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'''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 ''BSG'' [[gene]].<ref>{{cite journal |vauthors=Kasinrerk W, Fiebiger E, Stefanová I, Baumruker T, Knapp W, Stockinger H |title=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 |journal=J Immunol |volume=149 |issue=3 |pages=847–54 |year=1992 |pmid=1634773}}</ref><ref name = yurch>{{cite journal |vauthors=Yurchenko V, Constant S, Bukrinsky M |title=Dealing with the family: CD147 interactions with cyclophilins |journal=Immunology |volume=117 |issue=3 |pages=301–9 |year=2006 |pmid=16476049 |doi=10.1111/j.1365-2567.2005.02316.x |pmc=1782239}}</ref><ref name = "Miyauchi_1992">{{cite journal | vauthors=Miyauchi T, Masuzawa Y, Muramatsu T |title=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 |journal=J. Biochem. |volume=110 |issue= 5 |pages= 770–4 |year= 1992 |pmid= 1783610 |doi=  }}</ref> 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''.<ref name="pmid22080952" />
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{{GNF_Protein_box
| image = 
| image_source = 
| PDB =
| Name = Basigin (Ok blood group)
| HGNCid = 1116
| Symbol = BSG
| AltSymbols =; 5F7; CD147; EMMPRIN; M6; OK; TCSF
| OMIM = 109480
| ECnumber =
| Homologene = 1308
| MGIid = 88208
| GeneAtlas_image1 = PBB_GE_BSG_208677_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004871 |text = signal transducer activity}} {{GNF_GO|id=GO:0005529 |text = sugar binding}} {{GNF_GO|id=GO:0005537 |text = mannose binding}}
| Component = {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0007166 |text = cell surface receptor linked signal transduction}}  
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 682
    | Hs_Ensembl = ENSG00000172270
    | Hs_RefseqProtein = NP_001719
    | Hs_RefseqmRNA = NM_001728
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 19
    | Hs_GenLoc_start = 462896
    | Hs_GenLoc_end = 534492
    | Hs_Uniprot = P35613
    | Mm_EntrezGene = 12215
    | Mm_Ensembl = ENSMUSG00000023175
    | Mm_RefseqmRNA = NM_001077184
    | Mm_RefseqProtein = NP_001070652
    | Mm_GenLoc_db =   
    | Mm_GenLoc_chr = 10
    | Mm_GenLoc_start = 79107635
    | Mm_GenLoc_end = 79115097
    | Mm_Uniprot = O55107
  }}
}}
{{SI}}
{{CMG}}


==Function==
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).<ref>{{cite web | title = Entrez Gene: BSG basigin (Ok blood group)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=682| accessdate = }}</ref><ref name = "Kanekura_1991">{{cite journal  | vauthors=Kanekura T, Chen X, Kanzaki T |title=Basigin (CD147) is expressed on melanoma cells and induces tumor cell invasion by stimulating production of matrix metalloproteinases by fibroblasts |journal=Int. J. Cancer |volume=99 |issue= 4 |pages= 520–8 |year= 2002 |pmid= 11992541 |doi= 10.1002/ijc.10390 }}</ref>


