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.
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.
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.
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.
Protein Disulfide-Isomerase A6 (PDIA6) is a 48.5kDa protein that belongs to the protein disulfide isomerase family (PDI). PDIA6 is an enzyme in the endoplasmic reticulum in eukaryotes which catalyzes the formation and breakage of disulfide bonds between cysteine residues within proteins as they fold. The PDIA6 expressed in platelets, its functions as a chaperone that inhibits aggregation of misfolded proteins. PDIA6 is part a large chaperone multiprotein complex comprising DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PDIA6, PPIB, SDF2L1, UGT1A1. PDIA6 also plays a role in platelet aggregation and activation by agonists such as convulxin, collagen and thrombin.
Protein Disulfide-Isomerase-Like Protein of the Testis (PDILT) is a protein that belongs to the protein disulfide isomerase family. Human PDILT is synthesized as a 584 amino acid precursor that contains an 20 amino acid signal sequence and a 564 amino acid mature chain. PDILT contains 1 thioredoxin domain lacks the conserved redox-active Cys at position 417 which is replaced by a Ser residue, suggesting that it lacks thioredoxin activity. PDILT is an enzyme in the endoplasmic reticulum in eukaryotes. It is not a disulfide-linked homodimer. The PDILT protein can interacts with ERO1L and CLGN. PDILT probable redox-inactive chaperone involved in spermatogenesis.
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