being actively investigated as a possible basis for cancer treatment.
Leukocyte immunoglobulin-like receptor subfamily B member 3, also known as Leukocyte immunoglobulin-like receptor 3, Immunoglobulin-like transcript 5, Monocyte inhibitory receptor HL9, CD85 antigen-like family member A, CD85a and LILRB3, is a single-pass type I membrane protein which belongs to the leukocyte receptor cluster (LRC) present on 19q13.4. LILRB3 / CD85a contains fourIg-like C2-type (immunoglobulin-like) domains. LILRB3 / CD85a contains three copies of a cytoplasmic motif that is referred to as the immunoreceptor tyrosine-based inhibitor motif (ITIM). This motif is involved in modulation of cellular responses. The phosphorylated ITIM motif can bind the SH2 domain of several SH2-containing phosphatases. LILRB3 / CD85a is expressed on immune cells where it binds to MHC class I molecules on antigen-presenting cells and transduces a negative signal that inhibits stimulation of an immune response. It is thought to control inflammatory responses and cytotoxicity to help focus the immune response and limit autoreactivity. Multiple transcript variants encoding different isoforms have been found.
Mouse Leukocyte Immunoglobulin-like Receptor Subfamily B Member 4 (LILRB4/CD85k/ILT3) is an approximately transmembrane glycoprotein that negatively regulates immune cell activation. Mouse LILRB4 consists of a 215 amino acid (aa) extracellular domain with two Ig-like domains, a 22 aa transmembrane segment, and a 75 aa cytoplasmic domain with 3 immunoreceptor tyrosine-based inhibitory motifs (ITIM). Within the ECD, mouse LILRB4 shares 45% and 77% aa sequence identity with human and rat LILRB4, respectively. Alternative splicing of mouse LILRB4 generates a potentially soluble isoform that lacks the transmembrane segment. LILRB4 is expressed on dendritic cells (DC), monocytes, macrophages, and vascular endothelial cells (EC). Ligation of LILRB4 triggers ITIM-mediated inhibition of cellactivating signaling, leading to enhanced immune tolerance and reduced allogeneic graft rejection. Soluble LILRB4 induces the differentiation of CD8+ T suppressor cells (Ts) that can inhibit the effector functions of CD4+ Th cells and CD8+ CTL. In turn, CD8+ Ts cells induce LILRB4 up-regulation and a tolerogenic phenotype in monocytes, DC, and EC.
Lysosome membrane protein II (LIMPII),also known as SCARB2, is a type III multi-pass membrane glycoprotein that is located primarily in limiting membranes of lysosomes and endosomes on all tissues and cell types so far examined. Earlier studies in mice and rat suggested that this protein may participate in membrane transportation and the reorganization of endosomal/lysosomal compartment. The protein deficiency in mice was reported to impair cell membrane transport processes and cause pelvic junction obstruction, deafness, and peripheral neuropathy. Further studies in human showed that this protein is identified as a receptor for EV71 (human enterovirus species A, Enterovirus 71) and CVA16 (coxsackievirus A16) which are most frequently associated with hand, foot and mouth disease (HFMD). Mutations in this gene caused an autosomal recessive progressive myoclonic epilepsy-4 (EPM4), also known as action myoclonus-renal failure syndrome (AMRF). Alternatively spliced transcript variants encoding different isoforms have been found for this gene. In addition, LIMPII also has been shown to bind thrombospondin-1, may contribute to the pro-adhesive changes of activated platelets during coagulation, and inflammation.
Regenerating protein 2 (Reg2) also known as Lithostathine 2, pancreatic thread protein (PTP2) and pancreatic stone protein 2 (PSP2), is a member of the Reg family of proteins. These small, secreted proteins have been implicated in a range of physiological processes including acting as acute phase reactants, lectins, survival/growth factors for insulin-producing pancreatic beta-cells, neural cells, and epithelial cells of the digestive system. Studies also indicate a role for Reg family members in tumor formation and indicate their potential for use as biomarkers of carcinogenesis. Mouse Reg2 is expressed in regenerating islets and normal exocrine pancreas. Reg2 also stimulates the growth of pancreatic beta cells. Mouse Reg2 belongs to the type II subclass of the Reg family and is the only subclass II Reg protein described.
LIX ( Liposaccharide-Induced CXC chemokine, also GARG-8 and Cxcl5) is a secreted 8-9 kDa member of the Intercrine alpha (or CxC) family of chemokines. It is widely expressed, being produced by diverse cell types such as fibroblasts, thymic epithelium, platelets, vascular endothelium, hepatocytes, lung type II alveolar cells and ileal columnar epithelium. As a chemokine, LIX demonstrates chemokinetic properties. It induces the chemotaxis of neutrophils and endothelial cells, and also promotes TNF-alpha secretion from mast cells and macrophages. Notably, circulating LIX is not derived from fibroblasts, but platelets. This suggests that neutrophil homeostasis/chemotaxis is a function of local resident cell activation and LIX secretion, not generally circulating LIX. Mouse LIX is synthesized as a 132 amino acid (aa) precursor that contains a 40 aa signal sequence, a 78 aa mature region (aa 41-118), and a cleavable 14 aa C-terminus. The mature region possesses an ELR/GluLeuArg motif between aa 50-52, and an alpha-family characteristic CxC motif between aa 53-55. Although there are no known splice variants of mouse LIX, considerable proteolytic processing occurs at both the N-and C-termini over aa 41-132. This may reduce the MW in SDS-PAGE by as much as 3 kDa. The majority of LIX appears to start between aa 47-50, and this is positively correlated with an bioactivity. Over aa 41-118, mouse LIX shares 73% aa sequence identity with an rat LIX. Although not a strict ortholog, mouse LIX shares 63% aa sequence identity with an human GCP-2.
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