Cytokines & Chemokines

Leukocyte surface antigen CD47 is also known as Antigenic surface determinant protein OA3, Integrin-associated protein (IAP) and Protein MER6. CD47 contains 1 Ig-like V-type (immunoglobulin-like) domain. CD47 is a 40‑60 kDa variably glycosylated atypical member of the immunoglobulin superfamily and an integral membrane protein that consists of a 123 amino acid (aa) extracellular domain (ECD) with a single Ig-like domain, five membrane-spanning regions with short intervening loops, and a 34 aa C-terminal cytoplasmic tail. CD47 has a role in both cell adhesion by acting as an adhesion receptor for THBS1 on platelets, and in the modulation of integrins and plays an important role in memory formation and synaptic plasticity in the hippocampus by similarity. CD47 is the receptor for SIRPA, binding to which prevents maturation of immature dendritic cells and inhibits cytokine production by mature dendritic cells. CD47 Interaction with SIRPG mediates cell-cell adhesion, enhances superantigen-

Signal regulatory protein alpha (SIRPα, designated CD172a), is also known as CD172 antigen-like family member A (CD172a), also called SHPS-1 (SHP substrate 1) and previously, MyD-1 (Myeloid/Dendritic-1), which is a monomeric about 90kDa type I transmembrane glycoprotein that belongs to the SIRP/SHPS (CD172) family of the immunoglobulin superfamily. SIRPα is Ubiquitous and highly expressed in brain. SIRPA/CD172a is immunoglobulin-like cell surface receptor for CD47 and acts as docking protein and induces translocation of PTPN6, PTPN11 and other binding partners from the cytosol to the plasma membrane. SIRPA/SHPS-1 supports adhesion of cerebellar neurons, neurite outgrowth and glial cell attachment and may play a key role in intracellular signaling during synaptogenesis and in synaptic function by similarity. SIRPα recognition of surfactants SP-A and SP-D in the lung can inhibit alveolar macrophage cytokine production.

Signal regulatory protein alpha (SIRPα, designated CD172a), is also known as CD172 antigen-like family member A (CD172a), also called SHPS-1 (SHP substrate 1) and previously, MyD-1 (Myeloid/Dendritic-1), which is a monomeric about 90kDa type I transmembrane glycoprotein that belongs to the SIRP/SHPS (CD172) family of the immunoglobulin superfamily. SIRPα is Ubiquitous and highly expressed in brain. SIRPA/CD172a is immunoglobulin-like cell surface receptor for CD47 and acts as docking protein and induces translocation of PTPN6, PTPN11 and other binding partners from the cytosol to the plasma membrane. SIRPA/SHPS-1 supports adhesion of cerebellar neurons, neurite outgrowth and glial cell attachment and may play a key role in intracellular signaling during synaptogenesis and in synaptic function by similarity. SIRPα recognition of surfactants SP-A and SP-D in the lung can inhibit alveolar macrophage cytokine production.

Lymphocyte activation gene-3 (LAG-3), also known as CD223, is a cell-surface 70kDa molecule belong to Ig superfamily with diverse biologic effects on T cell function. LAG-3 is a CD4 homolog originally cloned in 1990. The gene for LAG-3 lies adjacent to the gene for CD4 on human chromosome 12 (12p13) and is approximately 20% identical to the CD4 gene. human LAG-3 shares 70%, 67%, 76%, and 73% aa sequence identity with mouse, rat, porcine, and bovine LAG-3, respectively. LAG-3 is expressed on B cells, NK cells, tumor-infiltrating lymphocytes, and a subset of T cells. LAG-3 was relatively overexpressed on transgenic T cells rendered anergic in vivo by encounter with cognate self-antigen. LAG-3 negatively regulates murine T cell activation and homeostasis. LAG-3 activates antigen-presenting cells through MHC class II signaling, leading to increased antigen-specific T-cell responses in vivo. Blocking or knocking out LAG-3 in neuronal cultures or in animals mitigated the transmission of α-sy

