Basigin (BSG) also known as extracellular matrix metalloproteinase inducer (EMMPRIN) or cluster of differentiation 147 (CD147) is a protein that in humans is encoded by the BSGgene. This protein is a determinant for the Ok blood group system. Basigin has been shown to be an essential receptor on red blood cells for the human malaria parasite, Plasmodium falciparum.
Basigin is a member of the immunoglobulin superfamily, with a structure related to the putative primordial form of the family. As members of the immunoglobulin superfamily play fundamental roles in intercellular recognition involved in various immunologic phenomena, differentiation, and development, basigin is thought also to play a role in intercellular recognition (Miyauchi et al., 1991; Kanekura et al., 1991).
Basigin has been shown to form a complex with monocarboxylate transporters in the retina of mice. Basigin appears to be required for proper placement of MCTs in the membrane. In the Basigin null mouse, the failure of MCTs to integrate with the membrane may be directly linked to a failure of nutrient transfer in the retinal pigmented epithelium (the lactates transported by MCTs 1, 3, and 4 are essential nutrients for the developing RPE), resulting in loss of sight in the null animal.
It has recently (November 2011) been found that basigin is a receptor that is essential to erythrocyte invasion by most strains of Plasmodium falciparum, the most virulent species of the plasmodium parasites that cause human malaria. It is hoped that by developing antibodies to the parasite ligand for Basigin, Rh5, a better vaccine for malaria might be found. Basigin is bound by the PfRh5 protein on the surface of the malaria parasite.
^Kasinrerk W, Fiebiger E, Stefanová I, Baumruker T, Knapp W, Stockinger H (1992). "Human leukocyte activation antigen M6, a member of the Ig superfamily, is the species homologue of rat OX-47, mouse basigin, and chicken HT7 molecule". J Immunol. 149 (3): 847–54. PMID1634773.
^Miyauchi T, Masuzawa Y, Muramatsu T (1992). "The basigin group of the immunoglobulin superfamily: complete conservation of a segment in and around transmembrane domains of human and mouse basigin and chicken HT7 antigen". J. Biochem. 110 (5): 770–4. PMID1783610.
^Kanekura T, Chen X, Kanzaki T (2002). "Basigin (CD147) is expressed on melanoma cells and induces tumor cell invasion by stimulating production of matrix metalloproteinases by fibroblasts". Int. J. Cancer. 99 (4): 520–8. doi:10.1002/ijc.10390. PMID11992541.
^Yurchenko V, Zybarth G, O'Connor M, Dai W, Franchin G, Hao T, Guo H, Hung H, Toole B, Gallay P, Sherry B, Bukrinsky M (2002). "Active site residues of cyclophilin A are crucial for its signaling activity via CD147". J Biol Chem. 277 (25): 22959–65. doi:10.1074/jbc.M201593200. PMID11943775.
^Yurchenko V, O'Connor M, Dai W, Guo H, Toole B, Sherry B, Bukrinsky M (2001). "CD147 is a signaling receptor for cyclophilin B". Biochem Biophys Res Commun. 288 (4): 786–8. doi:10.1006/bbrc.2001.5847. PMID11688976.
^Berditchevski F, Chang S, Bodorova J, Hemler M (1997). "Generation of monoclonal antibodies to integrin-associated proteins. Evidence that alpha3beta1 complexes with EMMPRIN/basigin/OX47/M6". J Biol Chem. 272 (46): 29174–80. doi:10.1074/jbc.272.46.29174. PMID9360995.
^Wang, Wen-Juan; Li Qing-Quan; Xu Jing-Da; Cao Xi-Xi; Li Hai-Xia; Tang Feng; Chen Qi; Yang Jin-Ming; Xu Zu-De; Liu Xiu-Ping (2008). "Interaction between CD147 and P-glycoprotein and their regulation by ubiquitination in breast cancer cells". Chemotherapy. Switzerland. 54 (4): 291–301. doi:10.1159/000151225. PMID18689982.
^W.J. Philip; J.D. Ochrietor; C. Rudoy; T. Muramatsu; P.J. Linser (2003). "Loss of MCT1, MCT3, and MCT4 expression in the retinal pigment epithelium and neural retina of the 5A11/basigin-null mouse". Invest.Ophthalmol.Vis.Sci. United States. 44 (3): 1305–1311. doi:10.1167/iovs.02-0552. PMID12601063.
Muramatsu T, Miyauchi T (2004). "Basigin (CD147): a multifunctional transmembrane protein involved in reproduction, neural function, inflammation and tumor invasion". Histol. Histopathol. 18 (3): 981–7. PMID12792908.
