Signal-regulatory protein beta-1 (SIRPB1, CD172b) is a member of the signal-regulatory-protein (SIRP) family, and also belongs to the immunoglobulin superfamily. SIRP family members are receptor-type transmembrane glycoproteins known to be involved in the negative regulation of receptor tyrosine kinase-coupled signaling processes. This protein was found to interact with TYROBP/DAP12, a protein bearing immunoreceptor tyrosine-based activation motifs. This protein was also reported to participate in the recruitment of tyrosine kinase SYK.
Signal-regulatory protein beta-2(SIRP-beta-2), is a monomeric single pass type I membrane glycoprotein, belongs to the SIRP/SHPS (CD172) family of the immunoglobulin (Ig) superfamily. The SIRP family are paired receptors that have similar extracellular domains but differing C-terminal domains and functions. A positively charged residue within the transmembrane domain, in analogy to SIRP-beta-1, is implicated to mediate interaction with the adaptor DAP12 protein, which contains immunoreceptor tyrosine-based activation motifs (ITAMs) . Proteins in the SIRP family are typically expressed in immune cells, especially in the myeloid lineages . Based on expression patterns, SIRPs are thought to have roles in immune regulation. SIRP family members role in innate immunity and host defense has potential significance as a therapeutic target in cancer and inflammation. There are currently no known mouse or rat homologs for this protein.
Signal-Regulatory Protein Gamma (SIRPG) is a member of the signal-regulatory protein (SIRP) family and also belongs to the immunoglobulin superfamily. SIRPG is detected in the liver, and at very low levels in the brain, heart, lung, pancreas, kidney, placenta, and skeletal muscle. SIRPG is an immunoglobulin-like cell surface receptor. On binding with CD47, SIRPG mediates cell-cell adhesion. Engagement on T-cells by CD47 on antigen-presenting cells results in enhanced antigen-specific T-cell proliferation and costimulates T-cell activation. SIRPG as receptor-type transmembrane glycoproteins is involved in the negative regulation of receptor tyrosine kinase-coupled signaling processes.
Signal-regulatory protein gamma (SIRPG/SIRP gamma) also known as CD172 antigen-like family member B, CD172g, and CD172g antigen, is a member of the signal-regulatory protein (SIRP) family, and also belongs to the immunoglobulin superfamily. SIRP family members are receptor-type transmembrane glycoproteins known to be involved in the negative regulation of receptor tyrosine kinase-coupled signaling processes. SIRPG/SIRP gamma/CD172g is probable immunoglobulin-like cell surface receptor. On binding with CD47, SIRPG can mediate cell-cell adhesion. SIRPG/SIRP gamma is engagement on T-cells by CD47 on antigen-presenting cells results in enhanced antigen-specific T-cell proliferation and costimulates T-cell activation. SIRPG/SIRP gamma/CD172g is detected in liver, and at very low levels in brain, heart, lung, pancreas, kidney, placenta and skeletal muscle. Expressed on CD4+ T-cells, CD8+ T-cells, CD56-bright natural killer (NK) cells, CD20+ cells, and all activated NK cells. This cytokine is mainly present in the paracortical T-cell area of lymph nodes, with only sparse positive cells in the mantle and in the germinal center of B-cell follicles. In the thymus, SIRPG is primarily expressed in the medulla on mature T-lymphocytes that have undergone thymic selection.
SIRT3 is a nicotinamide adenine dinucleotide (NAD(+))-dependent mitochondrial protein deacetylase purported to influence metabolism through post-translational modification of metabolic enzymes. Sirtuin 3 (SIRT3) mediates cellular resistance toward various forms of stress. sirtuin 3 (SIRT3), the mitochondrial NAD(+)-dependent deacetylase, may regulate mitochondrial function and biosynthetic pathways such as glucose and fatty acid metabolism and the tricarboxylic acid (TCA) cycle, oxidative stress, and apoptosis by reversible protein lysine deacetylation. SIRT3 regulates glucose and lipid metabolism and maintains myocardial ATP levels, which protects the heart from metabolic disturbances. SIRT3 can also protect cardiomyocytes from oxidative stress-mediated cell damage and block the development of cardiac hypertrophy. Recent reports show that SIRT3 is involved in the protection of several heart diseases.
SLAMF3 (CD229) is a type I transmembrane glycoprotein in the SLAM subgroup of the CD2 family. Mature human SLAMF3 consists of a 407 amino acid (aa) extracellular domain (ECD) with two Ig-like V-set and two Ig-like truncated C2-set domains. The ECD of human SLAMF3 shares 57% - 59% aa sequence identity with mouse and rat SLAMF3. Within the first two Ig-like domains that are common to all SLAM proteins, human SLAMF3 shares 24% - 39% aa sequence identity with human 2B4, BLAME, CD2F-10, CD84, CRACC, NTB-A, and SLAM. It is expressed on T and B cells, thymocytes, and more weakly on NK cells. It may participate in adhesion reactions between T lymphocytes and accessory cells by homophilic interaction. Promotes T-cell differentiation into a helper T-cell Th17 phenotype leading to increased IL-17 secretion; the costimulatory activity requires SH2D1A. SLAMF3 may be involved in the maintenance of peripheral cell tolerance by serving as a negative regulator of the immune response. It also disable autoantibody responses and inhibit IFN-gamma secretion by CD4+ T-cells and negatively regulate the size of thymic innate CD8+ T-cells and the development of invariant natural killer T (iNKT) cells.
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