CD40 is a Type I Transmembrane Glycoprotein that belongs to the TNF Receptor Superfamily. CD40 is expressed in B cells, follicular dendritic cells, dendritic cells, activated monocytes, macrophages, endothelial cells, vascular smooth muscle cells, and several tumor cell lines. The extracellular domain of CD40 is characterized by Cysteine rich repeat regions. Interaction of CD40 with its ligand (CD40L) leads to aggregation of CD40 molecules, which in turn interact with cytoplasmic components to initiate signaling pathways. Several different TRAF proteins (adaptor proteins) have been identified to serves as mediators of the signal transduction. CD40 plays an essential role in mediating a broad variety of immune and inflammatory responses including T cell-dependent immunoglobulin class switching, memory B cell development, and germinal center formation.
CD40, also known as TNFRSF5, is a member of the TNF receptor superfamily which are single transmembrane-spanning glycoproteins. CD40 protein plays an essential role in mediating a broad variety of immune and inflammatory responses including T cell-dependent immunoglobulin class switching, memory B cell development, and germinal center formation. CD40 protein is expressed in B cells, dendritic cells, macrophages, endothelial cells, and several tumor cell lines. Defects in CD40 result in hyper-IgM immunodeficiency type 3 (HIGM3). In addition, CD40/CD40L interaction is found to be necessary for amyloid-beta-induced microglial activation, and thus is thoμght to be an early event in Alzheimer disease pathogenesis.
Protein tyrosine phosphatase, receptor type C (CD45), also known as PTPRC is a member of the protein tyrosine phosphatase (PTP) family which is known for its function to serve as signaling molecules and to regulate a variety of cellular processes such as cell proliferation, differentiation, mitotic cycle and oncogenic transformation. It is a variably glycosylated 180-220 kDa transmembrane protein that is abundantly expressed on all nucleated cells of hematopoietic origin. CD45 has several isoforms, expressed according to cell type, developmental stage and antigenic exposure. CD45 has been best studied in T cells, where it determines T cell receptor signaling thresholds. CD45 is moved into or out of the immunological synapse (IS) membrane microdomain depending on the relative influence of interaction with the extracellular galectin lattice or the intracellular actin cytoskeleton. Galectin interaction can be fine-tuned by varying usage of the heavily O-glycosylated spliced regions and sialylation of N-linked carbohydrates. Within the IS, CD45 dephosphorylates and negatively regulates the src family kinase, LCK. In other leukocytes, CD45 influences differentiation and links immunoreceptor signaling with cytokine secretion and cell survival, partially overlapping in function with DEP-1/CD148. CD45 deletion causes in severe immunodeficiency, while point mutations may be associated with autoimmune disorders.
The cluster of differentiation (CD) system is commonly used as cell markers in immunophynotyping. Different kinds of cells in the immune system can be identified through the surface CD molecules which associating with the immune function of the cell. There are more than 320 CD unique clusters and subclusters have been identified. Some of the CD molecules serve as receptors or ligands important to the cell through initiating a signal cascade which then alter the behavior of the cell. Some CD proteins do not take part in cell signal process but have other functions such as cell adhesion. Protein tyrosine phosphatase, receptor type C (CD45), also known as PTPRC is a member of the protein tyrosine phosphatase (PTP) family which is known for its function to serve as signaling molecules and to regulate a variety of cellular processes such as cell proliferation, differentiation, mitotic cycle and oncogenic transformation. CD45 is found expression specifically in hemotopietic cells. CD45 consists of an extracellular domain, a single transmembrane segment and two tandem intracytoplasmic catalytic domains. It serves as an essential regulator of T-cell and B-cell antigen receptor signaling through either direct interaction with components of the antigen receptor complexs or by activating various Src family kinases required for the antigen receptor signaling and it also can suppress JAK kinases.
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