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Gene Review

BSG  -  basigin (Ok blood group)

Homo sapiens

Synonyms: 5F7, Basigin, CD147, Collagenase stimulatory factor, EMMPRIN, ...
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Disease relevance of BSG


Psychiatry related information on BSG


High impact information on BSG

  • Peptides were aligned with the amino acid sequence of the entire M6 protein predicted by the DNA sequence of the M6 gene [8].
  • Competitive inhibition studies using peptides synthesized on the basis of peptide and DNA sequences, in concert with selective blocking of amino acid residues, allowed for the further identification and placement of these crossreactive epitopes within the M6 molecule [8].
  • Conversion of an M- group A streptococcus to M+ by transfer of a plasmid containing an M6 gene [9].
  • In heart cells, CD147 and MCT1 co-localize, concentrating at the t-tubular and intercalated disk regions [10].
  • We conclude that CD147 facilitates proper expression of MCT1 and MCT4 at the cell surface, where they remain tightly bound to each other [10].

Chemical compound and disease context of BSG


Biological context of BSG


Anatomical context of BSG


Associations of BSG with chemical compounds

  • Regulation of CD147 cell surface expression: involvement of the proline residue in the CD147 transmembrane domain [21].
  • Previously, we demonstrated that cell surface expression of CD147 is sensitive to cyclophilin-binding drug cyclosporin A, suggesting involvement of a cyclophilin in the regulation of intracellular transport of CD147 [2].
  • The production and glycosylation of EMMPRIN in the stromal cells were augmented by progesterone at the posttranscriptional and posttranslational stages, respectively [19].
  • EMMPRIN mRNA levels varied throughout the menstrual cycle in parallel with the cyclic changes in estradiol [22].
  • In the parenchymal epithelia of kidney, thyroid, and liver, MCT/CD147 heterocomplexes are localized in the basolateral membrane where they transport lactate out of or into the cell depending on metabolic conditions [23].

Physical interactions of BSG

  • Presentation of MMP-1 complexed to EMMPRIN at the tumor cell surface may be important in modifying the tumor cell pericellular matrix to promote invasion [20].
  • Solution binding experiments demonstrated that the transmembrane domain was both necessary and sufficient for CD147 binding to cyclophilin A (CypA) [21].

Co-localisations of BSG


Regulatory relationships of BSG


Other interactions of BSG

  • EMMPRIN (CD147), an inducer of matrix metalloproteinase synthesis, also binds interstitial collagenase to the tumor cell surface [20].
  • Thus, the MT1-MMP-dependent cleavage eliminates the functional N-terminal domain of EMMPRIN from the cell surface, which is expected to down-regulate its function [18].
  • These results suggest that Cyp60 plays an important role in the translocation of CD147 to the cell surface [2].
  • Overexpression of caveolin-1 caused a specific decrease in clustering of cell surface CD147, as detected by "cluster specific" mAb M6/13 [24].
  • MMP-3 protein (308%) and EMMPRIN mRNA and protein were also upregulated (171% and 200%) [27].