It has a variety of functions. In addition to its metalloproteinase-inducing ability, basigin also regulates several distinct functions, such as [[spermatogenesis]], expression of the [[monocarboxylate transporter]] and the responsiveness of [[lymphocyte]]s.<ref name = yurch/>
Basigin is a type I [[Integral membrane protein|integral membrane receptor]] that has many [[ligand]]s, including the [[cyclophilin]] (CyP) proteins Cyp-A and CyP-B and certain [[integrin]]s.<ref>{{cite journal |vauthors=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 |title=Active site residues of cyclophilin A are crucial for its signaling activity via CD147 |journal=J Biol Chem |volume=277 |issue=25 |pages=22959–65 |year=2002 |pmid=11943775 |doi=10.1074/jbc.M201593200}}</ref><ref>{{cite journal |vauthors=Yurchenko V, O'Connor M, Dai W, Guo H, Toole B, Sherry B, Bukrinsky M |title=CD147 is a signaling receptor for cyclophilin B |journal=Biochem Biophys Res Commun |volume=288 |issue=4 |pages=786–8 |year=2001 |pmid=11688976 |doi=10.1006/bbrc.2001.5847}}</ref><ref>{{cite journal |vauthors=Berditchevski F, Chang S, Bodorova J, Hemler M |title=Generation of monoclonal antibodies to integrin-associated proteins. Evidence that alpha3beta1 complexes with EMMPRIN/basigin/OX47/M6 |journal=J Biol Chem |volume=272 |issue=46 |pages=29174–80 |year=1997 |pmid=9360995 |doi=10.1074/jbc.272.46.29174}}</ref> It is expressed by many cell types, including [[epithelial cell]]s, [[endothelial cell]]s and [[leukocyte]]s. The human basigin protein contains 269 amino acids that form two heavily [[glycosylation|glycosylated]] [[immunoglobulin domain|C2 type immunoglobulin-like domains]] at the N-terminal extracellular portion. A second form of basigin has also been characterized that contains one additional immunoglobulin-like domain in its extracellular portion.<ref name = yurch/>


'''Basigin''' is a member of the [[immunoglobulin superfamily]] that is also known as EMMPRIN, short for ''extracellular matrix metalloproteinase inducer'', and recently has been designated '''CD147''' ([[cluster of differentiation]] 147).<ref>{{cite journal |author=Kasinrerk W, Fiebiger E, Stefanová I, Baumruker T, Knapp W, Stockinger H |title=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 |journal=J Immunol |volume=149 |issue=3 |pages=847-54 |year=1992 |pmid=1634773}}</ref><ref name = yurch>{{cite journal |author=Yurchenko V, Constant S, Bukrinsky M |title=Dealing with the family: CD147 interactions with cyclophilins |journal=Immunology |volume=117 |issue=3 |pages=301-9 |year=2006 |pmid=16476049}}</ref>
==Interactions==
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Basigin has been shown to [[Protein-protein interaction|interact]] with [[Ubiquitin C]].<ref name=pmid18689982>{{cite journal |last=Wang |first=Wen-Juan |author2=Li Qing-Quan |author3=Xu Jing-Da |author4=Cao Xi-Xi |author5=Li Hai-Xia |author6=Tang Feng |author7=Chen Qi |author8=Yang Jin-Ming |author9=Xu Zu-De |author10=Liu Xiu-Ping  |year=2008|title=Interaction between CD147 and P-glycoprotein and their regulation by ubiquitination in breast cancer cells |journal=Chemotherapy |volume=54 |issue=4 |pages=291–301 |publisher= |location = Switzerland| pmid = 18689982 |doi = 10.1159/000151225 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref>
{{PBB_Summary
| section_title =  
| summary_text = 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).[supplied by OMIM]<ref>{{cite web | title = Entrez Gene: BSG basigin (Ok blood group)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=682| accessdate = }}</ref>
}}
This protein is a determinant for the Ok blood group system.


It has a variety of functions. In addition to its metalloproteinase-inducing ability, basigin also regulates several distinct functions, such as [[spermatogenesis]], expression of the monocarboxylate transporter and the responsiveness of [[lymphocyte]]s.<ref name = yurch/>
Basigin has been shown to form a complex with [[monocarboxylate transporter]]s 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.<ref name=pmid12601063 >{{cite journal |author=W.J. Philip |author2=J.D. Ochrietor |author3=C. Rudoy |author4=T. Muramatsu |author5=P.J. Linser|year=2003|title=Loss of MCT1, MCT3, and MCT4 expression in the retinal pigment epithelium and neural retina of the 5A11/basigin-null mouse |journal=Invest. Ophthalmol. Vis. Sci.|volume=44|issue=3 |pages=1305–1311 |publisher= |location = United States| pmid = 12601063 |doi = 10.1167/iovs.02-0552| bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref>


