Mouse DNAX accessory molecule-1(DNAM-1) is a type I transmembrane glycoprotein that belongs to the immunoglobulin superfamily. As an activating receptor, it interacts with the ligands CD155 and CD112, and activates natural killer (NK) cells via its immu-noreceptor tyrosine-based activatory motif (ITAM). Mature mouse DNAM-1 has extracellular domain (ECD) that contains two Ig-like C2-set domains, and possesses a cytoplasmic region that contains motifs for binding PDZ domains. DNAM-1 is expressed on several lymphoid and myeloid cell types and interacts with CD155/PVR and Nectin-2/CD112. Ligation of DNAM-1 promotes the activation of NK cells, CD8+ T cells, and mast cells, induces dendritic cell maturation, initiates megakaryocyte and activated platelet adhesion to vascular endothelial cells, and stimulates monocyte extravasation. Conversely, it inhibits the formation of osteoclasts. Platelet-endothelium interactions that are mediated by DNAM-1 enable the metastasis of tumor cells to the lung.
Siglecs (sialic acid binding Ig-like lectins) are I-type (Ig-type) lectins belonging to the Ig superfamily. They are characterized by an N-terminal Ig-like V-type domain which mediates sialic acid binding, followed by varying numbers of Ig-like C2-type domains. Human Siglec-2, also known as B-cell antigen CD22 or B-lymphocyte cell adhesion molecule (BL-CAM), is a B-cell restricted glycoprotein that is expressed in the cytoplasm of progenitor B and pre-B cells and on the surface of mature B cells. Two distinct human Siglec-2/CD22 cDNAs that arise from differential RNA processing of the same gene have been isolated. Siglec-2/CD22 is an adhesion molecule that preferentially binds alpha 2,6-linked sialic acid on the same (cis) or adjacent (trans) cells. Interaction of CD22 with trans ligands on opposing cells was found to be favored over the binding of ligands in cis.
Fc fragment of IgE, low affinity II, receptor for (CD23) or CD23 antigen is a member of the cluster of differentiation family. The cluster of differentiation (cluster of designation) (often abbreviated as CD) is a protocol used for the identification and investigation of cell surface molecules present on white blood cells initially but found in almost any kind of cell of the body, providing targets for immunophenotyping of cells. Physiologically, CD molecules can act in numerous ways, often acting as receptors or ligands (the molecule that activates a receptor) important to the cell. A signal cascade is usually initiated, altering the behavior of the cell (see cell signaling). Some CD proteins do not play a role in cell signaling, but have other functions, such as cell adhesion. CD23/FCER2 is a B-cell specific antigen, and a low-affinity receptor for IgE. It has essential roles in B cell growth and differentiation, and the regulation of IgE production. This protein also exists as a soluble secreted form, then functioning as a potent mitogenic growth factor. Increased levels of soluble CD23/FCER2 cause the recruitment of non-sensitised B-cells in the presentation of antigen peptides to allergen-specific B-cells, therefore increasing the production of allergen specific IgE. IgE, in turn, is known to upregulate the cellular expression of CD23 and Fc epsilon RI (high-affinity IgE receptor).
Inserisci la tua e-mail e seleziona le aree di interesse per ricevere le ultime novità, approfondimenti e promozioni.
Seleziona uno o più ambiti di interesse per ricevere comunicazioni più utili e mirate.
2025 TEMA Ricerca - All Rights Reserved.
