SLAM family member 5 (SLAMF5/CD84) is a type I transmembrane protein in the SLAM subgroup of the CD2 family. SLAM family proteins regulate multiple aspects of immune system function. Mature human CD84 consists of a 204 amino acid (aa) extracellular domain (ECD) with two Iglike domains,a 21 aa transmembrane segment, and a 99 aa cytoplasmic domain with two immunoreceptor tyrosinebased switch motifs (ITSMs). CD84 exhibits homophilic binding which is mediated by the N-terminal Ig-like domain. Ligation induces tyrosine phosphorylation in the cytoplasmic ITSMs which then recruit the signaling adaptor molecules SAP (SLAM-associated protein) and EAT-2(EWS/Fli1-activated transcript 2).CD84 signaling inhibits Fc epsilon RI-induced mast cell activation but enhances platelet activation. LPS-induced macrophage activation,T cell proliferation and IFN-γproduction, and the interactions between T cells and B cells that are required for germinal center formation.
SLAM Family Member 6 (SLAMF6) is a 60 kD single-pass type I membrane protein that belongs to the SLAM subgroup of the CD2 family. Human SLAMF6/ NTB-A contains a 205 amino acid extracellular domain (ECD) with one Ig-like V-set and one Ig-like C2-set domain, a 21 amino acid transmembrane segment and an 84 amino acid cytoplasmic domain, with two immunoreceptor tyrosine-based switch motifs. SLAMF6 is a homodimer. SLAMF6 can interact with PTN6 and, upon phosphorylation, with PTN11 and SH2D1A/SAP. Phosphorylation-dependent NTB-A association with SAP is required for full production of IFN-γ by NK cells and independent of EAT-2 binding. It Triggers cytolytic activity only in natural killer cells (NK) expressing high surface densities of natural cytotoxicity receptors. On B cells, NTB-A modulates immunoglobulin class switching and the balance between tolerance and autoimmunity.
SLAMF7 is a single-pass type I membrane protein and contains 1 Ig-like C2-type (immunoglobulin-like) domain. SLAMF7 is expressed in NK cells, activated B-cells, NK-cell line but not in promyelocytic, B-cell lines, or T-cell lines. Although the cytoplasmic domain of CS1 contains immunoreceptor tyrosine-based switch motifs (ITSM), which enables to recruite signaling lymphocyte activation molecule (SLAM)-associated protein (SAP/SH2D1A), it activates NK cells in the absence of a functional SAP. SLAMF7 positively regulated natural killer cell functions by a mechanism dependent on the adaptor EAT-2 but not the related adaptor SAP. However, in the absence of EAT-2, CRACC potently inhibited natural killer cell function. It was also inhibitory in T cells, which are typically devoid of EAT-2. Thus, SLAMF7 can exert activating or inhibitory influences on cells of the immune system depending on cellular context and the availability of effector proteins.
SLITRK1 (Slit and Trk-like family member 1) is a integral membrane protein belonging to the SLITRK family consists of at least 6 members (SLITRK1-6). They are named and characterized by the presence of two leucine-rich repeats (LRRs) in the extracellular domain similar to those found in a secreted axonal growth-controlling protein; Slit; as well as a C-terminal domain with homology to Trk neurotrophin tyrosine kinase receptors. Expression of SLITRKs are highly restricted to neural tissues; and are identified as the neuronal components modulating the neurite outgrowth. More specifically; SLITRK1 expression is found in the mature neurons of the cerebrum; thalamus and hippocampus; and induces unipolar neurites in cultured neuronal cells. Human SLITRK1 is a 696 amino acid precursor protein; and one truncating frameshift mutation (448 aa) has been linked to Tourette's syndrome; a genetically influenced developmental neuropsychiatric disorder characterized by chronic vocal and motor tics. In addition; all SLITRK genes are differentially expressed in brain tumors; such as astrocytoma; oligodendroglioma; glioblastoma; and are suggested to be useful molecular indicators of brain tumor properties.
SLIT and NTRK-like family proteins 4 is a member of the SLIT and NTRK-like family.This protein is characterized as an integral membrane protein that has two leucine-rich repeat (LRR) domains and a carboxy-terminal domain that is partially similar to SLIT protein andTRK Neurotrophin There are six members in this family: SLITRK1, SLITRK2, SLITRK3, SLITRK4, SLITRK5, and SLITRK6. Their expression was detected mainly in the brain, but the expression profile of each SLITRK was unique. Each of these members is located in nervous system except for SLITRK6. SLITRK expression was also investigated in various types of brain tumor tissue.
Secretory leukoprotease inhibitor (SLPI); also called antileukoprotease (ALP); is a 12-kDa; nonglycosylated serine protease inhibitor present in mucous secretions. It is thought to play a role in protecting the mucosae from injury associated with inflammation. SLPI is locally produced by serous cells; including bronchial submucosal glands. Elafin and SLPI are members of larger families of proteins secreted predominantly at mucosal sites; and have been shown to be modulated in multiple pathological conditions. Elafin and SLPI are structurally related in that both have a fold with a four-disulfide core or whey acidic protein (WAP) domain responsible for inhibiting proteases. SLPI is a prominent innate immune protein of the respiratory tract; possessing serine protease inhibitor activity; antibacterial activity; and anti-inflammatory/immunomodulatory activity.
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