Basigin

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Basigin (Ok blood group)
Identifiers
Symbol(s) BSG; 5F7; CD147; EMMPRIN; M6; OK; TCSF
External IDs OMIM: 109480 MGI88208 Homologene1308
RNA expression pattern

File:PBB GE BSG 208677 s at tn.png

More reference expression data

Orthologs
Human Mouse
Entrez 682 12215
Ensembl ENSG00000172270 ENSMUSG00000023175
Uniprot P35613 O55107
Refseq NM_001728 (mRNA)
NP_001719 (protein)
NM_001077184 (mRNA)
NP_001070652 (protein)
Location Chr 19: 0.46 - 0.53 Mb Chr 10: 79.11 - 79.12 Mb
Pubmed search [1] [2]

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Editor-In-Chief: C. Michael Gibson, M.S., M.D. [3]


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).[1][2]

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][3]

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 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.[4][5][6] 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]

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. PMID 16476049. 
  3. "Entrez Gene: BSG basigin (Ok blood group)". 
  4. 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. PMID 11943775. 
  5. 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. PMID 11688976. 
  6. 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. PMID 9360995. 

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. PMID 15711733. doi:10.1267/THRO05020199. 
  • 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. 
  • 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. 
  • 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. 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. 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. 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. 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. 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. 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. PMID 10921872. doi:10.1093/emboj/19.15.3896. 
  • 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. PMID 11688976. doi:10.1006/bbrc.2001.5847. 
  • 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. PMID 11943775. doi:10.1074/jbc.M201593200. 
  • 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. PMID 11992541. doi:10.1002/ijc.10390. 
  • 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. 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. PMID 12173047. doi:10.1038/sj.onc.1205702. 
  • 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. PMID 12477932. doi:10.1073/pnas.242603899. 
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