Basigin is a type I [[Integral membrane protein|integral membrane receptor]] that has many [[ligand]]s, including the [[cyclophilin]] (CyP) proteins Cyp-A and CyP-B and certain [[integrin]]s.<ref>{{cite journal |author=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 |title=Active site residues of cyclophilin A are crucial for its signaling activity via CD147 |journal=J Biol Chem |volume=277 |issue=25 |pages=22959-65 |year=2002 |pmid=11943775}}</ref><ref>{{cite journal |author=Yurchenko V, O'Connor M, Dai W, Guo H, Toole B, Sherry B, Bukrinsky M |title=CD147 is a signaling receptor for cyclophilin B |journal=Biochem Biophys Res Commun |volume=288 |issue=4 |pages=786-8 |year=2001 |pmid=11688976}}</ref><ref>{{cite journal |author=Berditchevski F, Chang S, Bodorova J, Hemler M |title=Generation of monoclonal antibodies to integrin-associated proteins. Evidence that alpha3beta1 complexes with EMMPRIN/basigin/OX47/M6 |journal=J Biol Chem |volume=272 |issue=46 |pages=29174-80 |year=1997 |pmid=9360995}}</ref> It is expressed by many cell types, including [[epithelial cell]]s, [[endothelial cell]]s and [[leukocyte]]s. The human basigin protein contains 269 amino acids that form two heavily [[glycosylation|glycosylated]] [[immunoglobulin fold|C2 type immunoglobulin-like domains]] at the N-terminal extracellular portion. A second form of basigin has also been characterized that contains one additional immunoglobulin-like domain in its extracellular portion.<ref name = yurch/>
==Role in malaria==
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.<ref name="pmid22080952">{{cite journal | vauthors = Crosnier C, Bustamante LY, Bartholdson SJ, Bei AK, Theron M, Uchikawa M, Mboup S, Ndir O, Kwiatkowski DP, Duraisingh MT, Rayner JC, Wright GJ | title = Basigin is a receptor essential for erythrocyte invasion by ''Plasmodium falciparum'' | journal = Nature | volume = 480| issue = 7378| pages = 534–7|date=November 2011 | pmid = 22080952 | doi = 10.1038/nature10606 | pmc=3245779}}</ref> Basigin is bound by the PfRh5 protein on the surface of the malaria parasite.


