Platelet-Derived Growth Factor Subunit B (PDGFB) belongs to the PDGF/VEGF growth factor family. Platelet-derived growth factor is a potent mitogen for cells of mesenchymal origin. PDGFB can exist either as a homodimer (PDGF-BB) or as a heterodimer with the platelet-derived growth factor alpha polypeptide (PDGF-AB), where the dimers are connected by disulfide bonds. Mutations in this gene are associated with meningioma.Binding of PDGFB to its receptor elicits a variety of cellular responses. In addition, PDGFB is released by platelets upon wounding and plays an important role in stimulating adjacent cells to grow and thereby heals the wound.
PDGFRA; also known as CD140a; together with the structurally homolog protein PDGFRB (CD140b); are cell surface receptors for members of the platelet-derived growth factor family. They are members of the class III subfamily of receptor tyrosine kinase (RTKs) with the similar structure characteristics of five immunoglobulin-like domains in their extracellular region and a split kinase domain in their intracellular region. PDGFRA is expressed in oligodendrocyte progenitor cells and mesothelial cell; and binds all three ligand isoforms PDGF-AA; PDGF-BB and PDGF-AB with high affinity; whereas PDGFRB dose not bind PDGF-AA. PDGFRA plays an essential role in regulating proliferation; chemotaxis and migration of mesangial cells. Recent studies have indicated that PDGFRA acts as a critical mediator of signaling in testis organogenesis and Leydig cell differentiation; and in addition; particularly important for kidney development. Additionally; PDGFRA is involved in tumor angiogenesis and maintenance of the tumor microenvironment and has been implicated in development and metastasis of Hepatocellular carcinoma (HCC). PDGFRA may represent a potential therapeutic target in thymic tumours. PDGFRA gene amplification rather than gene mutation may be the underlying genetic mechanism driving PDGFRA overexpression in a portion of gliomas.
Platelet-derived Growth Factor Receptor Alpha (PDGF Rα) is an enzyme that belongs to the class III subfamily of receptor tyrosine kinases.It is a type I transmembrane glycoprotein, and can form homo- or hetero-dimeric receptors when engaged by dimers of the PDGF family of growth factors, PDGF Rα is strongly expressed in oligodendrocyte, lung, skin and intestinal progenitor cells and induced by inflammation or growth in culture, but is lowly expressed in most mesenchymal cells. PDGF Rα autophosphorylates upon dimerization, activating signaling cascades in PI-3kinase Ras-MAP kinase, and PLC-γ pathways. PDGF Rα has infulence on local gradients of epithelially produced PDGF-AA or PDGF-CC during formation of the cranial ,cardiac neural crest and interstitial kidney mesenchyme.
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. CD140b, also known as PDGFRB, is a member of the CD system. CD140b is a cell surface tyrosine kinase receptor essencial for development interacting with the platelet-derived growth factors (PDGFs) which serves as mitogens for mesenchymal cells. CD140b can bind with platelet-derived growth factor (PDGF)-B, that are secreted by tumors and phosphorylation of PDGFR-β was correlated with depth of cancer invasion at statistically significant level.
Platelet-Derived Growth Factor Receptor β (PDGFR-β) is a member of the protein kinase superfamily and CSF-1/PDGF receptor subfamily. The PDGF family consists of PDGF-A, -B, -C and -D, which form either homo- or heterodimers (PDGF-AA, -AB, -BB, -CC, -DD). The four PDGFs are inactive in their monomeric forms. The PDGFs bind to the protein tyrosine kinase receptors PDGF receptor-α and -β. These two receptor isoforms dimerize upon binding the PDGF dimer, leading to three possible receptor combinations, namely -αα, -ββ and -αβ. The extracellular region of the PDGF receptor-β consists of five immunoglobulin-like domains while the intracellular part is a tyrosine kinase domain. In addition to being a potent mitogen for cells of mesenchymal origin, PDGF has also been shown to be a potent chemoattractant for mesenchymal cells, mononuclear cells, and neutrophils and has been reported to be important in the modification of cellular matrix constituents.
Protein disulfide-isomerase A5 is a 519 amino acids protein that belongs to the protein disulfide isomerase family.It contains 3 thioredoxin domains.It can catalyze the rearrangement of -S-S- bonds in proteins.
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