Cytokines & Chemokines

TSLP is a hemopoietic protein that is expressed in the heart, liver and prostate. TSLP overlaps biological activities with IL-7 and binds with the heterodimeric receptor complex consisting of the IL-7R alpha chain (IL-7Rα) and the TSLP-specific chain (TSLPR). Like IL-7, TSLP induces phosphorylation of STAT3 and STAT5, but uses kinases other than the JAKs for activation. TSLP prohibited apoptosis and stimulated growth of the human acute myeloid leukemia (AML)-derived cell line MUTZ3. It induces the release of T cell-attracting chemokines TARC and MDC from monocytes and activates CD11c(+) dendritic cells (DCs). TSLP activated DCs primed naive T cells to produce the proallergic cytokines (IL-4, IL-5, IL-13, TNFα) while down-regulating IL-10 and IFN-γ suggesting a role in initiating allergic inflammation.

PEDF is a noninhibitory serpin with neurotrophic, anti-angiogenic, and anti-tumorigenic properties. It is a 50 kDa glycoprotein produced and secreted in many tissues throughout the body. A major component of the anti-angiogenic action of PEDF is the induction of apoptosis in proliferating endothelial cells. In addition, PEDF is able to inhibit the activity of angiogenic factors such as VEGF and FGF-2. The neuroprotective effects of PEDF are achieved through suppression of neuronal apoptosis induced by peroxide, glutamate, or other neurotoxins. The recent identification of a lipase-linked cell membrane receptor for PEDF (PEDF-R) that binds to PEDF with high affinity should facilitate further elucidation of the underlying mechanisms of this pluripotent serpin. To date, PEDF-R is the only signaling receptor known to be used by a serpin family member. The unique range of PEDF activities implicate it as a potential therapeutic agent for the treatment of vasculature related neurodegenerative

PEDF is a noninhibitory serpin with neurotrophic, anti-angiogenic, and anti-tumorigenic properties. It is a 50 kDa glycoprotein produced and secreted in many tissues throughout the body. A major component of the anti-angiogenic action of PEDF is the induction of apoptosis in proliferating endothelial cells. In addition, PEDF is able to inhibit the activity of angiogenic factors such as VEGF and FGF-2. The neuroprotective effects of PEDF are achieved through suppression of neuronal apoptosis induced by peroxide, glutamate, or other neurotoxins. The recent identification of a lipase-linked cell membrane receptor for PEDF (PEDF-R) that binds to PEDF with high affinity should facilitate further elucidation of the underlying mechanisms of this pluripotent serpin. To date, PEDF-R is the only signaling receptor known to be used by a serpin family member. The unique range of PEDF activities implicate it as a potential therapeutic agent for the treatment of vasculature related neurodegenerative

BAFF Receptor (BAFF-R), a member of the TNFR superfamily, is highly expressed in spleen, lymph node, and resting B cells and to some extent in activated B cells, resting CD4+ cells and peripheral blood leukocytes. BAFF-R is a type III transmembrane protein that binds with high specificity to BAFF (TNFSF13B). BAFF-R/BAFF signaling plays a critical role in B cell survival and maturation.

BAFF Receptor (BAFF-R), a member of the TNFR superfamily, is highly expressed in spleen, lymph node, and resting B cells and to some extent in activated B cells, resting CD4+ cells and peripheral blood leukocytes. BAFF-R is a type III transmembrane protein that binds with high specificity to BAFF (TNFSF13B). BAFF-R/BAFF signaling plays a critical role in B cell survival and maturation.

CD40 ligand, CD40L (also known as CD154, TRAP or gp39), is a 261 amino acid type II transmembrane glycoprotein belonging to the TNF family, CD40L is expressed predominantly on activated CD4+ T lymphocytes, and also found in other types of cells, like NK cells, mast cells, basophils and eosinophils. Human CD40L shares 78% amino acid identity with its mouse counterpart. The receptor of CD40L is CD40, a type I transmembrane glycoprotein belonging to the TNF receptor family. CD40 is expressed on B lymphocytes, monocytes, dendritic cells and thymic epithelium. Although all monomeric, dimeric and trimeric forms of soluble CD40L can bind to CD40, the trimeric form of soluble CD40L has the most potent biological activity through oligomerization of cell surface CD40, a common feature of TNF receptor family members. CD40L mediates a range of activities on B cells including induction of activation-associated surface antigen, entry into cell cycle, isotype switching and Ig secretion and memory gen

CD40 ligand, CD40L (also known as CD154, TRAP or gp39), is a 261 amino acid type II transmembrane glycoprotein belonging to the TNF family, CD40L is expressed predominantly on activated CD4+ T lymphocytes, and also found in other types of cells, like NK cells, mast cells, basophils and eosinophils. Human CD40L shares 78% amino acid identity with its mouse counterpart. The receptor of CD40L is CD40, a type I transmembrane glycoprotein belonging to the TNF receptor family. CD40 is expressed on B lymphocytes, monocytes, dendritic cells and thymic epithelium. Although all monomeric, dimeric and trimeric forms of soluble CD40L can bind to CD40, the trimeric form of soluble CD40L has the most potent biological activity through oligomerization of cell surface CD40, a common feature of TNF receptor family members. CD40L mediates a range of activities on B cells including induction of activation-associated surface antigen, entry into cell cycle, isotype switching and Ig secretion and memory gen

BCMA, a member of the TNF receptor superfamily, binds to BAFF and APRIL. BCMA is expressed on mature B-cells and other B-cell lines and plays an important role in B cell development, function and regulation. BCMA also has the capability to activate NF-kappaB and JNK. The human BCMA gene codes for a 184 amino acid type I transmembrane protein, which contains a 54 amino acid extracellular domain, a 23 amino acid transmembrane domain, and a 107 amino acid extracellular domain.

BCMA, a member of the TNF receptor superfamily, binds to BAFF and APRIL. BCMA is expressed on mature B-cells and other B-cell lines and plays an important role in B cell development, function and regulation. BCMA also has the capability to activate NF-kappaB and JNK. The human BCMA gene codes for a 184 amino acid type I transmembrane protein, which contains a 54 amino acid extracellular domain, a 23 amino acid transmembrane domain, and a 107 amino acid extracellular domain.