Yan L, Zucker S, Toole BP (2005). "Roles of the multifunctional glycoprotein, emmprin (basigin; CD147), in tumour progression". Thromb. Haemost. 93 (2): 199–204. doi:10.1160/TH04-08-0536. PMID15711733.
Kasinrerk W, Fiebiger E, Stefanová I, et al. (1992). "Human leukocyte activation antigen M6, a member of the Ig superfamily, is the species homologue of rat OX-47, mouse basigin, and chicken HT7 molecule". J. Immunol. 149 (3): 847–54. PMID1634773.
Nabeshima K, Lane WS, Biswas C (1991). "Partial sequencing and characterization of the tumor cell-derived collagenase stimulatory factor". Arch. Biochem. Biophys. 285 (1): 90–6. doi:10.1016/0003-9861(91)90332-D. PMID1846736.
Biswas C, Zhang Y, DeCastro R, et al. (1995). "The human tumor cell-derived collagenase stimulatory factor (renamed EMMPRIN) is a member of the immunoglobulin superfamily". Cancer Res. 55 (2): 434–9. PMID7812975.
Kaname T, Miyauchi T, Kuwano A, et al. (1993). "Mapping basigin (BSG), a member of the immunoglobulin superfamily, to 19p13.3". Cytogenet. Cell Genet. 64 (3–4): 195–7. doi:10.1159/000133573. PMID8404035.
DeCastro R, Zhang Y, Guo H, et al. (1996). "Human keratinocytes express EMMPRIN, an extracellular matrix metalloproteinase inducer". J. Invest. Dermatol. 106 (6): 1260–5. doi:10.1111/1523-1747.ep12348959. PMID8752667.
Spring FA, Holmes CH, Simpson KL, et al. (1997). "The Oka blood group antigen is a marker for the M6 leukocyte activation antigen, the human homolog of OX-47 antigen, basigin and neurothelin, an immunoglobulin superfamily molecule that is widely expressed in human cells and tissues". Eur. J. Immunol. 27 (4): 891–7. doi:10.1002/eji.1830270414. PMID9130641.
Berditchevski F, Chang S, Bodorova J, Hemler ME (1997). "Generation of monoclonal antibodies to integrin-associated proteins. Evidence that alpha3beta1 complexes with EMMPRIN/basigin/OX47/M6". J. Biol. Chem. 272 (46): 29174–80. doi:10.1074/jbc.272.46.29174. PMID9360995.
Guo H, Majmudar G, Jensen TC, et al. (1998). "Characterization of the gene for human EMMPRIN, a tumor cell surface inducer of matrix metalloproteinases". Gene. 220 (1–2): 99–108. doi:10.1016/S0378-1119(98)00400-4. PMID9767135.
Guo H, Li R, Zucker S, Toole BP (2000). "EMMPRIN (CD147), an inducer of matrix metalloproteinase synthesis, also binds interstitial collagenase to the tumor cell surface". Cancer Res. 60 (4): 888–91. PMID10706100.
Yurchenko V, O'Connor M, Dai WW, et al. (2001). "CD147 is a signaling receptor for cyclophilin B". Biochem. Biophys. Res. Commun. 288 (4): 786–8. doi:10.1006/bbrc.2001.5847. PMID11688976.
Yurchenko V, Zybarth G, O'Connor M, et al. (2002). "Active site residues of cyclophilin A are crucial for its signaling activity via CD147". J. Biol. Chem. 277 (25): 22959–65. doi:10.1074/jbc.M201593200. PMID11943775.
Major TC, Liang L, Lu X, et al. (2002). "Extracellular matrix metalloproteinase inducer (EMMPRIN) is induced upon monocyte differentiation and is expressed in human atheroma". Arterioscler. Thromb. Vasc. Biol. 22 (7): 1200–7. doi:10.1161/01.ATV.0000021411.53577.1C. PMID12117738.
Taylor PM, Woodfield RJ, Hodgkin MN, et al. (2002). "Breast cancer cell-derived EMMPRIN stimulates fibroblast MMP2 release through a phospholipase A(2) and 5-lipoxygenase catalyzed pathway". Oncogene. 21 (37): 5765–72. doi:10.1038/sj.onc.1205702. PMID12173047.
Thorns C, Feller AC, Merz H (2002). "EMMPRIN (CD 174) is expressed in Hodgkin's lymphoma and anaplastic large cell lymphoma. An immunohistochemical study of 60 cases". Anticancer Res. 22 (4): 1983–6. PMID12174874.