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal  | author=Muramatsu T, Miyauchi T |title=Basigin (CD147): a multifunctional transmembrane protein involved in reproduction, neural function, inflammation and tumor invasion. |journal=Histol. Histopathol. |volume=18 |issue= 3 |pages= 981-7 |year= 2004 |pmid= 12792908 |doi=  }}
*{{cite journal  | vauthors=Muramatsu T, Miyauchi T |title=Basigin (CD147): a multifunctional transmembrane protein involved in reproduction, neural function, inflammation and tumor invasion |journal=Histol. Histopathol. |volume=18 |issue= 3 |pages= 981–7 |year= 2004 |pmid= 12792908 |doi=  }}
*{{cite journal  | author=Yan L, Zucker S, Toole BP |title=Roles of the multifunctional glycoprotein, emmprin (basigin; CD147), in tumour progression. |journal=Thromb. Haemost. |volume=93 |issue= 2 |pages= 199-204 |year= 2005 |pmid= 15711733 |doi= 10.1267/THRO05020199 }}
*{{cite journal  | vauthors=Yan L, Zucker S, Toole BP |title=Roles of the multifunctional glycoprotein, emmprin (basigin; CD147), in tumour progression |journal=Thromb. Haemost. |volume=93 |issue= 2 |pages= 199–204 |year= 2005 |pmid= 15711733 |doi= 10.1160/TH04-08-0536 }}
*{{cite journal  | author=Kasinrerk W, Fiebiger E, Stefanová I, ''et al.'' |title=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. |journal=J. Immunol. |volume=149 |issue= 3 |pages= 847-54 |year= 1992 |pmid= 1634773 |doi=  }}
*{{cite journal  | vauthors=Kasinrerk W, Fiebiger E, Stefanová I |title=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 |journal=J. Immunol. |volume=149 |issue= 3 |pages= 847–54 |year= 1992 |pmid= 1634773 |doi=  |display-authors=etal}}
*{{cite journal  | author=Miyauchi T, Masuzawa Y, Muramatsu T |title=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. |journal=J. Biochem. |volume=110 |issue= 5 |pages= 770-4 |year= 1992 |pmid= 1783610 |doi= }}
*{{cite journal  | vauthors=Nabeshima K, Lane WS, Biswas C |title=Partial sequencing and characterization of the tumor cell-derived collagenase stimulatory factor |journal=Arch. Biochem. Biophys. |volume=285 |issue= 1 |pages= 90–6 |year= 1991 |pmid= 1846736 |doi=10.1016/0003-9861(91)90332-D  }}
*{{cite journal  | author=Nabeshima K, Lane WS, Biswas C |title=Partial sequencing and characterization of the tumor cell-derived collagenase stimulatory factor. |journal=Arch. Biochem. Biophys. |volume=285 |issue= 1 |pages= 90-6 |year= 1991 |pmid= 1846736 |doi=  }}
*{{cite journal  | vauthors=Biswas C, Zhang Y, DeCastro R |title=The human tumor cell-derived collagenase stimulatory factor (renamed EMMPRIN) is a member of the immunoglobulin superfamily |journal=Cancer Res. |volume=55 |issue= 2 |pages= 434–9 |year= 1995 |pmid= 7812975 |doi=  |display-authors=etal}}
*{{cite journal  | author=Biswas C, Zhang Y, DeCastro R, ''et al.'' |title=The human tumor cell-derived collagenase stimulatory factor (renamed EMMPRIN) is a member of the immunoglobulin superfamily. |journal=Cancer Res. |volume=55 |issue= 2 |pages= 434-9 |year= 1995 |pmid= 7812975 |doi=  }}
*{{cite journal  | vauthors=Kaname T, Miyauchi T, Kuwano A |title=Mapping basigin (BSG), a member of the immunoglobulin superfamily, to 19p13.3 |journal=Cytogenet. Cell Genet. |volume=64 |issue= 3–4 |pages= 195–7 |year= 1993 |pmid= 8404035 |doi=10.1159/000133573 |display-authors=etal}}
*{{cite journal  | author=Kaname T, Miyauchi T, Kuwano A, ''et al.'' |title=Mapping basigin (BSG), a member of the immunoglobulin superfamily, to 19p13.3. |journal=Cytogenet. Cell Genet. |volume=64 |issue= 3-4 |pages= 195-7 |year= 1993 |pmid= 8404035 |doi=  }}
