Interleukin 36 beta (IL-36B) is a member of the IL-1 family of proteins. It is a cytokine that binds to and signals through the IL1RL2/IL-36R receptor which in turn activates NF-kappa-B and MAPK signaling pathways in target cells linked to a pro-inflammatory response. IL-36B is synthesized in several cells including resting and activated monocytes, and B cells. The receptor for IL-36 beta is thought to be a combination of IL-1 Rrp2 and IL-1 RAcP. Interleukin 36 beta is one part of the IL-36 signaling system that is thought to be present in epithelial barriers and to take part in local inflammatory response, similar to the IL-1 system with which it shares the coreceptor IL1RAP. IL36B are involved in a number of fundamental biological processes such as stimulating production of interleukin-6 and interleukin-8, inducing expression of a number of antimicrobial peptides including beta-defensin 4 and beta-defensin 103 as well as a number of matrix metalloproteases , inducing the production of proinflammatory cytokines in bone marrow-derived dendritic cells (BMDCs), and activating p38 MAPK phosphorylation in BMDCs. Moreover, interleukin 36 beta may be involved in skin inflammatory response by acting on keratinocytes, dendritic cells, and indirectly on T cells to drive tissue infiltration, cell maturation and cell proliferation. It plays an important role in dendritic cell maturation by stimulating the surface expression of CD80, CD86 and MHC class II and inducing the production of IFN-gamma, IL-4 and IL-17 by T helper 1 (Th1) cells, cultured CD4+ T cells and splenocytes.
Interleukin-36 gamma (IL-36γ) is a member of the interleukin 1 cytokine family that includes three closely related genes, IL-36α, β, and γ, formerly known as IL-1F6, F8, and F9 respectively. IL-36α has been detected in both neuronal and synovial tissue, whereas IL-36β and IL-36γ are expressed in both cutaneous and mucosal epithelial cells, including the respiratory tract. IL-36β and IL-36γ stimulate proliferation, maturation and/or cytokine expression by innate immune cells (such as keratinocytes and dendritic cells), and adaptive immune cells (neutrophils and T-cells) in both humans and mice. The activity of IL-36α is mediated by interleukin 1 receptor-like 2 (IL1RL2/IL1R-rp2), and is specifically inhibited by interleukin 1 family, member 5 (IL1F5/IL-1 delta). IL-36γ plays an important role in communicating the cell death to surrounding cells.
The CD146 antigen, also known as melanoma cell adhesion molecule (MCAM) and MUC18, is an integral membrane glycoprotein belonging to the immunoglobulin superfamily. CD146 contains the characteristic immunoglobulin-like domains (V-V-C2-C2-C2), a transmembrane region and a short cytoplasmic tail. The CD146 expression is detected in endothelial cells in vascular tissue throughout the body, and plays a role in cell adhesion, as well as in cohesion of the endothelial monolayer at intercellular junctions in vascular tissue. As a Ca2+-independent cell adhesion molecule involved in heterophilic cell to cell interactions and a surface receptor, CD146 triggers tyrosine phosphorylation of FYN and PTK2 and subsequently induced signal transduction, proteolysis, or immune recognition. This protein is also expressed predominantly on metastatic lesions and advanced primary tumours, and thus has been suggested to play an important role in tumour progression and the development of metastasis in certain human carcinomas.
Junctional adhesion molecules (JAMs) are endothelial and epithelial adhesion molecules involved in the recruitment of circulating leukocytes to inflammatory sites. JAML (Junctional adhesion molecule-like); also known as AMICA1 (Adhesion molecule interacting with CXADR antigen 1); a protein related to the JAM family; is restricted to leukocytes and promotes their adhesion to endothelial cells. It contains 2 extracellular immunoglobulin-like domains; a transmembrane segment; and a cytoplasmic tail involved in activation signaling. Monocytic JAML/AMICA1 plays a critical role in regulating monocyte transendothelial migration (TEM) probably via binding to the endothelial coxsackie and adenovirus receptor (CAR) and other tight junction-associated adhesive molecules. The Expression of JAML/AMICA1 is restricted to the hematopoietic tissues with the exception of liver. JAML may function in transmigration of leukocytes through epithelial and endothelial tissues. Expressed at the plasma membrane of polymorphonuclear leukocytes; JAML/AMICA1 also enhances myeloid leukemia cell adhesion to endothelial cells.
Vaccinia H1-related phosphatase (VHR) is classified as a dual-specificity phosphatase (DUSP); and the other name is dual-specificity phosphatase 3 (DUSP3). DUSPs are a heterogeneous group of protein phosphatases that can dephosphorylate both phosphotyrosine and phosphoserine/phosphothreonine residues within the one substrate. Unlike typical DUSPs; VHR lacks mitogen-activated protein kinase (MAPK)-binding domain; and shows poor activity against MAPKs. VHR often act on bisphosphorylated protein substrates; it displays a strong preference for dephosphorylating phosphotyrosine residues over phosphothreonine residues. VHR has been identified as a novel regulator of extracellular regulated kinases (ERKs). VHR is responsible for the rapid inactivation of ERK following stimulation and for its repression in quiescent cells. VHR is a negative regulator of the Erk and Jnk pathways in T cells and; therefore; may play a role in aspects of T lymphocyte physiology that depend on these kinases.
Human Interleukin-36 Receptor Antagonist (IL-36RN) is a secreted protein which belongs to the Interleukin 1 cytokine family (IL-1 family). IL-36RN is predominantly expressed in keratinocytes but not in fibroblasts, endothelial cells or melanocytes. IL-36RN is also detected in the spleen, brain leukocyte and macrophage cell types. Increased in lesional psoriasis skin. IL-36RN is a highly and a specific antagonist of the IL-1 receptor-related protein 2-mediated response to Interleukin 1 family member 9 (IL1F9). Dysregulated expression of novel agonistic and antagonistic IL-1 family member ligands can promote cutaneous inflammation, revealing potential novel targets for the treatment of inflammatory skin disorders. Human and mouse IL-36RN share 90% sequence identity.
CD123; also known as Interleukin-3 receptor subunit alpha; belongs to the type I cytokine receptor family. In mouse; there are two classes of high-affinity IL3 receptors. One contains an IL3-specific beta subunit and the other contains the beta subunit also shared by high-affinity IL5 and GM-CSF receptors. CD123 stimulates the proliferation and differentiation of hemopoietic cells including the pluripotent hematopoietic stem cells as well as various lineage committed cells. CD123 is a heterodimer consisting of an alpha and a beta subunit. The alpha subunit alone binds IL-3 with low affinity. The beta subunit does not bind IL-3 by itself but is required for the high affinity binding of IL-3 to the heterodimeric receptor complex.
CD123; also known as Interleukin-3 receptor subunit alpha; belongs to the type I cytokine receptor family. In mouse; there are two classes of high-affinity IL3 receptors. One contains an IL3-specific beta subunit and the other contains the beta subunit also shared by high-affinity IL5 and GM-CSF receptors. CD123 stimulates the proliferation and differentiation of hemopoietic cells including the pluripotent hematopoietic stem cells as well as various lineage-committed cells. CD123 is a heterodimer consisting of an alpha and a beta subunit. The alpha subunit alone binds IL-3 with low affinity. The beta subunit does not bind IL-3 by itself but is required for the high-affinity binding of IL-3 to the heterodimeric receptor complex.
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