Lymphocyte activation gene-3 (LAG-3), also known as CD223, is a cell-surface 70kDa molecule belong to Ig superfamily with diverse biologic effects on T cell function. LAG-3 is a CD4 homolog originally cloned in 1990. The gene for LAG-3 lies adjacent to the gene for CD4 on human chromosome 12 (12p13) and is approximately 20% identical to the CD4 gene. human LAG-3 shares 70%, 67%, 76%, and 73% aa sequence identity with mouse, rat, porcine, and bovine LAG-3, respectively. LAG-3 is expressed on B cells, NK cells, tumor-infiltrating lymphocytes, and a subset of T cells. LAG-3 was relatively overexpressed on transgenic T cells rendered anergic in vivo by encounter with cognate self-antigen. LAG-3 negatively regulates murine T cell activation and homeostasis. LAG-3 activates antigen-presenting cells through MHC class II signaling, leading to increased antigen-specific T-cell responses in vivo. Blocking or knocking out LAG-3 in neuronal cultures or in animals mitigated the transmission of α-sy

Programmed death (PD-1) is an immunoinhibitory receptor that belongs to the CD28 family and is expressed on T cells, B cells, monocytes, natural killer cells, and many tumor-infiltrating lymphocytes (TILs); PD-1 is a type I membrane protein of 268 amino acids and which structure includes an extracellular IgV domain followed by a transmembrane region and an intracellular tail. The intracellular tail contains two phosphorylation sites located in an immunoreceptor tyrosine-based inhibitory motif and an immunoreceptor tyrosine-based switch motif, which suggests that PD-1 negatively regulates TCR signals. This is consistent with binding of SHP-1 and SHP-2 phosphatases to the cytoplasmic tail of PD-1 upon ligand binding. It has 2 ligands that have been described PD-L1(B7H1) and PD-L2(B7-DC); PD-1 induction on activated T cells occurs in response to PD-L1 or L2 engagement and limits effector T-cell activity in peripheral organs and tissues during inflammation, thus preventing autoimmunity.Rec

Programmed death (PD-1) is an immunoinhibitory receptor that belongs to the CD28 family and is expressed on T cells, B cells, monocytes, natural killer cells, and many tumor-infiltrating lymphocytes (TILs); PD-1 is a type I membrane protein of 268 amino acids and which structure includes an extracellular IgV domain followed by a transmembrane region and an intracellular tail. The intracellular tail contains two phosphorylation sites located in an immunoreceptor tyrosine-based inhibitory motif and an immunoreceptor tyrosine-based switch motif, which suggests that PD-1 negatively regulates TCR signals. This is consistent with binding of SHP-1 and SHP-2 phosphatases to the cytoplasmic tail of PD-1 upon ligand binding. It has 2 ligands that have been described PD-L1(B7H1) and PD-L2(B7-DC); PD-1 induction on activated T cells occurs in response to PD-L1 or L2 engagement and limits effector T-cell activity in peripheral organs and tissues during inflammation, thus preventing autoimmunity.Rec

Programmed death-ligand 1 (PD-L1) also known as cluster of differentiation 274 (CD274) or B7 homolog 1 (B7-H1), is a protein that in humans is encoded by the CD274 gene. PD-L1 is a 40 kDa type 1 transmembrane protein that has been speculated to play a major role in suppressing the immune system during particular events such as pregnancy, tissue allografts, autoimmune disease and other disease states such as hepatitis. Normally the immune system reacts to foreign antigens where there is some accumulation in the lymph nodes or spleen which triggers a proliferation of antigen-specific CD8+ T cell. The formation of PD-1 receptor / PD-L1 or B7.1 receptor /PD-L1 ligand complex transmits an inhibitory signal which reduces the proliferation of these CD8+ T cells at the lymph nodes and supplementary to that PD-1 is also able to control the accumulation of foreign antigen specific T cells in the lymph nodes through apoptosis which is further mediated by a lower regulation of the gene Bcl-2. PD-L

Programmed death-ligand 1 (PD-L1) also known as cluster of differentiation 274 (CD274) or B7 homolog 1 (B7-H1), is a protein that in humans is encoded by the CD274 gene. PD-L1 is a 40 kDa type 1 transmembrane protein that has been speculated to play a major role in suppressing the immune system during particular events such as pregnancy, tissue allografts, autoimmune disease and other disease states such as hepatitis. Normally the immune system reacts to foreign antigens where there is some accumulation in the lymph nodes or spleen which triggers a proliferation of antigen-specific CD8+ T cell. The formation of PD-1 receptor / PD-L1 or B7.1 receptor /PD-L1 ligand complex transmits an inhibitory signal which reduces the proliferation of these CD8+ T cells at the lymph nodes and supplementary to that PD-1 is also able to control the accumulation of foreign antigen specific T cells in the lymph nodes through apoptosis which is further mediated by a lower regulation of the gene Bcl-2. PD-L