*{{cite journal  | vauthors=DeCastro R, Zhang Y, Guo H |title=Human keratinocytes express EMMPRIN, an extracellular matrix metalloproteinase inducer |journal=J. Invest. Dermatol. |volume=106 |issue= 6 |pages= 1260–5 |year= 1996 |pmid= 8752667 |doi=10.1111/1523-1747.ep12348959 |display-authors=etal}}
*{{cite journal  | author=DeCastro R, Zhang Y, Guo H, ''et al.'' |title=Human keratinocytes express EMMPRIN, an extracellular matrix metalloproteinase inducer. |journal=J. Invest. Dermatol. |volume=106 |issue= 6 |pages= 1260-5 |year= 1996 |pmid= 8752667 |doi=  }}
*{{cite journal  | vauthors=Spring FA, Holmes CH, Simpson KL |title=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 |journal=Eur. J. Immunol. |volume=27 |issue= 4 |pages= 891–7 |year= 1997 |pmid= 9130641 |doi=10.1002/eji.1830270414 |display-authors=etal}}
*{{cite journal  | author=Spring FA, Holmes CH, Simpson KL, ''et al.'' |title=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. |journal=Eur. J. Immunol. |volume=27 |issue= 4 |pages= 891-7 |year= 1997 |pmid= 9130641 |doi= }}
*{{cite journal  | vauthors=Berditchevski F, Chang S, Bodorova J, Hemler ME |title=Generation of monoclonal antibodies to integrin-associated proteins. Evidence that alpha3beta1 complexes with EMMPRIN/basigin/OX47/M6 |journal=J. Biol. Chem. |volume=272 |issue= 46 |pages= 29174–80 |year= 1997 |pmid= 9360995 |doi=10.1074/jbc.272.46.29174  }}
*{{cite journal  | author=Berditchevski F, Chang S, Bodorova J, Hemler ME |title=Generation of monoclonal antibodies to integrin-associated proteins. Evidence that alpha3beta1 complexes with EMMPRIN/basigin/OX47/M6. |journal=J. Biol. Chem. |volume=272 |issue= 46 |pages= 29174-80 |year= 1997 |pmid= 9360995 |doi= }}
*{{cite journal  | vauthors=Guo H, Majmudar G, Jensen TC |title=Characterization of the gene for human EMMPRIN, a tumor cell surface inducer of matrix metalloproteinases |journal=Gene |volume=220 |issue= 1–2 |pages= 99–108 |year= 1998 |pmid= 9767135 |doi=10.1016/S0378-1119(98)00400-4  |display-authors=etal}}
*{{cite journal  | author=Guo H, Majmudar G, Jensen TC, ''et al.'' |title=Characterization of the gene for human EMMPRIN, a tumor cell surface inducer of matrix metalloproteinases. |journal=Gene |volume=220 |issue= 1-2 |pages= 99-108 |year= 1998 |pmid= 9767135 |doi=  }}
*{{cite journal  | vauthors=Guo H, Li R, Zucker S, Toole BP |title=EMMPRIN (CD147), an inducer of matrix metalloproteinase synthesis, also binds interstitial collagenase to the tumor cell surface |journal=Cancer Res. |volume=60 |issue= 4 |pages= 888–91 |year= 2000 |pmid= 10706100 |doi=  }}
*{{cite journal  | author=Guo H, Li R, Zucker S, Toole BP |title=EMMPRIN (CD147), an inducer of matrix metalloproteinase synthesis, also binds interstitial collagenase to the tumor cell surface. |journal=Cancer Res. |volume=60 |issue= 4 |pages= 888-91 |year= 2000 |pmid= 10706100 |doi= }}
*{{cite journal  | vauthors=Kirk P, Wilson MC, Heddle C |title=CD147 is tightly associated with lactate transporters MCT1 and MCT4 and facilitates their cell surface expression |journal=EMBO J. |volume=19 |issue= 15 |pages= 3896–904 |year= 2000 |pmid= 10921872 |doi= 10.1093/emboj/19.15.3896  | pmc=306613 |display-authors=etal}}
*{{cite journal  | author=Kirk P, Wilson MC, Heddle C, ''et al.'' |title=CD147 is tightly associated with lactate transporters MCT1 and MCT4 and facilitates their cell surface expression. |journal=EMBO J. |volume=19 |issue= 15 |pages= 3896-904 |year= 2000 |pmid= 10921872 |doi= 10.1093/emboj/19.15.3896 }}