Analytical, diagnostic and therapeutic context of BSG


  1. Regulation of MMP-1 and MMP-2 production through CD147/extracellular matrix metalloproteinase inducer interactions. Sun, J., Hemler, M.E. Cancer Res. (2001) [Pubmed]
  2. Cell surface expression of CD147/EMMPRIN is regulated by cyclophilin 60. Pushkarsky, T., Yurchenko, V., Vanpouille, C., Brichacek, B., Vaisman, I., Hatakeyama, S., Nakayama, K.I., Sherry, B., Bukrinsky, M.I. J. Biol. Chem. (2005) [Pubmed]
  3. Basigin (CD147) is expressed on melanoma cells and induces tumor cell invasion by stimulating production of matrix metalloproteinases by fibroblasts. Kanekura, T., Chen, X., Kanzaki, T. Int. J. Cancer (2002) [Pubmed]
  4. EMMPRIN-induced MMP-2 activation cascade in human cervical squamous cell carcinoma. Sier, C.F., Zuidwijk, K., Zijlmans, H.J., Hanemaaijer, R., Mulder-Stapel, A.A., Prins, F.A., Dreef, E.J., Kenter, G.G., Fleuren, G.J., Gorter, A. Int. J. Cancer (2006) [Pubmed]
  5. Proteome analysis of multidrug resistance of human oral squamous carcinoma cells using CD147 silencing. Kuang, Y.H., Chen, X., Su, J., Wu, L.S., Li, J., Chang, J., Qiu, Y., Chen, Z.S., Kanekura, T. J. Proteome Res. (2008) [Pubmed]
  6. EMMPRIN expression as a prognostic factor in radiotherapy of cervical cancer. Ju, X.Z., Yang, J.M., Zhou, X.Y., Li, Z.T., Wu, X.H. Clin. Cancer Res. (2008) [Pubmed]
  7. CD147 is a regulatory subunit of the gamma-secretase complex in Alzheimer's disease amyloid beta-peptide production. Zhou, S., Zhou, H., Walian, P.J., Jap, B.K. Proc. Natl. Acad. Sci. U.S.A. (2005) [Pubmed]
  8. Immunochemical localization and amino acid sequences of crossreactive epitopes within the group A streptococcal M6 protein. Jones, K.F., Khan, S.A., Erickson, B.W., Hollingshead, S.K., Scott, J.R., Fischetti, V.A. J. Exp. Med. (1986) [Pubmed]
  9. Conversion of an M- group A streptococcus to M+ by transfer of a plasmid containing an M6 gene. Scott, J.R., Guenthner, P.C., Malone, L.M., Fischetti, V.A. J. Exp. Med. (1986) [Pubmed]
  10. CD147 is tightly associated with lactate transporters MCT1 and MCT4 and facilitates their cell surface expression. Kirk, P., Wilson, M.C., Heddle, C., Brown, M.H., Barclay, A.N., Halestrap, A.P. EMBO J. (2000) [Pubmed]
  11. Clinicopathological significance of expression of paxillin, syndecan-1 and EMMPRIN in hepatocellular carcinoma. Li, H.G., Xie, D.R., Shen, X.M., Li, H.H., Zeng, H., Zeng, Y.J. World J. Gastroenterol. (2005) [Pubmed]
  12. CD147 facilitates HIV-1 infection by interacting with virus-associated cyclophilin A. Pushkarsky, T., Zybarth, G., Dubrovsky, L., Yurchenko, V., Tang, H., Guo, H., Toole, B., Sherry, B., Bukrinsky, M. Proc. Natl. Acad. Sci. U.S.A. (2001) [Pubmed]
  13. PEA3 is the second Ets family transcription factor involved in tumor progression in ovarian carcinoma. Davidson, B., Goldberg, I., Gotlieb, W.H., Kopolovic, J., Ben-Baruch, G., Reich, R. Clin. Cancer Res. (2003) [Pubmed]
  14. Oxidized low-density lipoproteins stimulate extracellular matrix metalloproteinase Inducer (EMMPRIN) release by coronary smooth muscle cells. Haug, C., Lenz, C., Díaz, F., Bachem, M.G. Arterioscler. Thromb. Vasc. Biol. (2004) [Pubmed]
  15. High incidence of EMMPRIN expression in human tumors. Riethdorf, S., Reimers, N., Assmann, V., Kornfeld, J.W., Terracciano, L., Sauter, G., Pantel, K. Int. J. Cancer (2006) [Pubmed]
  16. Overexpression of HAb18G/CD147 promotes invasion and metastasis via alpha3beta1 integrin mediated FAK-paxillin and FAK-PI3K-Ca2+ pathways. Tang, J., Wu, Y.M., Zhao, P., Yang, X.M., Jiang, J.L., Chen, Z.N. Cell. Mol. Life Sci. (2008) [Pubmed]
  17. Differential expression of extracellular matrix metalloproteinase inducer (CD147) in normal and ulcerated corneas: role in epithelio-stromal interactions and matrix metalloproteinase induction. Gabison, E.E., Mourah, S., Steinfels, E., Yan, L., Hoang-Xuan, T., Watsky, M.A., De Wever, B., Calvo, F., Mauviel, A., Menashi, S. Am. J. Pathol. (2005) [Pubmed]
