Extracellular Matrix Metalloproteinase Inducer (EMMPRIN) belongs to the immunoglobulin superfamily, which has the homology to both the immunoglobulin V domain and MHC class II antigen β-chain. EMMPRIN is a transmembrane glycoprotein with different forms, resulting from different modes of glycosylation and N-terminal sequence variants. EMMPRIN can be expressed in breast cancer, oral squamous cell carcinoma, glioma, lymphoma, lung, bladder, and melanoma carcinomas cells. EMMPRIN promotes invasion, metastasis, growth, and survival of malignants cells, serves as a receptor for extracellular cyclophilinthe, may play a role in signal transduction.
CD147/EMMPRIN (Extracellular Matrix Metalloproteinase Inducer), also known as Basigin (BSG), is a transmembrane glycoprotein with different forms resulted from different modes of glycosylation and N-terminal sequence variants. It is a member of the immunoglobulin superfamily with homology to both the immunoglobulin V domain and MHC class II antigen beta-chain. This protein play important roles in variety of events including spermatogenesis, embryo implantation, neural network formation. CD147 induces the production and release of matrix metalloproteinases (MMP) in the surrounding mesenchymal cells and tumor cells, and thereby promotes invasion, metastasis, growth and survival of malignant cells. Furthermore, CD147 also serves as a receptor for extracellular cyclophilinthe and its association with integrins might be important in signal transduction. Recently, CD147 displays increased expression in many cancers, and it has been previously demonstrated to participate in cancer metastasis and progression. Thus, CD147 and its antibody are used as an effective treatment for malignant cancers.
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. Cluster of differentiation 14 (CD14) is a member of the CD system. It takes its name from its inclusion in the CD molecule surface marker proteins. CD14 exists in two forms: a form anchored into the membrane or a soluble form. CD14 was found expressed in macrophages, neutrophil granulocyte and dendritic cells. The major function is serve as a co-receptor (along with TLR4 and MD-2) for the bacterial lipopolysaccharide (LPS) and other pathogen-associated molecular patterns.
CD14 is a cell surface glycoprotein that is preferentially expressed on monocytes/macrophages. CD14 is anchored to cells by linkage to glycosylphosphatidylinositol (GPI) and functions as a pattern recognition receptor that binds lipopolysaccharides (LPS) and a variety of ligands derived from different microbial sources. The binding of CD14 with LPS is catalyzed by LPS binding protein (LBP). Toll like receptors have also been implicated in the transduction of CD14-LPS signals. Soluble CD14 can be released from the cell surface by phosphatidyinositolspecific phospholipase C and has been detected in serum and body fluids. High concentrations of soluble CD14 have been shown to inhibit LPS mediated responses. However, soluble CD14 can also potentiate LPS response in cells that do not express cell surface CD14.
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