*{{cite journal  | vauthors=Yurchenko V, O'Connor M, Dai WW |title=CD147 is a signaling receptor for cyclophilin B |journal=Biochem. Biophys. Res. Commun. |volume=288 |issue= 4 |pages= 786–8 |year= 2001 |pmid= 11688976 |doi= 10.1006/bbrc.2001.5847 |display-authors=etal}}
*{{cite journal  | author=Yurchenko V, O'Connor M, Dai WW, ''et al.'' |title=CD147 is a signaling receptor for cyclophilin B. |journal=Biochem. Biophys. Res. Commun. |volume=288 |issue= 4 |pages= 786-8 |year= 2001 |pmid= 11688976 |doi= 10.1006/bbrc.2001.5847 }}
*{{cite journal  | vauthors=Yurchenko V, Zybarth G, O'Connor M |title=Active site residues of cyclophilin A are crucial for its signaling activity via CD147 |journal=J. Biol. Chem. |volume=277 |issue= 25 |pages= 22959–65 |year= 2002 |pmid= 11943775 |doi= 10.1074/jbc.M201593200 |display-authors=etal}}
*{{cite journal  | author=Yurchenko V, Zybarth G, O'Connor M, ''et al.'' |title=Active site residues of cyclophilin A are crucial for its signaling activity via CD147. |journal=J. Biol. Chem. |volume=277 |issue= 25 |pages= 22959-65 |year= 2002 |pmid= 11943775 |doi= 10.1074/jbc.M201593200 }}
*{{cite journal  | vauthors=Major TC, Liang L, Lu X |title=Extracellular matrix metalloproteinase inducer (EMMPRIN) is induced upon monocyte differentiation and is expressed in human atheroma |journal=Arterioscler. Thromb. Vasc. Biol. |volume=22 |issue= 7 |pages= 1200–7 |year= 2002 |pmid= 12117738 |doi=10.1161/01.ATV.0000021411.53577.1C  |display-authors=etal}}
*{{cite journal  | author=Kanekura T, Chen X, Kanzaki T |title=Basigin (CD147) is expressed on melanoma cells and induces tumor cell invasion by stimulating production of matrix metalloproteinases by fibroblasts. |journal=Int. J. Cancer |volume=99 |issue= 4 |pages= 520-8 |year= 2002 |pmid= 11992541 |doi= 10.1002/ijc.10390 }}
*{{cite journal  | vauthors=Taylor PM, Woodfield RJ, Hodgkin MN |title=Breast cancer cell-derived EMMPRIN stimulates fibroblast MMP2 release through a phospholipase A(2) and 5-lipoxygenase catalyzed pathway |journal=Oncogene |volume=21 |issue= 37 |pages= 5765–72 |date= 2002 |pmid= 12173047 |doi= 10.1038/sj.onc.1205702 |display-authors=etal}}
*{{cite journal  | author=Major TC, Liang L, Lu X, ''et al.'' |title=Extracellular matrix metalloproteinase inducer (EMMPRIN) is induced upon monocyte differentiation and is expressed in human atheroma. |journal=Arterioscler. Thromb. Vasc. Biol. |volume=22 |issue= 7 |pages= 1200-7 |year= 2002 |pmid= 12117738 |doi=  }}
*{{cite journal  | vauthors=Thorns C, Feller AC, Merz H |title=EMMPRIN (CD 174) is expressed in Hodgkin's lymphoma and anaplastic large cell lymphoma. An immunohistochemical study of 60 cases |journal=Anticancer Res. |volume=22 |issue= 4 |pages= 1983–6 |year= 2002 |pmid= 12174874 |doi=  }}
*{{cite journal  | author=Taylor PM, Woodfield RJ, Hodgkin MN, ''et al.'' |title=Breast cancer cell-derived EMMPRIN stimulates fibroblast MMP2 release through a phospholipase A(2) and 5-lipoxygenase catalyzed pathway. |journal=Oncogene |volume=21 |issue= 37 |pages= 5765-72 |year= 2002 |pmid= 12173047 |doi= 10.1038/sj.onc.1205702 }}
*{{cite journal  | vauthors=Strausberg RL, Feingold EA, Grouse LH |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 |display-authors=etal}}
*{{cite journal | author=Thorns C, Feller AC, Merz H |title=EMMPRIN (CD 174) is expressed in Hodgkin's lymphoma and anaplastic large cell lymphoma. An immunohistochemical study of 60 cases. |journal=Anticancer Res. |volume=22 |issue= 4 |pages= 1983-6 |year= 2002 |pmid= 12174874 |doi=  }}
 