  18. Membrane Type 1 Matrix Metalloproteinase (MT1-MMP/MMP-14) Cleaves and Releases a 22-kDa Extracellular Matrix Metalloproteinase Inducer (EMMPRIN) Fragment from Tumor Cells. Egawa, N., Koshikawa, N., Tomari, T., Nabeshima, K., Isobe, T., Seiki, M. J. Biol. Chem. (2006) [Pubmed]
  19. Identification and characterization of extracellular matrix metalloproteinase inducer in human endometrium during the menstrual cycle in vivo and in vitro. Noguchi, Y., Sato, T., Hirata, M., Hara, T., Ohama, K., Ito, A. J. Clin. Endocrinol. Metab. (2003) [Pubmed]
  20. EMMPRIN (CD147), an inducer of matrix metalloproteinase synthesis, also binds interstitial collagenase to the tumor cell surface. Guo, H., Li, R., Zucker, S., Toole, B.P. Cancer Res. (2000) [Pubmed]
  21. Regulation of CD147 cell surface expression: involvement of the proline residue in the CD147 transmembrane domain. Yurchenko, V., Pushkarsky, T., Li, J.H., Dai, W.W., Sherry, B., Bukrinsky, M. J. Biol. Chem. (2005) [Pubmed]
  22. Extracellular matrix metalloproteinase inducer regulates metalloproteinases in human uterine endometrium. Braundmeier, A.G., Fazleabas, A.T., Lessey, B.A., Guo, H., Toole, B.P., Nowak, R.A. J. Clin. Endocrinol. Metab. (2006) [Pubmed]
  23. Mechanisms regulating tissue-specific polarity of monocarboxylate transporters and their chaperone CD147 in kidney and retinal epithelia. Deora, A.A., Philp, N., Hu, J., Bok, D., Rodriguez-Boulan, E. Proc. Natl. Acad. Sci. U.S.A. (2005) [Pubmed]
  24. Caveolin-1 regulates matrix metalloproteinases-1 induction and CD147/EMMPRIN cell surface clustering. Tang, W., Hemler, M.E. J. Biol. Chem. (2004) [Pubmed]
  25. Extracellular matrix metalloproteinase inducer regulates matrix metalloproteinase activity in cardiovascular cells: implications in acute myocardial infarction. Schmidt, R., Bültmann, A., Ungerer, M., Joghetaei, N., Bülbül, O., Thieme, S., Chavakis, T., Toole, B.P., Gawaz, M., Schömig, A., May, A.E. Circulation (2006) [Pubmed]
  26. Expression of CD147 on monocytes/macrophages in rheumatoid arthritis: its potential role in monocyte accumulation and matrix metalloproteinase production. Zhu, P., Ding, J., Zhou, J., Dong, W.J., Fan, C.M., Chen, Z.N. Arthritis Res. Ther. (2005) [Pubmed]
  27. Regulation of matrix metalloproteinases and their inhibitors in the left ventricular myocardium of patients with aortic stenosis. Fielitz, J., Leuschner, M., Zurbrügg, H.R., Hannack, B., Pregla, R., Hetzer, R., Regitz-Zagrosek, V. J. Mol. Med. (2004) [Pubmed]
  28. Expression of the extracellular matrix metalloproteinase inducer (EMMPRIN) and the matrix metalloproteinase-2 in bronchopulmonary and breast lesions. Caudroy, S., Polette, M., Tournier, J.M., Burlet, H., Toole, B., Zucker, S., Birembaut, P. J. Histochem. Cytochem. (1999) [Pubmed]
  29. Cytokines regulate matrix metalloproteinases in human uterine endometrial fibroblast cells through a mechanism that does not involve increases in extracellular matrix metalloproteinase inducer. Braundmeier, A.G., Nowak, R.A. Am. J. Reprod. Immunol. (2006) [Pubmed]
  30. Overexpression of extracellular matrix metalloproteinase inducer in multidrug resistant cancer cells. Yang, J.M., Xu, Z., Wu, H., Zhu, H., Wu, X., Hait, W.N. Mol. Cancer Res. (2003) [Pubmed]
  31. Matrix metalloproteinase 2 is associated with stable and matrix metalloproteinases 8 and 9 with vulnerable carotid atherosclerotic lesions: a study in human endarterectomy specimen pointing to a role for different extracellular matrix metalloproteinase inducer glycosylation forms. Sluijter, J.P., Pulskens, W.P., Schoneveld, A.H., Velema, E., Strijder, C.F., Moll, F., de Vries, J.P., Verheijen, J., Hanemaaijer, R., de Kleijn, D.P., Pasterkamp, G. Stroke (2006) [Pubmed]
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