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
}}
}}
{{refend}}
{{refend}}
==External links==
==External links==
 
* {{UCSC gene info|BSG}}
* [http://www.ncbi.nlm.nih.gov/projects/mhc/xslcgi.fcgi?cmd=bgmut/systems_info&system=ok Ok blood group system at BGMUT] Blood Group Antigen Gene Mutation Database at [[NCBI]], [[NIH]]
* [https://www.ncbi.nlm.nih.gov/projects/mhc/xslcgi.fcgi?cmd=bgmut/systems_info&system=ok Ok blood group system] at [[BGMUT]] Blood Group Antigen Gene Mutation Database at [[National Center for Biotechnology Information|NCBI]], [[NIH]]
 
{{Clusters of differentiation}}
{{Clusters of differentiation}}
{{Complement_system}}
{{Complement_system}}
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[[Category:Complement system]]
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[[Category:Hematology]]
[[Category:Hematology]]
[[Category:Blood antigen systems]]
[[Category:Blood antigen systems]]
[[Category:Clusters of differentiation]]
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Revision as of 22:04, 14 November 2017

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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 BSG gene.[1][2][3] 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.[4]

Function

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).[5][6]

It has a variety of functions. In addition to its metalloproteinase-inducing ability, basigin also regulates several distinct functions, such as spermatogenesis, expression of the monocarboxylate transporter and the responsiveness of lymphocytes.[2] Basigin is a type I integral membrane receptor that has many ligands, including the cyclophilin (CyP) proteins Cyp-A and CyP-B and certain integrins.[7][8][9] It is expressed by many cell types, including epithelial cells, endothelial cells and leukocytes. The human basigin protein contains 269 amino acids that form two heavily glycosylated C2 type immunoglobulin-like domains at the N-terminal extracellular portion. A second form of basigin has also been characterized that contains one additional immunoglobulin-like domain in its extracellular portion.[2]

Interactions

Basigin has been shown to interact with Ubiquitin C.[10]

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.[11]

Role in malaria

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.[4] Basigin is bound by the PfRh5 protein on the surface of the malaria parasite.

References

  1. ↑ 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. PMID 1634773.
  2. ↑ 2.0 2.1 2.2 Yurchenko V, Constant S, Bukrinsky M (2006). "Dealing with the family: CD147 interactions with cyclophilins". Immunology. 117 (3): 301–9. doi:10.1111/j.1365-2567.2005.02316.x. PMC 1782239. PMID 16476049.
  3. ↑ 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. PMID 1783610.
  4. ↑ 4.0 4.1 Crosnier C, Bustamante LY, Bartholdson SJ, Bei AK, Theron M, Uchikawa M, Mboup S, Ndir O, Kwiatkowski DP, Duraisingh MT, Rayner JC, Wright GJ (November 2011). "Basigin is a receptor essential for erythrocyte invasion by Plasmodium falciparum". Nature. 480 (7378): 534–7. doi:10.1038/nature10606. PMC 3245779. PMID 22080952.
  5. ↑ "Entrez Gene: BSG basigin (Ok blood group)".
  6. ↑ 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. PMID 11992541.
  7. ↑ 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. PMID 11943775.
  8. ↑ 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. PMID 11688976.
  9. ↑ 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. PMID 9360995.
  10. ↑ 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. PMID 18689982.
  11. ↑ 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. PMID 12601063.

Further reading

  • 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. PMID 12792908.
  • 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. PMID 15711733.
  • 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. PMID 1634773.
  • 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. PMID 1846736.
  • 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. PMID 7812975.
  • 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. PMID 8404035.
  • 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. PMID 8752667.
  • 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. PMID 9130641.
  • 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. PMID 9360995.
  • 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. PMID 9767135.
  • 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. PMID 10706100.
  • Kirk P, Wilson MC, Heddle C, et al. (2000). "CD147 is tightly associated with lactate transporters MCT1 and MCT4 and facilitates their cell surface expression". EMBO J. 19 (15): 3896–904. doi:10.1093/emboj/19.15.3896. PMC 306613. PMID 10921872.
  • 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. PMID 11688976.
  • 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. PMID 11943775.
  • 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. PMID 12117738.
  • 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. PMID 12173047.
  • 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. PMID 12174874.
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.

External links

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